Immunoprecipitation (IP) is a common research technique used to precipitate a specific protein (or protein complex) of interest out of a heterogeneous lysate. The concept of precipitating proteins out of solution is often called a "pull-down". There are a variety of methods to achieve immunoprecipitation, the most common of which uses antibodies bound to magnetic or agarose beads. This process can be used to isolate and concentrate a particular protein or complex from a sample containing many thousands of different proteins, and is often used to study protein-protein interactions through Co-IP experiments.
Novus offers a range of support options for IP when you buy a product to help you with your IP experiment including:
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NBP3-38646SS | |||
| BSA Free | NBP3-38646 | |||
| BSA Free | NB100-690SS | |||
| Azide and BSA Free | NBP2-80570 | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB110-57130SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| Azide and BSA Free | NBP2-24863 | |||
| BSA Free | NBP2-24729SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB400-135SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB100-56519SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB600-503SS | |||
| Conjugate | Catalog # | Availability | Size | Price |
|---|---|---|---|---|
| Alkaline Phosphatase | NB600-1502 | |||
| Biotin | NB100-1678 | |||
| DyLight 488 | NBP1-69969 | |||
| FITC | NB100-1771 | |||
| FITC | NB100-1771SS | |||
| HRP | NB600-313 | |||
| Rhodamine | NBP1-97327-500ug | |||
| Texas Red | NB120-6660 | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB100-1770SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB100-106SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB100-904SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB100-104SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB100-56506SS | |||
| Azide and BSA Free | NBP2-33212 | |||
![Simple Western: alpha Tubulin Antibody (DM1A) [NB100-690] - Simple Western lane view shows a specific band for alpha Tubulin in 1.0 mg/ml of HeLa lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system. Alpha tubulin molecular weight: 50 kDa.](http://images.novusbio.com/fullsize/alpha-Tubulin-Antibody-DM1A-Simple-Western-NB100-690-img0023.jpg "Simple Western: alpha Tubulin Antibody (DM1A) [NB100-690] - Simple Western lane view shows a specific band for alpha Tubulin in 1.0 mg/ml of HeLa lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system. Alpha tubulin molecular weight: 50 kDa.")
![Immunohistochemistry: alpha Tubulin Antibody (DM1A) [NB100-690] - Analysis of formalin fixed colon sections. Heat mediated antigen retrieval was performed using sodium citrate buffer for 20 min before incubating with primary antibody at a 0.5ug/ml dilution for 15 min at RT.](http://images.novusbio.com/fullsize/alpha-Tubulin-Antibody-DM1A-Immunohistochemistry-NB100-690-img0028.jpg)
![Immunohistochemistry: alpha Tubulin Antibody (DM1A) [NB100-690] - Analysis of colon tissue. Sections were formalin fixed and embedded with paraffin. Sodium citrate heat mediated antigen retrieval for 20 min. Incubated with primary antibody for 15 min at a 5 ug/ml concentration. Corner image is staining with secondary only.](http://images.novusbio.com/fullsize/alpha-Tubulin-Antibody-DM1A-Immunohistochemistry-NB100-690-img0029.jpg)
![Immunohistochemistry: alpha Tubulin Antibody (DM1A) [NB100-690] - Analysis of formalin fixed paraffin embedded heart sections. Used at a dilution of 1:500.](http://images.novusbio.com/fullsize/alpha-Tubulin-Antibody-DM1A-Immunohistochemistry-NB100-690-img0031.jpg)
![Western Blot: alpha Tubulin Antibody (DM1A) [NB100-690] - Analsis of alpha tubulin in 9 cell lysates. Lane 1. HeLa; Lane 2. JURKAT; Lane 3. COS7; Lane 4. NIH-3T3; Lane 5. PC-12; Lane 6. RAT2; Lane 7. CHO; Lane 8. MDBK; Lane 9. MDCK](http://images.novusbio.com/fullsize/alpha-Tubulin-Antibody-DM1A-Western-Blot-NB100-690-img0032.jpg)
![Flow Cytometry: alpha Tubulin Antibody (DM1A) [NB100-690] - Intracellular flow cytometric staining of 1 x 10^6 CHO (A) and HEK-293 (B) cells using alpha Tubulin antibody (dark blue). Isotype control shown in orange. An antibody concentration of 1 ug/1x10^6 cells was used.](http://images.novusbio.com/fullsize/alpha-Tubulin-Antibody-DM1A-Flow-Cytometry-NB100-690-img0016.jpg)
![Immunomicroscopy: alpha Tubulin Antibody (DM1A) [NB100-690] - Analysis of HeLa cells, green staining is alpha tubulin whereas red is DNA stained with propidium iodide.](http://images.novusbio.com/fullsize/alpha-Tubulin-Antibody-DM1A-Immunomicroscopy-NB100-690-img0037.jpg)
![Western Blot: alpha Tubulin Antibody (DM1A) [NB100-690] - GS treatment increases markers of beiging in 3T3-L1 adipocytes. GS treatment upregulates markers of beiging, including beta-3AR (C) proteins. Data presented as mean +/- SEM from n = 4 replicates per group. * p 0 for sensitive & <0 resistant. (D) Apoptotic H1299 (null p53), A549 (wild type p53), Bm7-shGFP (mutant p53), & Bm7-shTP53 (knock-down p53) cells treated with simvastatin were detected using flow cytometry, *P < 0.05 & **P < 0.01. (E) Apoptotic HCC827-shGFP (mutant p53) & HCC827-shTP53 (knock-down p53) cells treated with simvastatin & cisplatin were detected using flow cytometry, *P < 0.05 & **P < 0.01. (F) Western blots of indicated proteins involved in apoptosis & autophagy in both Bm7 & HCC827 cells with control (shGFP) & p53 knockdown (shTP53) treated with simvastatin is shown. MDM2, murine double minute 2; AKT, serine–threonine kinase; PARP, poly (ADP-ribose) polymerase; mTOR, mammalian target of rapamycin; WT, wild type. Full-length blots/gels are presented in Supplementary Fig. 1. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31892709), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-690_mouse-monoclonal-alpha-tubulin-antibody-dm1a-img-80196-310202415541925.jpg)
![Western Blot: alpha Tubulin Antibody (DM1A) - BSA Free [NB100-690] - Pre-treatment with 0.5 mM sodium arsenite (SA) enhances permissivity in a cell-type-specific manner across reovirus strains. (A) CV-1, HeLa, L929, or HPDE cells were left untreated (no SA) or were treated with 0.5 mM SA for 30 min prior to infection (Pre-SA). Following this, cells were infected with T3D such that ~20% to 50% of cells were infected & at 18 h p.i. cells were fixed & immunostained for μNS & DAPI to visualize viral factories (VFs). The percent of cells containing VFs was quantified ((# of cells containing VFs/total # of cells) × 100) from three independent experiments. The expression level of μNS (B) & μ1 (C) was determined in CV-1, L929, or HeLa cells either left untreated (no SA) or treated with 0.5 mM SA for 30 min (Pre-SA) before infection with T3D at MOI = 1. At 18 h p.i., cells were harvested & the expression level of the indicated proteins was determined by immunoblot. M = mock. Densitometry analysis of the band intensity for μNS & μ1 was adjusted to the matched alpha -tubulin loading control for two independent experiments. Columns represent mean ± SEM. (D) CV-1; (E) L929; or (F) HeLa cells were left untreated (no SA) or were treated with 0.5 mM SA prior to infection (Pre-SA). Cells were then infected with the reovirus strains, T3D, T1L, or T3A, as described in (A). At 18 h p.i., cells were fixed & immunostained for μNS & DAPI to detect VFs. The percent of cells containing VFs was quantified ((# of cells containing VFs/total # of cells) × 100) from at least two independent experiments. * p < 0.05; ** p < 0.01; two-tailed unpaired t test. The error bars indicate S.D. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31216693), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-690_mouse-monoclonal-alpha-tubulin-antibody-dm1a-img-80196-31020241553208.jpg)
![Immunocytochemistry/Immunofluorescence: TRF-2 Antibody [NB110-57130] - HeLa cells were fixed for 10 minutes using 10% formalin and then permeabilized for 5 minutes using 1X TBS + 0.5% Triton X-100. The cells were incubated with antibody at a 1:200 dilution overnight at 4 degrees Celsius and detected with DyLight 488 (Green) at a 1:500 dilution. Alpha tubulin was used as a co-stain at a 1:1000 dilution and detected with Dylight 550 (Red). Nuclei were detected with DAPI (Blue) at 2.0 ug/ml in 1X PBS. Cells were imaged using a 40X objective.](http://images.novusbio.com/fullsize/TRF-2-Antibody-Immunocytochemistry-Immunofluorescence-NB110-57130-img0011.jpg "Immunocytochemistry/Immunofluorescence: TRF-2 Antibody [NB110-57130] - HeLa cells were fixed for 10 minutes using 10% formalin and then permeabilized for 5 minutes using 1X TBS + 0.5% Triton X-100. The cells were incubated with antibody at a 1:200 dilution overnight at 4 degrees Celsius and detected with DyLight 488 (Green) at a 1:500 dilution. Alpha tubulin was used as a co-stain at a 1:1000 dilution and detected with Dylight 550 (Red). Nuclei were detected with DAPI (Blue) at 2.0 ug/ml in 1X PBS. Cells were imaged using a 40X objective.")
![Simple Western: TRF-2 Antibody [NB110-57130] - Lane view shows a specific band for TRF2 in 1.0 mg/mL of HeLa lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system.](http://images.novusbio.com/fullsize/TRF-2-Antibody-Simple-Western-NB110-57130-img0010.jpg)
![Western Blot: TRF-2 Antibody [NB110-57130] - Analysis of HeLa whole cell lysate (A), HeLa nuclear cell lysate (B), k562 cell lysate (C), HepG2 cell lysate (D), NIH/3T3 cell lysate (E), CHO cell lysate (F), PC12 cell lysate (G), and Cos7 cell lysate (H) using antibody at a concentration of 2 ug/mL.](http://images.novusbio.com/fullsize/TRF-2-Antibody-Western-Blot-NB110-57130-img0008.jpg)
![Immunohistochemistry-Paraffin: TRF-2 Antibody [NB110-57130] - Analysis in xenografted human breast cancer tissue using DAB with hematoxylin counterstain.](http://images.novusbio.com/fullsize/TRF-2-Antibody-Immunohistochemistry-Paraffin-NB110-57130-img0007.jpg)
![Immunohistochemistry-Paraffin: TRF-2 Antibody [NB110-57130] - Analysis of FFPE human breast cancer tissue with rabbit polyclonal TRF2 antibody at a dilution of 1:200. The staining was developed with HRP-DAB detection method and the counterstaining was performed using hematoxylin. This TRF2 antibody generated an expected nuclear signal in all the cancer cells and the stromal cells. In the tested section, only a subset of myoepithelial cells showed positivity for this protein.](http://images.novusbio.com/fullsize/TRF-2-Antibody-Immunohistochemistry-Paraffin-NB110-57130-img0013.jpg)
![Immunocytochemistry/Immunofluorescence: TRF-2 Antibody [NB110-57130] - NIH3T3 cells were fixed in 4% paraformaldehyde for 10 minutes and permeabilized in 0.5% Triton X-100 in PBS for 5 minutes. The cells were incubated with anti-TRF-2 Antibody NB110-57130 at 2 ug/ml overnight at 4C and detected with an anti-rabbit Dylight 488 (Green) at a 1:1000 dilution for 60 minutes. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 100X objective and digitally deconvolved.](http://images.novusbio.com/fullsize/TRF-2-Antibody-Immunocytochemistry-Immunofluorescence-NB110-57130-img0016.jpg)
![Flow Cytometry: TRF-2 Antibody [NB110-57130] - An intracellular stain was performed on HeLa cells with TRF-2 Antibody NB110-57130 (blue) and a matched isotype control NBP2-24891 (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 1.0 ug/mL for 30 minutes at room temperature, followed by Rabbit IgG (H+L) Cross-Adsorbed Secondary Antibody, Dylight 550 (SA5-10033, Thermo Fisher).](http://images.novusbio.com/fullsize/TRF-2-Antibody-Flow-Cytometry-NB110-57130-img0017.jpg)
![Chromatin Immunoprecipitation: TRF-2 Antibody [NB110-57130] - Analysis in mouse. Titrated TRF2 antibody to determine concentration required for ChIP experiment. ChIP image submitted by a verified customer review.](http://images.novusbio.com/fullsize/TRF-2-Antibody-Chromatin-Immunoprecipitation-NB110-57130-img0009.jpg)
![<b>Genetic Strategies Validation. </b>Immunocytochemistry/Immunofluorescence: TRF-2 Antibody [NB110-57130] - RNAi-mediated depletion of human separase (ESPL1) induces TIFs. Control scrambled siRNA- (control) and ESPL1 siRNA-treated fibroblasts stained with anti-p53-binding protein 1 (53BP1; green) and anti-TRF2 (red). It is noteworthy that in ESPL1 siRNA-treated cells, 53BP1 signals frequently overlap with TRF2 signals marking the TIFs. Scale bar, 5 um. Image collected and cropped by CiteAb from the following publication (//www.nature.com/doifinder/10.1038/ncomms10405), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/TRF-2-Antibody-Immunocytochemistry-Immunofluorescence-NB110-57130-img0015.jpg)
![Immunohistochemistry-Paraffin: TRF-2 Antibody [NB110-57130] - Analysis of FFPE human breast cancer tissue with rabbit polyclonal TRF2 antibody at 1:200 dilution. The staining was developed with HRP-DAB detection method and the counterstaining was performed using hematoxylin. This TRF2 antibody generated an expected nuclear signal in all the cancer cells and the stromal cells. In the tested section, only a subset of myoepithelial cells showed positivity for this protein.](http://images.novusbio.com/fullsize/TRF-2-Antibody-Immunohistochemistry-Paraffin-NB110-57130-img0012.jpg)
![Flow Cytometry: TRF-2 Antibody [NB110-57130] - An intracellular stain was performed on HeLa cells with TRF-2 Antibody NB110-57130AF488 (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 5 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to Alexa Fluor 488.](http://images.novusbio.com/fullsize/TRF-2-Antibody-Flow-Cytometry-NB110-57130-img0014.jpg)
![Western Blot: TRF-2 Antibody - BSA Free [NB110-57130] - Repressive chromatin induced on p21 promoter in TRF2 dependent way. (A–C) Loss of chromatin activation marks H3K4Me, H3K4Me2 in stable TRF2 expressed HT1080 cells (A); increase in LSD1 occupancy in TRF2 over-expressing HT1080 cells. (B) (Full images are shown in Supplementary Figures S6 & S7); Co-immunoprecipitation of TRF2 with LSD1 (immunoprecipitation with anti-TRF2 antibody followed by immunoblotting with anti-LSD1 or anti-TRF2 antibody) (C); (D) Reverse Co-immunoprecipitation of LSD1 with TRF2 (immunoprecipitation with anti-LSD1 antibody followed by immunoblotting with anti-TRF2 antibody); (E) & reduced occupancy of the repressor complex REST, Co-REST & LSD1 on silencing TRF2 on p21 promoter. Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/s41598-017-11177-1), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-57130_rabbit-polyclonal-trf-2-antibody-31020241528452.jpg)
![Chromatin Immunoprecipitation: TRF-2 Antibody - BSA Free [NB110-57130] - TRF2 occupancy on G4-motif sites on gene promoters within cells.A, telomeric enrichment was tested for TRF2 ChIP samples performed in HT1080 cells. Telomeric signal was normalized to signal from ALU probe. B, TRF2 occupancy at gene promoter sites in HT1080 cells (endogenous TRF2 & TRF2-overexpressed) quantified using ChIP-qRT PCR. TRF2 ChIP/IgG (mock) enrichment was normalized to 1% input; CTCF promoter (which does not harbor a TRF2 peak) was used as negative control; error bars correspond to S.D., & statistical significance was calculated by paired t test (*, p < 0.05; **, p < 0.01). For the TRF2-overexpressed condition (in red), all p values were <0.01. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31575660), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-57130_rabbit-polyclonal-trf-2-antibody-310202415293320.jpg)
![Western Blot: TRF-2 Antibody - BSA Free [NB110-57130] - Repressive chromatin induced on p21 promoter in TRF2 dependent way. (A–C) Loss of chromatin activation marks H3K4Me, H3K4Me2 in stable TRF2 expressed HT1080 cells (A); increase in LSD1 occupancy in TRF2 over-expressing HT1080 cells. (B) (Full images are shown in Supplementary Figures S6 & S7); Co-immunoprecipitation of TRF2 with LSD1 (immunoprecipitation with anti-TRF2 antibody followed by immunoblotting with anti-LSD1 or anti-TRF2 antibody) (C); (D) Reverse Co-immunoprecipitation of LSD1 with TRF2 (immunoprecipitation with anti-LSD1 antibody followed by immunoblotting with anti-TRF2 antibody); (E) & reduced occupancy of the repressor complex REST, Co-REST & LSD1 on silencing TRF2 on p21 promoter. Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/s41598-017-11177-1), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-57130_rabbit-polyclonal-trf-2-antibody-310202415363710.jpg)
![Chromatin Immunoprecipitation: TRF-2 Antibody - BSA Free [NB110-57130] - Thousands of extra-telomeric TRF2 binding sites found across the genome.A, extra-telomeric TRF2 peaks found in HT1080 cells following TRF2 ChIP-Seq: 20304 TRF2 peaks were common between two independent experiments. B, distribution of common TRF2 peaks around TSSs. Distance from the TSS is shown in kb. C, replicate consistency plot generated using irreproducible discovery rate analysis; 1956 peaks found at ≤0.01 are marked. D, distribution of 1956 TRF2 peaks with IDR 0.01 (TRF2HC peaks) around the TSS. Distance from the TSS is shown in kb. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31575660), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-57130_rabbit-polyclonal-trf-2-antibody-310202415371955.jpg)
![Western Blot: TRF-2 Antibody - BSA Free [NB110-57130] - TRF1HP1 alpha allele-specific protection effects upon si-TRF2-induced telomeric damage. 72 h after transfection, a TRF2 knockdown efficiency with antibody against TRF2 (anti-TRF2) & GAPDH (anti-GAPDH) as loading control. (−) si-non-targeting; (+) si-TRF2. Quantification of TIFs in b si-non-targeting (n = 32–47 nuclei per group) or c si-TRF2. Left *p = 0.0188, right *p = 0.0192, **p = 0.0042, ****p < 0.0001 (n = 31–48 nuclei per group). b, c Significance is assessed by one-way ANOVA & Dunnett’s multiple comparison test with 95% confidence level. Error bars represent s.e.m. Note the similar pattern among TRF1HP1 alpha alleles in c compared to the corresponding allele pattern in Fig. 4b Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30181605), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-57130_rabbit-polyclonal-trf-2-antibody-310202415284520.jpg)
![Chromatin Immunoprecipitation: TRF-2 Antibody - BSA Free [NB110-57130] - TRF2 peaks harbor G-quadruplex motifs genome-wide.A, schematic representation of a G4 motif; sequence pattern with loop/stem & PG4 motif formed by a tetrad of guanine trimers interspersed with loops that can vary in length. B & C, PG4 motifs & TRF2 peaks significantly overlap. High-confidence TRF2-binding sites (TRF2HC peaks) determined by ChIP-Seq in HT1080 cells were significantly enriched in PG4-motif sequences (B), & conversely, PG4-motif sequences were enriched within TRF2HC peaks (C). Nonoverlapping PG4 motifs were considered for analysis; for control analysis, 100 regions of identical length for each TRF2 peak were taken. *, p < 0.05; **, p < 0.01 (Fisher's exact test). Error bars, S.D. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31575660), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-57130_rabbit-polyclonal-trf-2-antibody-31020241538415.jpg)
![Western Blot: TRF-2 Antibody - BSA Free [NB110-57130] - Repressive chromatin induced on p21 promoter in TRF2 dependent way. (A–C) Loss of chromatin activation marks H3K4Me, H3K4Me2 in stable TRF2 expressed HT1080 cells (A); increase in LSD1 occupancy in TRF2 over-expressing HT1080 cells. (B) (Full images are shown in Supplementary Figures S6 & S7); Co-immunoprecipitation of TRF2 with LSD1 (immunoprecipitation with anti-TRF2 antibody followed by immunoblotting with anti-LSD1 or anti-TRF2 antibody) (C); (D) Reverse Co-immunoprecipitation of LSD1 with TRF2 (immunoprecipitation with anti-LSD1 antibody followed by immunoblotting with anti-TRF2 antibody); (E) & reduced occupancy of the repressor complex REST, Co-REST & LSD1 on silencing TRF2 on p21 promoter. Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/s41598-017-11177-1), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-57130_rabbit-polyclonal-trf-2-antibody-310202415392522.jpg)
![Western Blot: TRF-2 Antibody - BSA Free [NB110-57130] - TRF2 transcriptionally regulates p21 expression through promoter occupancy. (A) Quantitative ChIP using TRF2 antibody gives enriched binding of TRF2 on p21 promoter in HT1080 & MDA-MB-231 cells, IgG was used as isotypic antibody control; normalized with 10% input (data represented as mean ± SEM, for three replicates). (B,C) TRF2 represses p21 promoter activity. In luciferase assay, si-RNA-mediated silencing or TRF2 over expression resulted in increased (B, *p value < 0.05, Student’s t-test; data represented as mean ± SEM of three replicates) or reduction (C, *p value < 0.05, Student’s t-test; data represented as mean ± SEM of three replicates) in p21 promoter activity in HT1080 & MDA-MB-231 cells, respectively; over expression of TRF2 devoid of DNA binding [deletion of basic (delB), myb (delM) & both basic/myb (delB-delM) domains] resulted in partial or complete rescue of p21 promoter activity in HT1080 & MDA-MB-231 cells (data represented as mean ± SEM, for three replicates) (C). (D,E) HT1080 cells over expressing TRF2 show reduced p21 protein expression, bar graph shows the densitometry analysis of three different immunoblot replicates (*p value < 0.05, Student’s t-test; data represented as mean ± SEM of three replicates). (E) (Full images are shown in Supplementary Figure S5); TRF2 silencing results in increase in p21 protein, bar graph shows the densitometry analysis of three different immunoblots (*p value < 0.05, Student’s t-test; data represented as mean ± SEM of three replicates) (F); & mRNA expression in HT1080 cells (*p value < 0.05, Student’s t-test; data represented as mean ± SEM of three replicates, GAPDH used as internal control for real-time PCR). Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/s41598-017-11177-1), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-57130_rabbit-polyclonal-trf-2-antibody-31020241624926.jpg)
![Chromatin Immunoprecipitation: TRF-2 Antibody - BSA Free [NB110-57130] - TRF2 occupancy at gene promoters is sensitive to intracellular G-quadruplex–binding ligand 360A.A, TRF2 occupancy at gene promoter sites was checked by ChIP qRT-PCR in HT1080 cells following overexpression of TRF2 in the presence or absence of 360A. Error bars, S.D. from three independent experiments; CTCF promoter was used as a negative control. B, TRF2 level was checked by Western blotting in the presence of the ligand 360A in both untransfected & TRF2 transient overexpression conditions. Overexpression was also confirmed by probing for DDK tag. GAPDH was used as loading control. C, expression of target genes was analyzed by qRT-PCR in HT1080 cells following overexpression of TRF2 in the presence or absence of 360A. GAPDH expression was used for normalization; error bars, S.D. from three independent experiments. Statistical significance was calculated by paired t test (*, p < 0.05; **, p < 0.01). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31575660), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-57130_rabbit-polyclonal-trf-2-antibody-3102024162491.jpg)
![Western Blot: TRF-2 Antibody - BSA Free [NB110-57130] - A. Co-IP analysis of the interaction between DSP & TRF2 in HEK293 cells & MCF-7 cells. B. Co-IP analysis of the interaction between DSP & TRF2 in DSP-EGFP transfected HEK293 cells or DSP△NLS-EGFP transfected HEK293 cells. C. DSP pull down by telomere targeting CASID with the condition of TRF2 knockdown in HEK293 cells. Histone H3 is the loading control. D.TRF1 & TRF2 pull-down assay by telomere targeting CASID with the condition of DSP knockdown in HEK293 cells. E. Left, Dot blot of telomere DNA repeats in chromatin pull down by DSP with the condition of TRF1 or TRF2 knockdown. The dot-blot was performed at least three times & the represented one is shown. Right, the histogram shows the quantitated results of the dot blots. The triple asterisks (***) indicates a p-value less than 0.01. ns. indicates the insignificance difference. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31595153), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-57130_rabbit-polyclonal-trf-2-antibody-310202416235527.jpg)
![Immunocytochemistry/ Immunofluorescence: TRF-2 Antibody - BSA Free [NB110-57130] - TERRA & telomere transcription in ALT cells.(a) TERRA northern blot hybridizations of RNA from the indicated cell lines (VA13: WI-38 VA13; 1.2.11: HeLa 1.2.11) pre-treated with RNaseA or left untreated. Ethidium bromide stained 18S ribosomal RNA (rRNA) is shown to control for loading. Long TERRA molecules comprised between the wells of the gels (w) & 28S rRNA are indicated. (b) TERRA CpG-island promoter methylation analysis of the indicated cell lines. Genomic DNA was digested with the methylation sensitive restriction enzyme MspI or its methylation insensitive isoschizomer HpaII. DNA was hybridized using a radioactively labelled probe detecting TERRA promoter CpG-island repeats. Nomet: fragments corresponding to unmethylated restriction products. (c) Dot blot hybridization of DNA immunoprecipitated with antibodies against phosphorylated Serines S2 & S5 of RNA polymerase II C-terminal domain. Hybridizations were performed with a telomeric probe. Quantifications are shown at the bottom. (d) Bars & error bars are averages & s.d. from three independent experiments. (e) Examples of TERRA FISH in the indicated cells. TERRA is shown in red, DAPI-stained DNA in blue. Scale bar, 9 μm. (f) IF/FISH experiments in the indicated cell lines. TERRA is in red, TRF2 in green & PML in blue. In the merge panels, arrowheads point to nuclear foci where the three factors co-localize. Scale bar, 9 μm. (g) Information surface at 0.01 μm detail level of three TERRA-containing APBs. TERRA is in red, TRF2 in green & PML in cyan. Images were generated with Three-Dimensional Structured Illumination Microscopy (3D-SIM). Scale bars, 0.4 μm. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/25330849), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-57130_rabbit-polyclonal-trf-2-antibody-310202416235545.jpg)
![Western Blot: TRF-2 Antibody - BSA Free [NB110-57130] - TRF2 occupancy at gene promoters is sensitive to intracellular G-quadruplex–binding ligand 360A.A, TRF2 occupancy at gene promoter sites was checked by ChIP qRT-PCR in HT1080 cells following overexpression of TRF2 in the presence or absence of 360A. Error bars, S.D. from three independent experiments; CTCF promoter was used as a negative control. B, TRF2 level was checked by Western blotting in the presence of the ligand 360A in both untransfected & TRF2 transient overexpression conditions. Overexpression was also confirmed by probing for DDK tag. GAPDH was used as loading control. C, expression of target genes was analyzed by qRT-PCR in HT1080 cells following overexpression of TRF2 in the presence or absence of 360A. GAPDH expression was used for normalization; error bars, S.D. from three independent experiments. Statistical significance was calculated by paired t test (*, p < 0.05; **, p < 0.01). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31575660), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-57130_rabbit-polyclonal-trf-2-antibody-31020241624924.jpg)
![Western Blot: TRF-2 Antibody - BSA Free [NB110-57130] - A. Gene ontology analysis of proteins identified by CASID targeting telomeres. B. Western blot detection of TRF1, POT1, & DSP in the proteins pulled down by CASID with the presence of telo-sgRNA in HEK293 cells. Input represents the initial nuclear extract before the pull-down mediated by CASID. C. left, ChIP assay of telomere binding of TRF2 or DSP in MCF-7 cells & HEK293 cells. The chromatin DNA precipitated by anti-DSP & anti-TRF2 antibodies were analyzed by dot blot using the probes recognizing telomere (Telo-p) or Alu DNA repeats (Alu-p). The detection of Alu DNA repeats serves as negative control. The dot-blot was performed at least three times & the represented one is shown. Right, the histogram shows the quantitated results of the dot blots. The triple asterisks (***) indicates a p-value less than 0.01. D. Fluorescence imaging of DSP-EGFP in MCF-7 cells & U2OS cells. The EGFP signal indicates the localization of DSP-EGFP (green) & the Telo-FISH signal indicates the localization of telomeres (red). The overlapping between DSP-EGFP & Telo-FISH is in yellow as revealed in the enlarged nuclear area. The dCAS9-EGFP construct without telo-sgRNA was used for U2OS transfection & the imaging of EGFP serves as negative control. E. DSP localization in interphase & pro-metaphase nucleus. DSP-EGFP indicates the DSP locations & DAPI indicates the nucleus. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31595153), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-57130_rabbit-polyclonal-trf-2-antibody-31020241624912.jpg)
![Western Blot: TRF-2 Antibody - BSA Free [NB110-57130] - TRF2 interacts with lamin A/C.(a) Pull down of endogenous TRF2 in IMR90s. The top panel shows a blot probed for endogenous lamin A/C, & the bottom panel shows a blot with the same samples probed for TRF2. (b) Pull down of endogenously expressed lamin A/C in IMR90s. The top panel shows a blot probed for endogenous TRF2, & the bottom panel shows a blot with the same samples probed for endogenous lamin A/C. (c) Pull down of endogenous lamin A/C in IMR90s exogenously expressing GFP, GFP-TRF2, GFP-TRF delta B delta M or GFP-TRF1. The top panel shows a blot probed for GFP, & the bottom panel shows the same blot probed for lamin A/C. (d) Pull down of endogenous TRF2 in IMR90s exogenously expressing GFP, GFP-LMNA or progerin (GFP-LMNA delta 50). The top panel shows a blot probed for GFP, & the bottom panel shows the same blot probed for TRF2. Asterisks denote IgG bands. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/25399868), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-57130_rabbit-polyclonal-trf-2-antibody-310202416235540.jpg)
![Western Blot: TRF-2 Antibody - BSA Free [NB110-57130] - Widespread dysregulation of shelterin protein expression in bortezomib-treated HEL & BGC-823 cellsA. & B. mRNA levels of shelterin factors TRF1, TRF2, TPP1, POT1, RAP1 & TIN2 in bortezomib-treated cells. Cells were treated with bortezomib for 24 hours & qPCR was used for quantitative assays. The levels of each target mRNA in bortezomib-treated cells were expressed as percentages of those in untreated cells. (A) HEL cells & (B) BGC-823 cells. C. & D. Immunoblotting assessment of TRF1, TRF2 & POT1 protein expression in bortezomib-treated cells. Same sets of cells above were analyzed for TRF1, TRF2 & POT1 protein levels & shown was representative of three independent experiments. (C) HEL cells & (D) BGC-823 cells. * & **: P < 0.05 & 0.01, respectively. BTZ, bortezomib. Image collected & cropped by CiteAb from the following publication (//www.oncotarget.com/lookup/doi/10.18632/oncotarget.5752), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-57130_rabbit-polyclonal-trf-2-antibody-31020241623553.jpg)
![Western Blot: TRF-2 Antibody - BSA Free [NB110-57130] - A. Co-IP analysis of the interaction between DSP & TRF2 in HEK293 cells & MCF-7 cells. B. Co-IP analysis of the interaction between DSP & TRF2 in DSP-EGFP transfected HEK293 cells or DSP△NLS-EGFP transfected HEK293 cells. C. DSP pull down by telomere targeting CASID with the condition of TRF2 knockdown in HEK293 cells. Histone H3 is the loading control. D.TRF1 & TRF2 pull-down assay by telomere targeting CASID with the condition of DSP knockdown in HEK293 cells. E. Left, Dot blot of telomere DNA repeats in chromatin pull down by DSP with the condition of TRF1 or TRF2 knockdown. The dot-blot was performed at least three times & the represented one is shown. Right, the histogram shows the quantitated results of the dot blots. The triple asterisks (***) indicates a p-value less than 0.01. ns. indicates the insignificance difference. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31595153), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-57130_rabbit-polyclonal-trf-2-antibody-31020241624919.jpg)
![Western Blot: TRF-2 Antibody - BSA Free [NB110-57130] - Telomere deprotection contributes to replication stress lethality. a Western blots of whole cell extracts from HT1080 6TG cells stably transduced with control, TRF2 shRNA (TRF sh-F) or TRF2 over expression (TRF2OE) vectors. b Representative images of cyto-centrifuged chromosome spreads stained with DAPI (blue), gamma -H2AX IF (red) & telomere PNA (green) from control, TRF sh-F or TRF2OE HT1080 6TG cells treated with DMSO or APH. Scale bar represents 10 µm. c, d Quantitation of mitotic telomere DDR foci from Control sh & TRF2 sh-F cells (c) or vector & TRF2OE cells (d) ± DMSO or APH (three biological replicates scoring n = 50 mitotic spreads per replicate compiled in a Tukey box plot, Mann–Whitney test). e Difference in the mean number of mitotic telomeric gamma -H2AX foci between HT1080 6TG TRF2 sh-F or TRF2OE cells & their appropriate vector control. These are a different representation of the same data shown in (c, d) (mean ± s.e.m., n = 3 three biological replications, Student’s t-test). f Mitotic duration to cell death in APH treated control, TRF2 sh-F & or TRF2OE cells (three biological replicates scoring ≥267 mitotic death events per condition are shown in a dot plot, mean ± s.e.m., Mann–Whitney test). g Mitotic outcome of control, TRF2 sh-F & TRF2OE cells treated with APH or DMSO (mean ± s.e.m., n = 3 biological replicates of at least 267 mitoses per condition, Fisher’s Exact Test). For all panels, *p < 0.05, **p < 0.01. Source data are provided as a Source Data file Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31530811), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-57130_rabbit-polyclonal-trf-2-antibody-310202416235510.jpg)
![Western Blot: TRF-2 Antibody - BSA Free [NB110-57130] - A. Co-IP analysis of the interaction between DSP & TRF2 in HEK293 cells & MCF-7 cells. B. Co-IP analysis of the interaction between DSP & TRF2 in DSP-EGFP transfected HEK293 cells or DSP△NLS-EGFP transfected HEK293 cells. C. DSP pull down by telomere targeting CASID with the condition of TRF2 knockdown in HEK293 cells. Histone H3 is the loading control. D.TRF1 & TRF2 pull-down assay by telomere targeting CASID with the condition of DSP knockdown in HEK293 cells. E. Left, Dot blot of telomere DNA repeats in chromatin pull down by DSP with the condition of TRF1 or TRF2 knockdown. The dot-blot was performed at least three times & the represented one is shown. Right, the histogram shows the quantitated results of the dot blots. The triple asterisks (***) indicates a p-value less than 0.01. ns. indicates the insignificance difference. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31595153), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-57130_rabbit-polyclonal-trf-2-antibody-31020241624913.jpg)
![Western Blot: TRF-2 Antibody - BSA Free [NB110-57130] - A. TRF2 or DSP1 pull down by telomere targeting CASID with the condition of MST-312 treatment (left) or hTERT knockdown (right) in MDA-MB-231cells. B. Southern blot of telomere DNA from MDA-MB-231cells treated with MST-312 or with hTERT knockdown. C. Top, Dot blot of telomere DNA repeats from the chromatin pull down by DSP from the cells treated by MST-312 (left) or hTERT knockdown (right). Alu DNA repeats serve as negative control. Bottom, the histogram shows the quantitated results of the dot blots. The triple asterisks (***) indicates a p-value less than 0.01. D. Fluorescence image of DSP-EGFP transfected MDA-MB-231 cells with the conditions of MST-312 treatment or hTERT knockdown. E. Pull down assay of DSP by CASID targeting telomere in WI38 cells with or without ectopically expression of hTERT gene. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31595153), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-57130_rabbit-polyclonal-trf-2-antibody-31020241624911.jpg)
![Western Blot: TRF-2 Antibody - BSA Free [NB110-57130] - Attenuation of bortezomib-induced shelterin protein dysregulation by hTERT over-expressionA. & B. Cells expressing ectopic hTERT were treated with bortezomib for 24 hours & mRNA levels of shelterin proteins then analyzed using qPCR. The levels of each target mRNA in bortezomib-treated cells were expressed as percentages of those in untreated cells. (A) HEL-hTERT cells & (B) BGC-823-hTERT cells. C. & D. Immunoblotting assessment of TRF1, TRF2 & POT1 protein expression in bortezomib-treated cells. Same sets of cells above were analyzed for TRF1, TRF2 & POT1 protein levels & shown was representative of three independent experiments. (C) HEL-hTERT cells & (D) BGC-823-hTERT cells.* & **: P < 0.05 & 0.01, respectively. BTZ, bortezomib. Image collected & cropped by CiteAb from the following publication (//www.oncotarget.com/lookup/doi/10.18632/oncotarget.5752), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-57130_rabbit-polyclonal-trf-2-antibody-310202416235549.jpg)
![Immunocytochemistry/ Immunofluorescence: TRF-2 Antibody - BSA Free [NB110-57130] - RNaseH1 depletion leads to RPA activation at ALT telomeres.(a) HeLa & U2OS cells were transfected with the indicated siRNAs & 48 & 72 h later protein extracts were prepared. Western blot analysis was performed using antibodies against RNaseH1, RPA32 phosphorylated at Serine 33 (pSer33), total RPA32 & KAP1 (loading control). The asterisk indicates a cross-reacting band. Cells treated for 6 h with 5 mM hydroxyurea (HU) were used as controls for pSer33 activation. (b) SiRNA transfected cells were subjected to indirect immunofluorescence using antibodies against TRF2 (to visualize telomeres; red) & pSer33 (green). DNA was counterstained with DAPI (blue). Arrows point to examples of pSer33 foci co-localizing with TRF2 (TIFs). Scale bar, 9 μm. Cells treated for 6 h with 5 mM HU were used as controls for pSer33 activation. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/25330849), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-57130_rabbit-polyclonal-trf-2-antibody-310202416235532.jpg)
![Western Blot: TRF-2 Antibody - BSA Free [NB110-57130] - TRF2 interacts with lamin A/C.(a) Pull down of endogenous TRF2 in IMR90s. The top panel shows a blot probed for endogenous lamin A/C, & the bottom panel shows a blot with the same samples probed for TRF2. (b) Pull down of endogenously expressed lamin A/C in IMR90s. The top panel shows a blot probed for endogenous TRF2, & the bottom panel shows a blot with the same samples probed for endogenous lamin A/C. (c) Pull down of endogenous lamin A/C in IMR90s exogenously expressing GFP, GFP-TRF2, GFP-TRF delta B delta M or GFP-TRF1. The top panel shows a blot probed for GFP, & the bottom panel shows the same blot probed for lamin A/C. (d) Pull down of endogenous TRF2 in IMR90s exogenously expressing GFP, GFP-LMNA or progerin (GFP-LMNA delta 50). The top panel shows a blot probed for GFP, & the bottom panel shows the same blot probed for TRF2. Asterisks denote IgG bands. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/25399868), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-57130_rabbit-polyclonal-trf-2-antibody-31020241624921.jpg)
![Western Blot: TRF-2 Antibody - BSA Free [NB110-57130] - Widespread dysregulation of shelterin protein expression in bortezomib-treated HEL & BGC-823 cellsA. & B. mRNA levels of shelterin factors TRF1, TRF2, TPP1, POT1, RAP1 & TIN2 in bortezomib-treated cells. Cells were treated with bortezomib for 24 hours & qPCR was used for quantitative assays. The levels of each target mRNA in bortezomib-treated cells were expressed as percentages of those in untreated cells. (A) HEL cells & (B) BGC-823 cells. C. & D. Immunoblotting assessment of TRF1, TRF2 & POT1 protein expression in bortezomib-treated cells. Same sets of cells above were analyzed for TRF1, TRF2 & POT1 protein levels & shown was representative of three independent experiments. (C) HEL cells & (D) BGC-823 cells. * & **: P < 0.05 & 0.01, respectively. BTZ, bortezomib. Image collected & cropped by CiteAb from the following publication (//www.oncotarget.com/lookup/doi/10.18632/oncotarget.5752), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-57130_rabbit-polyclonal-trf-2-antibody-310202416235531.jpg)
![Western Blot: TRF-2 Antibody - BSA Free [NB110-57130] - TRF2 interacts with lamin A/C.(a) Pull down of endogenous TRF2 in IMR90s. The top panel shows a blot probed for endogenous lamin A/C, & the bottom panel shows a blot with the same samples probed for TRF2. (b) Pull down of endogenously expressed lamin A/C in IMR90s. The top panel shows a blot probed for endogenous TRF2, & the bottom panel shows a blot with the same samples probed for endogenous lamin A/C. (c) Pull down of endogenous lamin A/C in IMR90s exogenously expressing GFP, GFP-TRF2, GFP-TRF delta B delta M or GFP-TRF1. The top panel shows a blot probed for GFP, & the bottom panel shows the same blot probed for lamin A/C. (d) Pull down of endogenous TRF2 in IMR90s exogenously expressing GFP, GFP-LMNA or progerin (GFP-LMNA delta 50). The top panel shows a blot probed for GFP, & the bottom panel shows the same blot probed for TRF2. Asterisks denote IgG bands. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/25399868), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-57130_rabbit-polyclonal-trf-2-antibody-3102024162490.jpg)
![Western Blot: TRF-2 Antibody - BSA Free [NB110-57130] - TRF2 transcriptionally regulates p21 expression through promoter occupancy. (A) Quantitative ChIP using TRF2 antibody gives enriched binding of TRF2 on p21 promoter in HT1080 & MDA-MB-231 cells, IgG was used as isotypic antibody control; normalized with 10% input (data represented as mean ± SEM, for three replicates). (B,C) TRF2 represses p21 promoter activity. In luciferase assay, si-RNA-mediated silencing or TRF2 over expression resulted in increased (B, *p value < 0.05, Student’s t-test; data represented as mean ± SEM of three replicates) or reduction (C, *p value < 0.05, Student’s t-test; data represented as mean ± SEM of three replicates) in p21 promoter activity in HT1080 & MDA-MB-231 cells, respectively; over expression of TRF2 devoid of DNA binding [deletion of basic (delB), myb (delM) & both basic/myb (delB-delM) domains] resulted in partial or complete rescue of p21 promoter activity in HT1080 & MDA-MB-231 cells (data represented as mean ± SEM, for three replicates) (C). (D,E) HT1080 cells over expressing TRF2 show reduced p21 protein expression, bar graph shows the densitometry analysis of three different immunoblot replicates (*p value < 0.05, Student’s t-test; data represented as mean ± SEM of three replicates). (E) (Full images are shown in Supplementary Figure S5); TRF2 silencing results in increase in p21 protein, bar graph shows the densitometry analysis of three different immunoblots (*p value < 0.05, Student’s t-test; data represented as mean ± SEM of three replicates) (F); & mRNA expression in HT1080 cells (*p value < 0.05, Student’s t-test; data represented as mean ± SEM of three replicates, GAPDH used as internal control for real-time PCR). Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/s41598-017-11177-1), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-57130_rabbit-polyclonal-trf-2-antibody-310202416235546.jpg)
![Western Blot: TRF-2 Antibody - BSA Free [NB110-57130] - TRF2 transcriptionally regulates p21 expression through promoter occupancy. (A) Quantitative ChIP using TRF2 antibody gives enriched binding of TRF2 on p21 promoter in HT1080 & MDA-MB-231 cells, IgG was used as isotypic antibody control; normalized with 10% input (data represented as mean ± SEM, for three replicates). (B,C) TRF2 represses p21 promoter activity. In luciferase assay, si-RNA-mediated silencing or TRF2 over expression resulted in increased (B, *p value < 0.05, Student’s t-test; data represented as mean ± SEM of three replicates) or reduction (C, *p value < 0.05, Student’s t-test; data represented as mean ± SEM of three replicates) in p21 promoter activity in HT1080 & MDA-MB-231 cells, respectively; over expression of TRF2 devoid of DNA binding [deletion of basic (delB), myb (delM) & both basic/myb (delB-delM) domains] resulted in partial or complete rescue of p21 promoter activity in HT1080 & MDA-MB-231 cells (data represented as mean ± SEM, for three replicates) (C). (D,E) HT1080 cells over expressing TRF2 show reduced p21 protein expression, bar graph shows the densitometry analysis of three different immunoblot replicates (*p value < 0.05, Student’s t-test; data represented as mean ± SEM of three replicates). (E) (Full images are shown in Supplementary Figure S5); TRF2 silencing results in increase in p21 protein, bar graph shows the densitometry analysis of three different immunoblots (*p value < 0.05, Student’s t-test; data represented as mean ± SEM of three replicates) (F); & mRNA expression in HT1080 cells (*p value < 0.05, Student’s t-test; data represented as mean ± SEM of three replicates, GAPDH used as internal control for real-time PCR). Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/s41598-017-11177-1), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-57130_rabbit-polyclonal-trf-2-antibody-31020241624927.jpg)
![Western Blot: TRF-2 Antibody - BSA Free [NB110-57130] - Attenuation of bortezomib-induced shelterin protein dysregulation by hTERT over-expressionA. & B. Cells expressing ectopic hTERT were treated with bortezomib for 24 hours & mRNA levels of shelterin proteins then analyzed using qPCR. The levels of each target mRNA in bortezomib-treated cells were expressed as percentages of those in untreated cells. (A) HEL-hTERT cells & (B) BGC-823-hTERT cells. C. & D. Immunoblotting assessment of TRF1, TRF2 & POT1 protein expression in bortezomib-treated cells. Same sets of cells above were analyzed for TRF1, TRF2 & POT1 protein levels & shown was representative of three independent experiments. (C) HEL-hTERT cells & (D) BGC-823-hTERT cells.* & **: P < 0.05 & 0.01, respectively. BTZ, bortezomib. Image collected & cropped by CiteAb from the following publication (//www.oncotarget.com/lookup/doi/10.18632/oncotarget.5752), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-57130_rabbit-polyclonal-trf-2-antibody-310202416235529.jpg)
![Simple Western: TLR9 Antibody (26C593.2) [NBP2-24729] - Lane view shows a specific band for TLR9 in 0.5 mg/ml of Ramos lysate. This experiment was performed under reducing conditions using the 66-440 kDa separation system. Image using the Azide Free format of this antibody.](http://images.novusbio.com/fullsize/TLR9-Antibody-26C593-2-Simple-Western-NBP2-24729-img0029.jpg "Simple Western: TLR9 Antibody (26C593.2) [NBP2-24729] - Lane view shows a specific band for TLR9 in 0.5 mg/ml of Ramos lysate. This experiment was performed under reducing conditions using the 66-440 kDa separation system. Image using the Azide Free format of this antibody.")
![Flow Cytometry: TLR9 Antibody (26C593.2) [NBP2-24729] - Expression of TLR9 protein on epithelial cells. HNEC, Detroit-562 and FaDu were stained intracellularly with PE-Ab against TLR9 (open histograms) or appropriate isotype control (shaded histograms) and analyzed by flow cytometry. Representative pictures from one out of three independent experiments are shown. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0098239), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/TLR9-Antibody-26C593-2-Flow-Cytometry-NBP2-24729-img0025.jpg)
![<b>Genetic Strategies Validation. </b>Western Blot: TLR9 Antibody (26C593.2) [NBP2-24729] - Expression of TLR-9 protein in HB cells before and after 48 hr of transfection. Beta-actin was used as an internal control. Image collected and cropped by CiteAb from the following publication (//doi.org/10.1371/journal.pone.0092748) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/TLR9-Antibody-26C593-2-Knockdown-Validated-NBP2-24729-img0031.jpg)
![Flow Cytometry: TLR9 Antibody (26C593.2) [NBP2-24729] - Analysis of colonic LP or peritoneal cavity (PerC) of normal mice were evaluated by flow cytometry. B cells were intracellularly stained with the anti-TLR9 antibody after the cell surface staining with anti-B220 and CD5 antibodies, and examined using flow cytometry. N = 3, performed twice. Image collected and cropped by CiteAb from the following publication (//doi.org/10.1371/journal.pone.0146191) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/TLR9-Antibody-26C593-2-Flow-Cytometry-NBP2-24729-img0027.jpg)
![Immunocytochemistry/Immunofluorescence: TLR9 Antibody (26C593.2) [NBP2-24729] - Cbl-b is required for the endocytic transit of TLR9. Representative confocal microscopic images of splenocytes from mice with indicated genotypes. For experiments, cells were stimulated through the BCR (green) for 30 minutes then fixed and stained for TLR9 (blue) and Lamp-1 (red)(n = 3). Image collected and cropped by CiteAb from the following publication (//doi.org/10.1371/journal.pone.0089792) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/TLR9-Antibody-26C593-2-Immunocytochemistry-Immunofluorescence-NBP2-24729-img0032.jpg)
![Immunohistochemistry-Paraffin: TLR9 Antibody (26C593.2) [NBP2-24729] - Monkey retina tissue. Image from verified customer review.](http://images.novusbio.com/fullsize/TLR9-Antibody-26C593-2-Immunohistochemistry-Paraffin-NBP2-24729-img0023.jpg)
![Flow Cytometry: TLR9 Antibody (26C593.2) [NBP2-24729] - Gating strategy for the detection of TLR-7 and -9 in B cell subsets. PBMC were isolated from whole blood and stained for surface markers before cells were fixed, permeabilised and stained for TLR-9. FSC and SSC were first used to gate out debris and SSC-A and SSC-H was utilized to eliminate duplicates. Further gating was done on CD45 and CD19, to target B cells. To separate between the different B cell populations, we gated on CD27 and IgD (D), followed by TLR-9 expression on these subsets. Data from one representative patient is shown. Image collected and cropped by CiteAb from the following publication (//doi.org/10.1371/journal.pone.0120383) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/TLR9-Antibody-26C593-2-Flow-Cytometry-NBP2-24729-img0028.jpg)
![Western Blot: TLR9 Antibody (26C593.2) [NBP2-24729] - Analysis of TLR9 in A) human PBMC, B) human intestine, C) mouse intestine, and D) rat intestine tissue lysates using this antibody at a dilution of 3 ug/ml.](http://images.novusbio.com/fullsize/TLR9-Antibody-26C593-2-Western-Blot-NBP2-24729-img0033.jpg)
![Flow Cytometry: TLR9 Antibody (26C593.2) [NBP2-24729] - Expression of TLR9 on turbinate epithelial cells from healthy controls compared to turbinate and polyp epithelial cells from patients with CRSwNP, n = 5 (A). Intracellular staining for TLR9 (open histogram, black line) and isotype control (filled histogram) on turbinate epithelial cells from a healthy control (B), turbinate epithelial cells (C) and polyp epithelial cells from a patient (D), analysed using flow cytometry. Results are presented as mean +/- SEM, **P<0.01. Image collected and cropped by CiteAb from the following publication (//doi.org/10.1371/journal.pone.0105618) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/TLR9-Antibody-26C593-2-Flow-Cytometry-NBP2-24729-img0030.jpg)
![Western Blot: CHREBP Antibody - BSA Free [NB400-135] - CHREBP Antibody [NB400-135] - Mouse liver tissue lysate, 10 ug total protein per lane, probed with CHREBP antibody. Specific bands at ~150 kDa (some wells as doublets). Weaker bands at ~45 kDa, very faint bands at ~100 kDa. These bands were absent after exposure to ChREBP blocking peptide, although some faint non-specific banding remained at ~90, ~60, and ~40 kDa. WB image submitted by a verified customer review.](http://images.novusbio.com/fullsize/CHREBP-Antibody---BSA-Free-Western-Blot-NB400-135-img0023.jpg "Western Blot: CHREBP Antibody - BSA Free [NB400-135] - CHREBP Antibody [NB400-135] - Mouse liver tissue lysate, 10 ug total protein per lane, probed with CHREBP antibody. Specific bands at ~150 kDa (some wells as doublets). Weaker bands at ~45 kDa, very faint bands at ~100 kDa. These bands were absent after exposure to ChREBP blocking peptide, although some faint non-specific banding remained at ~90, ~60, and ~40 kDa. WB image submitted by a verified customer review.")
![Immunocytochemistry/Immunofluorescence: CHREBP Antibody - BSA Free [NB400-135] - CHREBP Antibody [NB400-135] - RetSat depletion prevents the glucose-induced nuclear accumulation of ChREBP independent of 13,14-dihydroretinol generation. Hepatocytes were treated with Control or RetSat siRNA overnight. The next morning, cells were incubated with vehicle (DMSO) or 1 uM 13,14-dhretinol for 24 h at the indicated glucose concentrations and mRNA expression of Txnip determined by qPCR. Data are shown as mean +/- s.d., n = 4. Two-way ANOVA with Bonferroni post test revealed significances between low and high glucose (#P < 0.05) and between siControl and siRetSat (*P < 0.05), treatment with 13,14-dhretinol had no effect. Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/s41467-017-00430-w), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/CHREBP-Antibody---BSA-Free-Immunocytochemistry-Immunofluorescence-NB400-135-img0021.jpg)
![Immunohistochemistry-Paraffin: CHREBP Antibody - BSA Free [NB400-135] - CHREBP Antibody [NB400-135] - Staining of human colon, epithelium at a 40X magnification.](http://images.novusbio.com/fullsize/CHREBP-Antibody---BSA-Free-Immunohistochemistry-Paraffin-NB400-135-img0016.jpg)
![Chromatin Immunoprecipitation: CHREBP Antibody - BSA Free [NB400-135] - CHREBP Antibody [NB400-135] - Effects of glucose on ChREBP binding.HepG2 cells were treated with low (2.7 mM) and high (25 mM) glucose for 8 h. Chromatin was isolated and fragmented, and ChIP was performed with control IgG or anti-ChREBP antibody. Validated primers for each gene were used for quantitative real-time PCR. The data presented as fold increase for the signal from anti-ChREBP relative to control IgG. The negative control, Cyclo, showed no enrichment (data not shown). Values represent the mean +/- S.D. of three independent samples. *p<0.005 vs. IgG, #p<0.0001 vs. 2.7 mM glucose with anti-ChREBP. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0022544), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/CHREBP-Antibody---BSA-Free-Chromatin-Immunoprecipitation-NB400-135-img0018.jpg)
![Western Blot: CHREBP Antibody - BSA Free [NB400-135] - CHREBP Antibody [NB400-135] - Detection of ChREBP in 20 ug of human hepatocyte lysate using NB400-135. 5-10 second film exposure.](http://images.novusbio.com/fullsize/CHREBP-Antibody---BSA-Free-Western-Blot-NB400-135-img0007.jpg)
![Western Blot: CHREBP Antibody - BSA Free [NB400-135] - CHREBP Antibody [NB400-135] - Detection of ChREBP in liver nuclear extracts from well-fed rats. 7% SDS-PAGE gel, 1:1000 dilution of NB400-135. Photo courtesy of Dr. Uyeda, UT Southwestern University.](http://images.novusbio.com/fullsize/CHREBP-Antibody---BSA-Free-Western-Blot-NB400-135-img0010.jpg)
![Western Blot: CHREBP Antibody - BSA Free [NB400-135] - CHREBP Antibody [NB400-135] - RetSat depletion in mouse liver reduces protein levels and target gene expression of ChREBP. RetSat and ChREBP protein expression by immunoblotting. Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/s41467-017-00430-w), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/CHREBP-Antibody---BSA-Free-Western-Blot-NB400-135-img0019.jpg)
![Western Blot: CHREBP Antibody - BSA Free [NB400-135] - CHREBP Antibody [NB400-135] - Protein expression levels of carbohydrate-responsive element-binding protein (ChREBP), in livers of rats receiving normal water (CON), a 13% (w/v) glucose solution (GLU), a 13% (w/v) fructose solution (FRUC), or a 0.4% (w/v) aspartame solution (n = 6 per diet group). All data were normalized to beta-actin expression levels and are expressed relative to the controls (CON). Data are expressed as means +/- SEM. * p < 0.05, ** p < 0.01, *** p < 0.001 vs. CON; +p < 0.05, ++p < 0.01, +++p < 0.001 vs. ASP; p < 0.01, p < 0.001 vs. GLU. Image collected and cropped by CiteAb from the following publication (//www.mdpi.com/2072-6643/9/5/476), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/CHREBP-Antibody---BSA-Free-Western-Blot-NB400-135-img0020.jpg)
![Immunocytochemistry/Immunofluorescence: CHREBP Antibody - BSA Free [NB400-135] - CHREBP Antibody [NB400-135] - HeLa cells were fixed for 10 minutes using 10% formalin and permeabilized for 5 minutes using 1X TBS + 0.5% Triton X-100. The cells were incubated with anti-ChREBP (NB400-135) at a 1:200 dilution overnight at 4C and detected with an anti-rabbit DyLight 488 (Green) at a 1:500 dilution. Alpha tubulin was used as a co-stained at 1:1000 and detected with an anti-mouse DyLight 550 (Red) at a 1:500. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 40X objective.](http://images.novusbio.com/fullsize/CHREBP-Antibody---BSA-Free-Immunocytochemistry-Immunofluorescence-NB400-135-img0017.jpg)
![Immunohistochemistry: CHREBP Antibody - BSA Free [NB400-135] - CHREBP Antibody [NB400-135] - Analysis of CHREBP in mouse liver using DAB with hematoxylin counterstain.](http://images.novusbio.com/fullsize/CHREBP-Antibody---BSA-Free-Immunohistochemistry-NB400-135-img0013.jpg)
![<b>Genetic Strategies Validation. </b>Western Blot: CHREBP Antibody - BSA Free [NB400-135] - Immunoblot analysis of ChREBP in liver lysates of control and L-Chrebp -/- mice. Aliquots (60 ug of protein) of liver whole-cell lysates were subjected to SDS-PAGE and immunoblot analysis with anti-ChREBP and anti-calnexin antibodies. ChREBP delta denotes a truncated aberrant ChREBP protein present only in lysates prepared from L-Chrebp -/- livers. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29335275/) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/CHREBP Antibody - BSA Free-Knockout Validated-NB400-135-img0024.jpg)
![Western Blot: CHREBP Antibody - BSA Free [NB400-135] - Raffinose stimulates transcription of genes involved in epidermal barrier function in HaCaT cells.(a & b) HaCaT cells were treated with vehicle, 1 μM or 10 μM raffinose (Raf), or 1 μM TO901317 (T17) for 24 h. Expressions of transcripts (a) & proteins (b) were analyzed by qRT-PCR or western blotting, respectively. FLG; filaggrin. IVL; involucrin, LOR; loricrin, AQP3; aquaporin3. (c) HaCaT cells were transfected with siGFP control, siLXR alpha , or siLXR beta , & then treated with 1 μM raffinose for 24 h. Expression of proteins was analyzed by western blotting. The original blots are shown in Supplementary Fig. S9. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28266648), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-135_rabbit-polyclonal-chrebp-antibody-310202415291928.jpg)
![Immunohistochemistry-Paraffin: CHREBP Antibody - BSA Free [NB400-135] - Impaired hepatic SIRT1-FoxO signaling in L-G6pc-/- mice.(A) Western blots & densitometry analysis (n = 5), & quantification of mRNA for hepatic SIRT1 & FoxO3a (n = 8). (B) Hepatic NAD+ levels (n = 9). (C) Western blots & densitometry analysis of PPAR-gamma , PPAR-alpha & beta -actin (n = 5). (D) Immunohistochemical analysis of hepatic ChREBP & quantification of nuclear ChREBP-translocated cells (n = 4). Scale bar, 25 μm. (E) Quantification of mRNA for hepatic Acaca, Fasn & Elovl6 by real-time RT-PCR (n = 6). (F) Western blots of acetylated & total FoxO3a after immunoprecipitation of nuclear extracts using anti-FoxO3a, & quantification of the acetylated FoxO3a/total FoxO3a (n = 5). Data represent the mean ± SEM. *P < 0.05, **P < 0.005. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28558013), licensed under a CC0-1.0 license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-135_rabbit-polyclonal-chrebp-antibody-310202415171345.jpg)
![Western Blot: CHREBP Antibody - BSA Free [NB400-135] - Expressing recombinant ChREBP beta in Rictor-deficient adipocytes rescues expression of DNL enzymes.Western blot of indicated proteins in differentiated adipocytes with or without Rictor deletion transfected with various rescue constructs that were stably expressed in cells before differentiation. ‘*' indicates ChREBP beta based on molecular weight. Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/ncomms11365), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-135_rabbit-polyclonal-chrebp-antibody-310202415171318.jpg)
![Western Blot: CHREBP Antibody - BSA Free [NB400-135] - Hepatic expression of mRNAs encoding carbohydrate response element-binding protein (ChREBP) (a), liver pyruvate kinase (LPK) (c), & microsomal triglyceride transfer protein (MTTP) (d), & nuclear ChREBP protein (b) in water-control, 10% fructose solution-control, & fructose pair-fed oleanolic acid- (OA-) treated rats at week 10. Animals were administered with OA (25 mg/kg/day) or vehicle (OA: 0 mg/kg, 5% Gum Arabic) by oral gavage daily for 10 weeks. mRNA was determined by real-time PCR. Protein expression was determined by Western blot. Data are means ± SEM (n = 6 each group). *P < 0.05. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/23737835), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-135_rabbit-polyclonal-chrebp-antibody-31020241529337.jpg)
![Western Blot: CHREBP Antibody - BSA Free [NB400-135] - LXR mediate the induction of lipogenesis induced by an oleic acid-rich diet.(A) Hepatic Acly, Acaca, Acacb, Fasn, Elovl6, Scd1 mRNA levels quantified by qPCR. (B) Cytoplasmic protein expression levels of P-ACLY, ACLY, ACC, ELOVL6, SCD1, FASN & beta -ACTIN assayed by Western Blotting. (C) Fads1, Fads2, Elovl5, Gpat, Pnpla3 & Lpk mRNA quantification assayed by qPCR. (D) Srebp-1c & Chrebp mRNA quantification assayed by qPCR. (E) Cytoplasmic & nuclear expression levels of LXR, SREBP-1c & ChREBP assayed by Western Blotting. Data are the mean±SEM of values measured in LXR+/+ & LXR-/- mice fed REF or OLIV diet. a Significant genotype effect. b Significant difference versus REF diet (n = 6 mice per group). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28732092), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-135_rabbit-polyclonal-chrebp-antibody-31020241534316.jpg)
![Western Blot: CHREBP Antibody - BSA Free [NB400-135] - Analysis of protein levels in livers transfected with GK & GKA456V. Livers excised from mice in postabsorptive state were homogenized & resolved by Western blot. (a, b) Representative blots from three independent experiments. The densitometric analysis is presented (N = 4, *P < 0.05 versus pControl, ***P < 0.001 versus pGKA456V). (c) Liver sections of 5-hour fasted mice injected with pControl, pGK, or pGKA456V were immunostained with Glc6Pase antibody. TO-PRO-3 was used to visualize nuclei. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/22194744), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-135_rabbit-polyclonal-chrebp-antibody-310202415371929.jpg)
![Western Blot: CHREBP Antibody - BSA Free [NB400-135] - ChREBP knockdown inhibited glycolysis, lipogenesis & p21 in HT29 cells. (A) Inhibited relative mRNA expression of ChREBP alpha & ChREBP beta normalized to B2M after control or ChREBP siRNA transfection for 48 hours. (B) Western-blot of ChREBP, phospho-p53 & p21 & their quantification on the right. beta -actin was served as a loading control. Proteins were extracted from cells transfected with sicontrol & siChREBP after 48 hours. The quantification of western blot was normalized to beta -actin. (C) Decreased relative mRNA expression of glycolytic & lipogenic genes, normalized to B2M. (D) Relative mRNA expression of p53 & p21, normalized to B2M. (E) Relative mRNA expression of cell Cyclins, normalized to B2M. n = 4. *p < 0.05; **p < 0.01; ***p < 0.001. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32144313), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-135_rabbit-polyclonal-chrebp-antibody-31020241528455.jpg)
![Western Blot: CHREBP Antibody - BSA Free [NB400-135] - Ligand-activated LXR reduces ChREBP binding to chromatin. (A). Left panels: Local pattern of LXR-ChREBP co-occupancy. Browser view of LXR & ChREBP tracks in the promoter region of Lpk (Pklr), Txnip, Fasn & Scd1. Square brackets indicate the scale maxima of ChIP/input ratios. Arrows indicate the genomic locations of quantitative RT-PCR primers. Right panel: AML12 cells transfected with ChREBP alpha /Mlx gamma & LXR alpha /RXR alpha were treated with DMSO (0.1%) or GW3965 (10 µM) for 18 h. ChREBP or LXR binding to genomic location indicated in the right panels were detected by ChIP using antibodies against ChREBP, LXR or IgG as negative control. Data are presented as mean ± SEM (n = 3–5). Significant differences are shown as * p < 0.05, ** p < 0.01, *** p < 0.001 compared to ChIP-IgG & #p < 0.05, ##p < 0.01, ###p < 0.001 between DMSO & GW3965 groups. ns, not significant. (B). CoIP of LXR alpha & ChREBP alpha , expressed in COS-1 cells cultured in 25 mM glucose, treated with DMSO (0.1%) or GW3965 (1 µM) for 18 h. Lysates were immunoprecipitated with ChREBP antibody (n = 3). Input & immunoprecipitated proteins were immunoblotted with ChREBP or LXR alpha antibodies. One representative western blot is shown. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32414201), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-135_rabbit-polyclonal-chrebp-antibody-310202416171431.jpg)
![Western Blot: CHREBP Antibody - BSA Free [NB400-135] - Induction of hepatic Srebp-1 & carbohydrate response element-binding protein (Chrebp) beta expression by dietary glucose is reduced in LXR alpha −/− mice. (A) Hepatic gene expression of Lxr alpha / beta , Srebp-1, & Chrebp alpha / beta was analyzed by quantitative RT-PCR & normalized to Tbp; (B) Cytosolic & nuclear lysates were immunoblotted with antibodies against LXR, SREBP-1, & ChREBP with alpha -Tubulin & Lamin A as loading controls. Each lane represents independent mice from each group. One representative western blot is shown (n = 3). Data represent the mean ± SEM (n = 5). Significant differences were found using two-way ANOVA followed by Tukey’s multiple comparison test (fasted vs. fructose fed & fasted vs. glucose fed RNA data were analyzed separately). * p < 0.05, ** p < 0.01, *** p < 0.001 compared to fasted. #p < 0.05, ##p < 0.01, ###p < 0.001 compared to LXR alpha +/+ mice. Image collected & cropped by CiteAb from the following publication (//www.mdpi.com/2072-6643/9/7/678), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-135_rabbit-polyclonal-chrebp-antibody-3102024161891.jpg)
![Western Blot: CHREBP Antibody - BSA Free [NB400-135] - Decreased glucose uptake & Chrebp beta -driven DNL is a primary consequence of Rictor loss in adipocytes.(a) Western blots of indicated proteins at different days of differentiation using Rictor iKO primary adipocytes (described in Methods). (b) Oil Red O staining of differentiated adipocytes. (c) The relative mRNA level of ChREBP beta in differentiated cells at various time points. n=3. (d) 2-DG uptake in differentiated adipocytes without or with insulin stimulation. n=3. (e) The C14-glucose-derived FA in differentiated adipocytes. n=3. (f) The C14-glucose derived triglyceride (TAG) in differentiated adipocytes. n=3. (g) Relative glut4 expression in differentiated cells at various time points. n=3. (h) Relative glut4 expression in sWAT. n=8. (i) Glycerol release in differentiated adipocytes under basal & isoproterenol (Iso) stimulation. n=4. (j) Glycerol release in ex vivo pgWAT under basal & isoproterenol stimulation. n=6. Data were analysed by Student's t-test. Values are expressed as mean+s.e.m. *P<0.05; **P<0.01; ***P<0.001. Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/ncomms11365), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-135_rabbit-polyclonal-chrebp-antibody-310202416163714.jpg)
![Western Blot: CHREBP Antibody - BSA Free [NB400-135] - RetSat controls ChREBP activity & glucose sensing in primary hepatocytes. Primary mouse hepatocytes were treated with Control or RetSat siRNA for 48 h, (a, left) ChREBP mRNA expression determined by qPCR, & RetSat & ChREBP protein levels determined by immunoblotting (a, right). left, Data are shown as mean ± 11s.d., n = 3 independent transfections of hepatocyte cultures from the same mouse. Two independent experiments yielded similar results. b Hepatocytes were treated as described in a & mRNA expression of a selection of known ChREBP target genes visualized in a heatmap. c Primary hepatocytes were depleted of RetSat using two siRNA’s targeting different sites of the RetSat transcript for 48 h, & expression of the indicated genes analyzed by qPCR. Data are shown as mean ± s.d., n = 6 independent transfections of hepatocyte cultures from two different mice; *P < 0.05 between siControl und siRetSat by one-way ANOVA with Bonferroni post test. An independent experiment yielded similar results. d Hepatocytes treated with Control or RetSat siRNA were transfected with a ChoRE-Luc reporter, exposed to low & high glucose concentrations as indicated, & analyzed for luciferase activity. e Hepatocytes treated with Control or RetSat siRNA were exposed to low & high glucose concentrations as indicated, & mRNA expression determined by qPCR. In d, e, data are shown as mean ± s.d., n = 6 independent transfections of hepatocyte cultures from two mice; two-way ANOVA with Bonferroni post test revealed significances between low & high glucose concentrations (#P < 0.05) & between siControl & siRetSat (*P < 0.05). An independent experiment yielded similar results Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/s41467-017-00430-w), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-135_rabbit-polyclonal-chrebp-antibody-310202416165648.jpg)
![Western Blot: CHREBP Antibody - BSA Free [NB400-135] - LXR alpha & ChREBP alpha interact via key activation domains. (A). Top panel: Schematic representation of the ChREBP alpha full-length (FL), ChREBP beta & the low glucose inhibitory domain (LID) protein. Bottom panel: CoIP of LXR alpha & ChREBP alpha , ChREBP beta or LID, expressed in COS-1 cells cultured in 25 mM glucose. The ChREBP expression plasmids were transfected with a DNA ratio of ChREBP alpha :ChREBP beta :LID = 1:6:1, to obtain comparable protein levels. Lysates were immunoprecipitated with ChREBP, FLAG (for LID) or LXR alpha antibodies & input & immunoprecipitated proteins immunoblotted with the same antibodies (n = 3). One representative western blot is shown. LID, low-glucose inhibitory domain; GRACE, glucose-response activation conserved element; bHLH, basic helix-loop-helix domain: ZIP, leucine zipper. (B). Top panel: Schematic representation of the LXR alpha FL & truncations. Bottom panel: CoIP of ChREBP alpha & LXR alpha FL or truncations expressed in COS-1 cells cultured in 25 mM glucose. Lysates were immunoprecipitated with ChREBP antibody (n = 3). Input & immunoprecipitated proteins were immunoblotted with ChREBP or FLAG (for LXR alpha FL & truncations) antibodies. One representative western blot is shown. NTD, N-terminal domain; DBD, DNA-binding domain; LBD, ligand-binding domain. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32414201), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-135_rabbit-polyclonal-chrebp-antibody-310202416175271.jpg)
![Western Blot: CHREBP Antibody - BSA Free [NB400-135] - FXR inhibits glucose-induced proglucagon expression(a) Proglucagon qPCR on cDNA from GLUTag cells starved for 12h with lactate (10 mmol L−1) & then incubated for 24h in lactate (10 mmol L−1), glucose (5.6 mmol L−1) or 2-deoxyglucose (5.6 mmol L−1) media containing DMSO, GW4064 (5 μmol L−1) or CDCA (100 μmol L−1) (n=3; performed 3 times). Data are represented as mean +/− SD. Two-Way ANOVA analysis followed by Bonferronni’s posthoc test. ***P≤0.001: effect of GW4064 & CDCA on proglucagon mRNA levels in each medium conditions. §§§P≤0.001: effect of glucose on proglucagon mRNA levels in DMSO, GW4064 & CDCA conditions. (b) Chrebp qPCR on cDNA from FACS-sorted proglucagon-negative & proglucagon-positive cells from the ileum (ileum L−; ileum L+) & colon (colon L−; colon L+) of GLU-VENUS mice (lower panel; n=3) & ChREBP protein expression from cytoplasm & nucleus extract from GLUTag cells (upper panel; performed 3 times). Data are represented as mean +/− SD. Student t-test. *P≤0.05 & **P≤0.01 (c) ChREBP & FXR western-blots after FXR immunoprecipitation on lysates from cytoplasm & nucleus of GLUTag cells treated or not with GW4064 (5 μmol L-1) in presence or not of glucose (5.6 mmol L−1) (performed 2 times). (d) Proglucagon qPCR on cDNA from GLUTag cells electroporated with a siCtrl or siChrebp, starved for 12h with lactate (10 mmol L−1) & then incubated for 24h in lactate 10 mmol L−1 (Glc −) or glucose 5.6 mmol L−1 (Glc +) media supplemented with DMSO or GW4064 (5 μmol L−1) (n=3; performed 3 times). Data are represented as mean +/− SD. Two-Way ANOVA analysis followed by Bonferronni’s posthoc test. *P≤0.05 & **P≤0.01: effect of treatments on each transfection condition. §§§P≤0.001: effect of siChrebp in each treatment condition. Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/ncomms8629), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-135_rabbit-polyclonal-chrebp-antibody-31020241616057.jpg)
![Western Blot: CHREBP Antibody - BSA Free [NB400-135] - Dietary fructose induces nuclear O-GlcNAc signaling. (A) Simplified schematic overview of the hexosamine signaling pathway including the rate limiting enzyme GFAT & O-GlcNAc transferase (OGT); (B) High-performance liquid chromatography (HPLC) analysis of hepatic UDP-GlcNAc levels. Left panel: Example of a typical running profile w/ or w/out injection of UDP-GlcNAc standard (Std.) is shown. Right panel: Quantification of the HPLC data normalized to protein concentration; (C) Hepatic expression of the Ogt gene & cytosolic & nuclear OGT protein analyzed by quantitative RT-PCR & western blotting/Image J & normalized to Tbp, alpha -tubulin, & Lamin A, respectively. Data represent the mean ± SEM (n = 5); (D) Cytosolic & nuclear lysates immunoblotted w/ anti-O-GlcNAc antibody (RL2) w/ alpha -Tubulin & Lamin A as loading controls. Each lane represents independent mice from each group. One representative western blot is shown (n = 2); (E) Nuclear lysates subjected to wheat germ agglutinin (WGA) beads to precipitate O-GlcNAcylated proteins. WGA enriched samples (upper panel) & input lysates (bottom panel) immunoblotted w/ antibodies detecting O-GlcNAcylated proteins (RL2), LXR & ChREBP. Each lane represents independent mice from experimental groups. Representative western blots are shown (n = 2); (F) ChREBP binding to carbohydrate response element (ChoRE) containing region of the L-pk promoter & negative control sequence (NC) 2216–2288 bp into L-pk gene after ChoRE sequence detected by chromatin immunoprecipitation (ChIP) using antibodies against ChREBP or IgG as a control. Data represent the mean ± SEM (n = 5). Significant differences found using two-way ANOVA followed by Tukey’s multiple comparison test. ** p < 0.01 compared to fasted. Image collected & cropped by CiteAb from the following publication (//www.mdpi.com/2072-6643/9/7/678), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-135_rabbit-polyclonal-chrebp-antibody-310202416171465.jpg)
![Immunohistochemistry-Paraffin: CHREBP Antibody - BSA Free [NB400-135] - Correction of hepatic G6Pase-alpha deficiency normalizes autophagy.L-G6pc-/- mice were treated with 1 x 1012 vp/kg of rAAV-G6PC at 4 WP & analyzed at 12 WP. (A) Hepatic G6Pase-alpha activity in control (n = 7), L-G6pc-/- (n = 7), & rAAV-treated L-G6pc-/- (AAV/ L-G6pc-/-, n = 8) mice. (B) Liver weights in control (n = 10), L-G6pc-/- (n = 5), & AAV/ L-G6pc-/- (n = 8) mice. (C) The levels of hepatic metabolites in control, L-G6pc-/- & AAV/ L-G6pc-/- (n = 8) mice. (D) Fasting glucose test (FGT) profile of control (n = 13), L-G6pc-/- (n = 6) & AAV/ L-G6pc-/- (n = 8) mice. (E) Western blots of hepatic SIRT1, FoxO3a, LC3B, p62 & beta -actin & densitometry analysis (n = 8). (F) Hematoxylin & eosin (H&E) stained liver sections, & immunohistochemical analysis of hepatic ChREBP & quantification of nuclear ChREBP-translocated cells in control, L-G6pc-/-, & rAAV-treated L-G6pc-/- (AAV/ L-G6pc-/-) mice (n = 4). The insets present higher magnification views. Scale bar, 25 μm. Data represent the mean ± SEM. *P < 0.05, **P < 0.005. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28558013), licensed under a CC0-1.0 license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-135_rabbit-polyclonal-chrebp-antibody-310202416175247.jpg)
![Western Blot: CHREBP Antibody - BSA Free [NB400-135] - Phf2 expression is increased in the liver of obese patients with benign hepatic steatosis & positively correlates with insulin sensitivity. Human liver biopsies from lean subjects with no fatty liver (NoFL) or obese patients with simple steatosis or NASH were obtained from the ABOS cohort. a Representative Western blot analysis of Phf2, ChREBP, SCD1, Nrf2, Gpx4, & alpha -SMA expression (n = 10 per group). b ChIP experiments for H3K9me2 levels & for the recruitment of ChREBP & the RNA polII at the SCD1 & Nrf2 promoter (n = 10 per group). c MUFA/SFA ratio reflecting SCD1 activity (n = 10 per group). d Expression of Nrf2 & Nrf2-regulated genes (n = 10 per group). e Levels of carbonylated proteins (n = 10 per group). f Expression of coll-Ia1, alpha -SMA, & TIMP-1 (n = 10 per group). All error bars represent mean ± SEM. Statistical analyses were made using Anova, followed by Bonferonni’s test. *Obese with steatosis compared to lean with noFL; P < 0.01. **Obese with steatosis compared to obese with NASH; P < 0.05 Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/s41467-018-04361-y), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-135_rabbit-polyclonal-chrebp-antibody-310202416163772.jpg)
![Western Blot: DNMT1 Antibody (60B1220.1) [NB100-56519] - Analysis of Dnmt1 in 2102EP (human embryonic carcinoma) in the A) absence and B) presence of immunizing peptide, recombinant human Dnmt1 protein in the C) absence and D) presence of immunizing peptide, NIH 3T3 (mouse embryonic fribroblast) in the E) absence and F) presence of immunizing peptide, and D3 (mouse embryonic stem cell) in the G) absence and H) presence of immunizing peptide using Dnmt1 antibody. this antibody. 5 ug/ml for testing the human cell line and 0.1 ug/ml was used for testing the recombinant protein and the mouse cell lines. ’s goat anti-mouse Ig HRP secondary antibody and PicoTect ECL substrate solution were used for this test.](http://images.novusbio.com/fullsize/DNMT1-Antibody-60B1220-1-Western-Blot-NB100-56519-img0003.jpg "Western Blot: DNMT1 Antibody (60B1220.1) [NB100-56519] - Analysis of Dnmt1 in 2102EP (human embryonic carcinoma) in the A) absence and B) presence of immunizing peptide, recombinant human Dnmt1 protein in the C) absence and D) presence of immunizing peptide, NIH 3T3 (mouse embryonic fribroblast) in the E) absence and F) presence of immunizing peptide, and D3 (mouse embryonic stem cell) in the G) absence and H) presence of immunizing peptide using Dnmt1 antibody. this antibody. 5 ug/ml for testing the human cell line and 0.1 ug/ml was used for testing the recombinant protein and the mouse cell lines. ’s goat anti-mouse Ig HRP secondary antibody and PicoTect ECL substrate solution were used for this test.")
![Immunocytochemistry/Immunofluorescence: DNMT1 Antibody (60B1220.1) [NB100-56519] - Dnmt1 antibody was tested in HeLa cells with Dylight 488 (green). Nuclei and alpha-tubulin were counterstained with DAPI (blue) and DyLight 550 (red). Antibody dilution of 1:10 was used. Image objective 40x.](http://images.novusbio.com/fullsize/DNMT1-Antibody-60B1220-1-Immunocytochemistry-Immunofluorescence-NB100-56519-img0006.jpg)
![Immunohistochemistry-Paraffin: DNMT1 Antibody (60B1220.1) [NB100-56519] - Tissue section of human hepatocellular carcinoma at 1:50 dilution.](http://images.novusbio.com/fullsize/DNMT1-Antibody-60B1220-1-Immunohistochemistry-Paraffin-NB100-56519-img0007.jpg)
![Flow Cytometry: DNMT1 Antibody (60B1220.1) [NB100-56519] - An intracellular stain was performed on HeLa cells with DNMT1 [60B1220.1] Antibody NB100-56519AF488 (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 5 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to Alexa Fluor 488.](http://images.novusbio.com/fullsize/DNMT1-Antibody-60B1220-1-Flow-Cytometry-NB100-56519-img0010.jpg)
![Flow Cytometry: DNMT1 Antibody (60B1220.1) [NB100-56519] - Analysis of PE conjugate of NB100-56519. An intracellular stain was performed on HeLa cells with DNMT1 antibody (60B1220.1) NB100-56519PE (blue) and a matched isotype control NBP2-27287PE (orange). Cells were fixed with 4% PFA and then permeablized with 0](http://images.novusbio.com/fullsize/DNMT1-Antibody-60B1220-1-Flow-Cytometry-NB100-56519-img0009.jpg)
![Simple Western: DNMT1 Antibody (60B1220.1) [NB100-56519] - Simple Western lane view shows a specific band for Dnmt1 in 0.5 mg/mL of HeLa lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system.](http://images.novusbio.com/fullsize/DNMT1-Antibody-60B1220-1-Simple-Western-NB100-56519-img0008.jpg)
![Immunoprecipitation: DNMT1 Antibody (60B1220.1) [NB100-56519] - The PCNAS228I mutation differentially affects PCNA binding to PIP box-containing proteins. GST-PIP pull down of His-S-PCNAWT or PCNAS228I. Figure shows Coomassie stained gel of representative pull down (top) and anti-PCNA western blot of the same samples diluted 1:20 (bottom). Amount of 'input' loaded for Coomassie is equivalent to 1%, 'Glut. beads' (Glutathione sepharose 4B beads) is equivalent to 25%. Molecular weight markers are indicated. Image collected and cropped by CiteAb from the following publication (//linkinghub.elsevier.com/retrieve/pii/S1568786416304013), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/DNMT1-Antibody-60B1220-1-Immunoprecipitation-NB100-56519-img0011.jpg)
![Western Blot: DNMT1 Antibody (60B1220.1) - BSA Free [NB100-56519] - WA does not alter DNMTs gene & protein expression(A) Effect of WA on DNMT1, DNMT3A & DNMT3B gene expression in MDA-MB-231 & MCF-7 cells normalized to select housekeeping genes & relative to DMSO-treated MCF-7 sample (2-delta delta Ct) as determined by Human Epigenetic Chromatin Modification Enzyme qPCR Array as previously described. Bars represent DNMT1, DNMT3A & DNMT3B relative mRNA (mean ± SEM) expression of at least two independent experiments. (B) Effect of WA on DNMT1, DNMT3A & DNMT3B protein expression in MDA-MB-231 & MCF-7 cells, as compared to to beta -Actin protein levels. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28467815), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-56519_mouse-monoclonal-dnmt1-antibody-60b1220-1-310202415171327.jpg)
![Chromatin Immunoprecipitation: DNMT1 Antibody (60B1220.1) - BSA Free [NB100-56519] - Epigenetic changes & protein binding at Ankrd26 promoter in eAT from mice upon 22 weeks of HFD.ChIP of DNMT1, DNMT3a, DNMT3b (a) & MBD2 (b) binding at Ankrd26 promoter region (−553 bp/−348 bp). (c) MNase for Nuc-2 (−257 bp/−198 bp) & Nuc-1 (−84 bp/−25 bp) occupancy at Ankrd26 promoter. (d) ChIP for acetyl-H4 enrichment at Nuc-2 & Nuc-1. (e) ChIP of RNA Pol II binding at Ankrd26 TSS (+16 bp/+159 bp). (a,b) & (d,e), ChIP enrichment is relative to Input chromatin. (a–e), results are mean ± SD from three independent experiments. **p < 0.01 & ***p < 0.001 vs STD. Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/srep43526), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-56519_mouse-monoclonal-dnmt1-antibody-60b1220-1-310202415304276.jpg)
![Western Blot: DNMT1 Antibody (60B1220.1) - BSA Free [NB100-56519] - Verification of the expression of the proteins identified.(A) Validation of the SILAC results of selected proteins in immunoblots of protein extracts from the bladder cancer cells analyzed. The results validated the expression levels of proteins identified by the proteomic approach, including differentially & non-differentially expressed candidates. Antibodies displaying a single predominant band at the expected molecular weights were accepted: & alpha -tubulin, was used as the loading control. GSN, Gelsolin; Cul3, Cullin 3; IPO9. Importin 9; EGFR, Epidermal Growth Factor Receptor; NUP133, Nucleoporin 133; HSP70, Heat Shock Protein 70kDa; MCM6, Minichromosome Maintenance Complex Component 6; RCC1, Regulator of Chromosome Condensation 1; BCAS2, Breast Carcinoma Amplified Sequence 2; DNM, Dynamin; NPM, Nucleophosmin; DCTN, Dynactin; CALR, Calreticulin; MAPK, Mitogen-Activated Protein Kinase; DDX21, DEAD (Asp-Glu-Ala-Asp) box polypeptide 21; CDC2: Cell Division Cycle 2; DNMT1, DNA (cytosine-5)-Methyltransferase 1; MSH6, MutS Homolog 6; RAB14, GTPase Rab14; VDAC, Voltage-Dependent Anion Channel; CK18, Cytokeratin 18; CALD, Caldesmon; CD44, CD44 antigen isoform 1 precursor 2; EZR, Ezrin; MSN, Moesin; ANXA2, Annexin A2; CPNE3, Copine 3; FLNA, Filamin A; CAV1, Caveolin 1. Western Blots were scanned & analyzed using alpha -tubulin as normalizing control. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/23308193), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-56519_mouse-monoclonal-dnmt1-antibody-60b1220-1-3102024165721.jpg)
![Immunocytochemistry/Immunofluorescence: beta-Actin Antibody [NB600-503] - Cultured pig trabecular meshwork cells stained with beta-Actin antibody at a dilution of 1:500 followed by an anti-rabbit Alexa Fluor488 at 1:1000 dilution (green). Image from verified customer review.](http://images.novusbio.com/fullsize/beta-Actin-Antibody-Immunocytochemistry-Immunofluorescence-NB600-503-img0012.jpg "Immunocytochemistry/Immunofluorescence: beta-Actin Antibody [NB600-503] - Cultured pig trabecular meshwork cells stained with beta-Actin antibody at a dilution of 1:500 followed by an anti-rabbit Alexa Fluor488 at 1:1000 dilution (green). Image from verified customer review.")
![Western Blot: beta-Actin Antibody [NB600-503] - Rabbit polyclonal at 1/5000.](http://images.novusbio.com/fullsize/beta-Actin-Antibody-Western-Blot-NB600-503-img0004.jpg)
![Simple Western: beta-Actin Antibody [NB600-503] - Simple Western lane view shows a specific band for Beta Actin in 0.1 mg/ml of HeLa lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system.](http://images.novusbio.com/fullsize/beta-Actin-Antibody-Simple-Western-NB600-503-img0008.jpg)
![Flow Cytometry: beta-Actin Antibody [NB600-503] - An intracellular stain was performed on HeLa cells with beta-actin Antibody NB600-503AF488 (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 5 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to Alexa Fluor 488.](http://images.novusbio.com/fullsize/beta-Actin-Antibody-Flow-Cytometry-NB600-503-img0013.jpg)
![Western Blot: beta-Actin Antibody [NB600-503] - Western blot analysis of Jurkat, COS, and CHO cell lysate using beta actin antibody at 1:100.](http://images.novusbio.com/fullsize/beta-Actin-Antibody-Western-Blot-NB600-503-img0006.jpg)
![Immunohistochemistry-Paraffin: beta-Actin Antibody [NB600-503] - Analysis of Beta Actin in mouse epidermis using DAB with hematoxylin counterstain.](http://images.novusbio.com/fullsize/beta-Actin-Antibody-Immunohistochemistry-Paraffin-NB600-503-img0009.jpg)
![Immunocytochemistry/Immunofluorescence: beta-Actin Antibody [NB600-503] - IF Confocal analysis of HeLa cells using Beta Actin antibody (NB600-503, 1:5). An Alexa Fluor 488-conjugated Goat to rabbit IgG was used as secondary antibody (green). DAPI was used to stain the cell nuclei (blue).](http://images.novusbio.com/fullsize/beta-Actin-Antibody-Immunocytochemistry-Immunofluorescence-NB600-503-img0007.jpg)
![Flow Cytometry: beta-Actin Antibody [NB600-503] - Analysis of HeLa cells using mouse Monoclonal beta-Actin antibody (Orange) and Isotype control Antibody (Blue).](http://images.novusbio.com/fullsize/beta-Actin-Antibody-Flow-Cytometry-NB600-503-img0010.jpg)
![Simple Western: beta-Actin Antibody [NB600-503] - Early start GM1 administration did not affect alpha-synuclein expression or transport to the striatum. When assessed 1 week following AAV-A53T alpha-synuclein injection, levels of striatal alpha-synuclein were no different in saline (N=6) vs. GM1-treated animals (N=6), suggesting no influence of GM1 on A53T alpha -synuclein transduction or transport to the striatum. Representative Wes Simple Western blots are shown after cropping (full length images of blots are presented as Supplementary Fig. 2. Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/s41598-019-42847-x), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/beta-Actin-Antibody-Simple-Western-NB600-503-img0014.jpg)
![Western Blot: beta-Actin Antibody [NB600-503] - Regulation of inflammatory signaling in hSMC.ND (open bars) & T2D (solid bars) cells extracted after 48 hr treatment with LPS, Pioglitazone (Pio), palmitate or oleate. Results expressed relative to untreated control for each individual set of cells, Ave + SEM. (A) IkBa protein, n = 7–12 & 6–15 for ND & T2D, respectively. (B) Total & phospho-p38, n = 6–14 & 5–8. (C) Total & phospho-p44/42, n = 7–13 & 7–11. (D) Total & phospho-JNK, n = 9–12 & 3–8. * p<0.05 T2D vs ND. †p<0.05 T2D response vs ND response Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27453994), licensed under a CC0-1.0 license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-503_rabbit-polyclonal-beta-actin-antibody-310202415384161.jpg)
![Western Blot: beta-Actin Antibody [NB600-503] - Impact of T2D on inflammatory signaling in hSMC.Proteins extracted from ND (open bars) & T2D (solid bars) hSMC under control conditions. (A) Representative western blots. (B) Quantification of protein expression normalized to loading control ( beta -actin). Ave + SEM, n = 13–21 for ND, 10–16 for T2D. (C) Protein phosphorylation, expressed as ratio of phosphorylated to total protein. Ave + SEM, n = 13–17 for ND, 9–15 for T2D. *p<0.05 vs ND Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27453994), licensed under a CC0-1.0 license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-503_rabbit-polyclonal-beta-actin-antibody-31020241539452.jpg)
![Western Blot: beta-Actin Antibody [NB600-503] - Early start GM1 administration did not affect alpha -synuclein expression or transport to the striatum. (A,B) When assessed 1 week following AAV-A53T alpha -synuclein injection, levels of striatal alpha -synuclein were no different in saline (N = 6) vs. GM1-treated animals (N = 6), suggesting no influence of GM1 on A53T alpha -synuclein transduction or transport to the striatum. Representative Wes Western blots are shown after cropping (full length images of blots are presented as Supplementary Fig. 2. (C) Double label immunofluorescence 1 week after AAV-A53T alpha -synuclein injection showed no differences between saline & GM1-treated animals in alpha -synuclein accumulation (green) in TH+ neurons (red) in the SNc. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31182727), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-503_rabbit-polyclonal-beta-actin-antibody-310202415175270.jpg)
![Western Blot: beta-Actin Antibody [NB600-503] - Anti-hnRNP A1 antibodies alter protein levels as measured by Western blot. SK-N-SH cells were cultured & treated with anti-hnRNP A1 antibodies or control IgG. Following a 48 hour incubation, cells were lysed & protein lysate was run on 10% Tris-glycine gels for Western blot analysis & probed for Beta-actin (A) or GAPDH (B)) (control), hnRNP A1, SPG4, SPG7, & SPG20. Results revealed that there was a marked reduction of SPG 4 & SPG 7 protein levels in anti-hnRNP A1 antibody compared to control isotype IgG treated cells. There was a variable response to hnRNP A1 protein & a modest reduction of SPG 20. Parentheses show relative percent reduction of signal comparing anti-hnRNP A1 antibody to control isotype IgG treatment of cells. (L=lysate, IgG=control isotype IgG, A1=anti-hnRNP A1-M9 antibody treatment of cells). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27375925), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-503_rabbit-polyclonal-beta-actin-antibody-310202416175268.jpg)
![Lane 1: HeLa cells. Lane 2: mock transfected HeLa cell lysate. Load: 35 ug per lane. Primary antibody: GFP antibody at 1 ug/ml for 1 h at room temperature. Secondary antibody: IRDye(R) 800 conjugated Donkey-a-Goat IgG [H&L] MX7 () secondary antibody at 1:2,500 for 45 min at RT. Block: 5% BLOTTO overnight at 4C. Predicted/Observed size: 27 kDa, 33 kDa for GFP. Other band(s): none.](http://images.novusbio.com/fullsize/nb100-1770_goat-polyclonal-gfp-antibody-25520231310522.jpg)
![Immunocytochemistry/ Immunofluorescence: GFP Antibody [NB100-1770] - Viral recombination of Oxtr in anterior DG hilar neurons impairs discrimination of social, but not non-social, stimuli. a Schematic illustrating viral injection & behavioral testing timeline. b Representative images of Cre & GFP virus infection in aDG. Scale bar, 200 μm. c Representative images & quantifications of cFos immunoreactivity in granule cell layer of aDG (GFP: n = 7, Cre: n = 4). Scale bar, 75 μm. d Behavioral schematic (top) & quantification (bottom) of single object exploration (GFP: n = 11, Cre: n = 6). e Behavioral schematic (top) & quantification (bottom) of novel objection recognition (GFP: n = 11, Cre: n = 6). Quantifications are displayed as Habituation (trials 1–3), Test (trial 4), & discrimination ratio (trial 4). f Behavioral schematic (top) & quantification (bottom) of social exploration test (GFP: n = 11, Cre: n = 6). g Behavioral schematic (top) & quantification (bottom) of social discrimination task (GFP: n = 11, Cre: n = 6). Quantifications are displayed as Habituation (trials 1–3), Test (trial 4), & discrimination ratio (trial 4). All data are displayed as mean ± SEM Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29222469), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-1770_goat-polyclonal-gfp-antibody-310202415525264.jpg)
![Immunohistochemistry: GFP Antibody [NB100-1770] - Macrophages regulate dormancy in tumor cells.a Representative image of triple immunofluorescently stained in E0771-GFP primary tumor tissue for tumor cells, macrophages, & NR2F1. Green = GFP; Red = NR2F1; White = IBA-1; Blue = DAPI. White arrow shows a macrophage. The yellow arrow contact between an NR2F1-positive tumor cell & a macrophage. Mϕ=Macrophage. Scale bar=20 μm. b Quantification showing frequency of distances between NR2F1+ tumor cells to nearest macrophage in primary tumor. Data is normalized to frequency of distances between all DAPI+ nuclei to nearest TMEM. Bar = mean. Error bars = ±SEM. n = 34 fields of view (551 × 316 µm2) in 4 animals. For comparison between 0 & 200 µm bins a two-tailed Mann-Whitney test used (p < 0.0001). ****p < 0.0001. c Representative immunofluorescence images of NR2F1 expression in E0771-GFP tumor cells cultured alone, in direct contact w/ BAC1.2F5 macrophages, or in direct contact w/ HUVEC endothelial cells. White arrows show macrophages or endothelial cells in direct contact w/ a tumor cell. Green = GFP; Red = NR2F1; Blue = DAPI. TC = Tumor Cell. Mϕ = Macrophage. EC = Endothelial Cell. Scale bar = 15 μm. d Percentage of NR2F1-positive tumor cells from each group in C. TC alone: n = 777 cells in 9 independent experiments; TC+Mϕ; n = 226 cells in 6 independent experiments, TC+EC = n = 359 cells in 4 independent experiments. Bar = mean. Error bars = ±SEM. For TC vs. TC+Mϕ (p = 0.0039), & for TC vs. TC+EC (p = 1), a two-tailed Kruskal-Wallis test w/ Dunn’s multiple comparisons adjustment used. For TC+Mϕ vs. TC+EC (0.012), a two-tailed one-way ANOVA w/ Sidak’s multiple comparison adjustment used. *p < 0.05. **p < 0.01; ns = not significant. Source data are provided as a Source Data file. Image collected & cropped by CiteAb from following publication (//pubmed.ncbi.nlm.nih.gov/35110548), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-1770_goat-polyclonal-gfp-antibody-31020241553380.jpg)
![Immunocytochemistry/ Immunofluorescence: GFP Antibody [NB100-1770] - Viral recombination of Oxtr in aCA2/CA3distal impairs discrimination of social, but not non-social, stimuli. a Schematic illustrating viral injection & behavioral testing timeline. b Representative images of Cre & GFP virus infection in aCA2/CA3. Scale bar, 200 μm. c Behavioral schematic (top) & quantification (bottom) of single object exploration (GFP: n = 7, Cre: n = 10). d Behavioral schematic (top) & quantification (bottom) of novel objection recognition (GFP: n = 7, Cre: n = 10). Quantifications are displayed as Habituation (trials 1–3), Test (trial 4), & discrimination ratio (trial 4). e Behavioral schematic (top) & quantification (bottom) of social exploration test (GFP: n = 7, Cre: n = 10). f Behavioral schematic (top) & quantification (bottom) of social discrimination task (GFP: n = 7, Cre: n = 10). Quantifications are displayed as Habituation (trials 1–3), Test (trial 4), & discrimination ratio (trial 4). All data are displayed as mean ± SEM Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29222469), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-1770_goat-polyclonal-gfp-antibody-31020241682115.jpg)
![Immunocytochemistry/ Immunofluorescence: GFP Antibody [NB100-1770] - Transduction of mature retinal ganglion cells.Dissociated retinal ganglion cells (RGCs) isolated from adult rats (a–c), mice (d–f) & zebrafish (g–i) were transduced with baculovirus (bv) encoding fGFP (rat & mice) or DsRed (zebrafish). Representative pictures of vehicle- (-) & bv -treated cultures (a,d,g) visualize transduced RGCs (GFP & DsRed, respectively) that were either co-stained with the neuronal marker beta III-tubulin (Tub, red) at 2 days after transduction (d.a.t) for rat & mice RGCs (a,d) or identified by EGFP expression for zebrafish RGCs at 6 d.a.t. (g). The percentage of transduced RGCs was determined at 1, 2 & 3 days after transduction (d.a.t.) for rat & mice (b,e) & at 4 & 6 d.a.t. for zebrafish (h). Treatment effects compared to vehicle-treated controls: ***p < 0.001, **p < 0.01. Scale bars: 50 μm. RGC survival (c,f,i) was not affected by baculovirus application (bv) compared to vehicle-treated controls (-). (j) Delayed transduction of adult zebrafish RGCs with DsRed-bv after 4 days in culture. Scale bar: 50 μm. (k,l) Co-transduction of adult rat RGCs with fGFP-bv & DsRed-bv. The two viruses were added to retinal cultures simultaneously at half the concentration of single transductions. Representative pictures show co-transduced, fGFP- & DsRed-expressing RGCs (green & red, respectively) that were co-stained against the neuronal marker beta III-tubulin (white) at 2 d.a.t. Scale bar: 50 μm. (k). The percentage of transduced RGCs was determined at 2 & 3 d.a.t. (l). Non-significant difference in co-tranduction efficiency compared to single transductions. Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/srep38928), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-1770_goat-polyclonal-gfp-antibody-31020241612616.jpg)
![Immunocytochemistry/ Immunofluorescence: GFP Antibody [NB100-1770] - Transduction of dorsal root ganglion neurons.Dissociated dorsal root ganglion neurons (DRG) isolated from postnatal (a–c) or adult (d–f) rats & adult mice (g–i) were transduced with fGFP-baculovirus (bv). Representative pictures of vehicle (-) & bv -treated cultures (a,d,g) show transduced, GFP-expressing neurons (green) that were co-stained with the neuronal marker beta III-tubulin (Tub, red) at 2 days after transduction (d.a.t.). The percentage of transduced, GFP-expressing DRG neurons was determined at 1, 2 & 3 d.a.t. (b,e,h), revealing similar transduction efficiencies of 80–90% in postnatal & adult DRG neurons. Cell survival in postnatal (c) & adult (f, i) DRG cultures was not affected by bv-application compared to vehicle-treated controls (-). Scale bars: 100 μm. Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/srep38928), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-1770_goat-polyclonal-gfp-antibody-310202415525262.jpg)
![Immunocytochemistry/ Immunofluorescence: GFP Antibody [NB100-1770] - hnRNPA3 knockout enhances DNA damage in DPR expressing HeLa cells. a Immunocytochemical detection of gamma H2AX foci in GFP-tagged DPR-expressing HeLa WT & A3KO HeLa cells. b Fold change of gamma H2AX foci in HeLa WT & A3KO cells expressing the indicated DPRs relative to HeLa WT cells with GFP expression. N = 47–127 cells from 2 biological replicates. c Immunocytochemical detection of pATM foci in GFP-tagged DPR-expressing HeLa WT & A3KO HeLa cells. d Fold change of pATM foci in HeLa WT & A3KO cells expressing the indicated DPRs relative to HeLa WT cells with GFP expression. N = 71–263 cells from 2 biological replicates. GFP EGFP transfected, GA EGFP-tagged poly-GA 175 repeats transfected, GR EGFP-tagged poly-GR 177 repeats transfected, PR: EGFP-tagged poly-PR 176 repeats transfected. All graphs are shown as mean ± SEM. *p < 0.05, **p < 0.01; one-way ANOVA & Tukey’s post-hoc test. Scale bar 10 μm Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31642962), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-1770_goat-polyclonal-gfp-antibody-310202415541948.jpg)
![Immunohistochemistry-Paraffin: OGG1 Antibody [NB100-106] - Analysis of OGG1 in human skin tissues. Image courtesy of product review by Arash Javeri.](http://images.novusbio.com/fullsize/OGG1-Antibody-Immunohistochemistry-Paraffin-NB100-106-img0023.jpg "Immunohistochemistry-Paraffin: OGG1 Antibody [NB100-106] - Analysis of OGG1 in human skin tissues. Image courtesy of product review by Arash Javeri.")
![Western Blot: OGG1 Antibody [NB100-106] - - Analysis of Ogg1 expression in Jurkat whole cell lysate.](http://images.novusbio.com/fullsize/OGG1-Antibody-Western-Blot-NB100-106-img0024.jpg)
![Immunohistochemistry: OGG1 Antibody [NB100-106] - Figure 5 IHC-P analysis of hOGG1 protein expression in serous ovarian cancer: (A) Normal ovarian tissue treated with anti-hOGG1 antibody, biotinylated anti-rabbit IgG secondary antibody, and avidin-biotin-peroxidase complex, and counterstained with p-dimethylaminobenzaldehyde reagent (magnification 100 x); (B) serous cystadenoma with positive staining (magnification 200 x); (C) LG-SOC tissue with moderate positive staining (magnification 200 x); and (D) HG-SOC with negative staining (magnification 200 x). Black arrow pointed at the immunostained epithelial cells. Image collected and cropped by CiteAb from the following publication (//ovarianresearch.biomedcentral.com/articles/10.1186/1757-2215-6-74), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/OGG1-Antibody-Immunohistochemistry-NB100-106-img0032.jpg)
![Immunocytochemistry/Immunofluorescence: OGG1 Antibody [NB100-106] - A431 cells were fixed for 10 minutes using 10% formalin and then permeabilized for 5 minutes using 1X TBS + 0.5% Triton-X100. The cells were incubated with anti-hOgg1 [NB100-106] at a 1:200 dilution overnight at 4C and detected with an anti-rabbit Dylight 488 (Green) at a 1:500 dilution. Alpha Tubulin (DM1A) [NB100-690] was used as a co-stain at a 1:1000 dilution and detected with an anti-mouse Dylight 550 (Red) at a 1:500 dilution. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 40X objective.](http://images.novusbio.com/fullsize/OGG1-Antibody-Immunocytochemistry-Immunofluorescence-NB100-106-img0020.jpg)
![Immunohistochemistry-Frozen: OGG1 Antibody [NB100-106] - Detection of OGG1 in formaldehyde-fixed frozen sections of the substantia nigra from a Rhesus macaque (Macaca mulatta) using NB100-106 at 10 ug/mL. Photo courtesy of Glen Kisby, Oregon Health Sciences University.](http://images.novusbio.com/fullsize/OGG1-Antibody-Immunohistochemistry-Frozen-NB100-106-img0021.jpg)
![Flow (Intracellular): OGG1 Antibody [NB100-106] - An intracellular stain was performed on HeLa cells with NB100-106C (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 2.5 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to Dylight 650.](http://images.novusbio.com/fullsize/OGG1-Antibody-Flow-Intracellular-NB100-106-img0028.jpg)
![Immunohistochemistry: OGG1 Antibody [NB100-106] - The H&E staining ((a)-(c)) and IHC staining for oxidative DNA damage, 8-oxo-dGuo ((d)-(g)), and DNA repair enzyme hOGG1 ((h)-(j)) in control subjects and tumor and nontumor lesions of BCC patients. Values given are mean +/- SD. The statistical significance of differences between the control and case and between adjacent epidermis and tumor lesions of BCC patients was evaluated by nonparametric variables with Kruskal-Wallis test followed by Dunnett's post hoc test. * P < 0.05, *P < 0.01, *P < 0.001 compared to control; ##P < 0.01, ###P < 0.001 compared to tumor lesions of BCC patients. Image collected and cropped by CiteAb from the following publication (//www.hindawi.com/journals/omcl/2016/5934024/), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/OGG1-Antibody-Immunohistochemistry-NB100-106-img0033.jpg)
![Western Blot: OGG1 Antibody [NB100-106] - The protein expression levels of HVL and LVL sorted cells by western blotting. The ATM, phospho-ATM, GPX2, MRE11, OGG1, and XPC levels were measured by western blot analysis. The figure is representative of three independent experiments. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0164281), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/OGG1-Antibody-Western-Blot-NB100-106-img0034.jpg)
![Immunohistochemistry-Paraffin: OGG1 Antibody [NB100-106] - Comparison of the expression of OGG1 protein in normal colon tissue, polyp and cancer tissue of adenoma (AD, n = 68) and carcinoma (CRC, n = 103) patients. Immunohistochemical detection in paraffin embedded sections stained with hematoxylin and eosin. Center mark in the box indicates the medians of the samples. The length of each box (IQR, interquartile range) represents the range within which the central 50% of the values fell, with the vertical edges placed at the first and third quartiles. Whiskers show variability outside the upper and lower quartiles. P was obtained with the Mann-Whitney test. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0115558), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/OGG1-Antibody-Immunohistochemistry-Paraffin-NB100-106-img0035.jpg)
![Flow Cytometry: OGG1 Antibody [NB100-106] - An intracellular stain was performed on HeLa cells with OGG1 Antibody NB100-106 (blue) and a matched isotype control NBP2-24891 (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 1.0 ug/mL for 30 minutes at room temperature, followed by Rabbit IgG (H+L) Cross-Adsorbed Secondary Antibody, Dylight 550 (SA5-10033, Thermo Fisher).](http://images.novusbio.com/fullsize/OGG1-Antibody-Flow-Cytometry-NB100-106-img0036.jpg)
![Immunohistochemistry: OGG1 Antibody [NB100-106] - Staining of human tonsil, germinal center and mantle zone.](http://images.novusbio.com/fullsize/OGG1-Antibody-Immunohistochemistry-NB100-106-img0022.jpg)
![Flow Cytometry: OGG1 Antibody [NB100-106] - Baseline Ogg1 expression in human PBMC from a healthy donor. Image from verified.customer review.](http://images.novusbio.com/fullsize/OGG1-Antibody-Flow-Cytometry-NB100-106-img0026.jpg)
![Flow Cytometry: OGG1 Antibody [NB100-106] - An intracellular stain was performed on Jurkat Cells with NB100-106 and a matched isotype control. Cells were fixed with 4% PFA and then permeablized with 0.1% saponin. Cells were incubated in an antibody dilution of 2.5 ug/mL for 30 minutes at room temperature, followed by Rabbit IgG (H+L) Cross-Adsorbed Secondary Antibody, Dylight 550.](http://images.novusbio.com/fullsize/OGG1-Antibody-Flow-Cytometry-NB100-106-img0029.jpg)
![Western Blot: OGG1 Antibody - BSA Free [NB100-106] - The protein expression levels of HVL & LVL sorted cells by western blotting.(A) The ATM, phospho-ATM, GPX2, MRE11, OGG1, & XPC levels were measured by western blot analysis. The figure is representative of three independent experiments. (B) The relative fold activity was quantified using AlphaImage software & normalized to the expression of the internal actin control. *P < 0.05, **P < 0.01. Image collected & cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0164281), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-106_rabbit-polyclonal-ogg1-antibody-310202415345339.jpg)
![Immunohistochemistry: OGG1 Antibody - BSA Free [NB100-106] - IHC-P analysis of hOGG1 protein expression in serous ovarian cancer: (A) Normal ovarian tissue treated with anti-hOGG1 antibody, biotinylated anti-rabbit IgG secondary antibody, & avidin-biotin-peroxidase complex, & counterstained with p-dimethylaminobenzaldehyde reagent (magnification 100 x); (B) serous cystadenoma with positive staining (magnification 200 x); (C) LG-SOC tissue with moderate positive staining (magnification 200 x); & (D) HG-SOC with negative staining (magnification 200 x). Black arrow pointed at the immunostained epithelial cells. Image collected & cropped by CiteAb from the following publication (//ovarianresearch.biomedcentral.com/articles/10.1186/1757-2215-6-74), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-106_rabbit-polyclonal-ogg1-antibody-310202415291933.jpg)
![Immunohistochemistry: OGG1 Antibody - BSA Free [NB100-106] - The H&E staining ((a)–(c)) & IHC staining for oxidative DNA damage, 8-oxo-dGuo ((d)–(g)), DNA repair enzyme, hOGG1 ((h)–(k)), & antioxidant proteins, CAT ((l)–(o)), GCLC ((p)–(s)), GPx ((t)–(w)), Nrf2 ((x)–(aa)), & MnSOD ((ab)–(ae)), in control subjects & tumor & nontumor lesions of BCC patients. Values given are mean ± SD. The statistical significance of differences between the control & case & between adjacent epidermis & tumor lesions of BCC patients was evaluated by nonparametric variables with Kruskal-Wallis test followed by Dunnett's post hoc test. ∗P < 0.05, ∗∗P < 0.01, ∗∗∗P < 0.001 compared to control; ##P < 0.01, ###P < 0.001 compared to tumor lesions of BCC patients. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27057281), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-106_rabbit-polyclonal-ogg1-antibody-31020241538247.jpg)
![Immunohistochemistry: OGG1 Antibody - BSA Free [NB100-106] - IHC-P analysis of hOGG1 protein expression in serous ovarian cancer: (A) Normal ovarian tissue treated with anti-hOGG1 antibody, biotinylated anti-rabbit IgG secondary antibody, & avidin-biotin-peroxidase complex, & counterstained with p-dimethylaminobenzaldehyde reagent (magnification 100 x); (B) serous cystadenoma with positive staining (magnification 200 x); (C) LG-SOC tissue with moderate positive staining (magnification 200 x); & (D) HG-SOC with negative staining (magnification 200 x). Black arrow pointed at the immunostained epithelial cells. Image collected & cropped by CiteAb from the following publication (//ovarianresearch.biomedcentral.com/articles/10.1186/1757-2215-6-74), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-106_rabbit-polyclonal-ogg1-antibody-310202415392553.jpg)
![Western Blot: OGG1 Antibody - BSA Free [NB100-106] - EBNA1 promotes the upregulation of oxidative DNA damage repair pathways in EBV converted cell lines & EBV positive BLs. a Representative western blots illustrating the expression of MTH1, OGG1, & MUTYH in pairs of EBV-negative & -positive cell lines. GAPDH was used as loading control. b Densitometry quantification of the specific bands. The intensity of the specific band in EBV positive cells relative the EBV-negative parental is shown. Mean ± SE of four independent experiments. c Representative western blots illustrating the expression of EBNA1, MTH1, OGG1, & MUTYH in the Mutu cell lines. d Densitometry quantification of expression in the EBV positive cell lines relative to the EBV-negative Mutu-30. Mean ± SE of four independent experiments Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31511648), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-106_rabbit-polyclonal-ogg1-antibody-310202415363736.jpg)
![Western Blot: OGG1 Antibody - BSA Free [NB100-106] - EBNA1 promotes the upregulation of oxidative DNA damage repair pathways in EBV converted cell lines & EBV positive BLs. a Representative western blots illustrating the expression of MTH1, OGG1, & MUTYH in pairs of EBV-negative & -positive cell lines. GAPDH was used as loading control. b Densitometry quantification of the specific bands. The intensity of the specific band in EBV positive cells relative the EBV-negative parental is shown. Mean ± SE of four independent experiments. c Representative western blots illustrating the expression of EBNA1, MTH1, OGG1, & MUTYH in the Mutu cell lines. d Densitometry quantification of expression in the EBV positive cell lines relative to the EBV-negative Mutu-30. Mean ± SE of four independent experiments Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31511648), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-106_rabbit-polyclonal-ogg1-antibody-31020241535637.jpg)
![Immunohistochemistry: OGG1 Antibody - BSA Free [NB100-106] - IHC-P analysis of hOGG1 protein expression in serous ovarian cancer: (A) Normal ovarian tissue treated with anti-hOGG1 antibody, biotinylated anti-rabbit IgG secondary antibody, & avidin-biotin-peroxidase complex, & counterstained with p-dimethylaminobenzaldehyde reagent (magnification 100 x); (B) serous cystadenoma with positive staining (magnification 200 x); (C) LG-SOC tissue with moderate positive staining (magnification 200 x); & (D) HG-SOC with negative staining (magnification 200 x). Black arrow pointed at the immunostained epithelial cells. Image collected & cropped by CiteAb from the following publication (//ovarianresearch.biomedcentral.com/articles/10.1186/1757-2215-6-74), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-106_rabbit-polyclonal-ogg1-antibody-310202415293311.jpg)
![Immunohistochemistry: OGG1 Antibody - BSA Free [NB100-106] - IHC-P analysis of hOGG1 protein expression in serous ovarian cancer: (A) Normal ovarian tissue treated with anti-hOGG1 antibody, biotinylated anti-rabbit IgG secondary antibody, & avidin-biotin-peroxidase complex, & counterstained with p-dimethylaminobenzaldehyde reagent (magnification 100 x); (B) serous cystadenoma with positive staining (magnification 200 x); (C) LG-SOC tissue with moderate positive staining (magnification 200 x); & (D) HG-SOC with negative staining (magnification 200 x). Black arrow pointed at the immunostained epithelial cells. Image collected & cropped by CiteAb from the following publication (//ovarianresearch.biomedcentral.com/articles/10.1186/1757-2215-6-74), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-106_rabbit-polyclonal-ogg1-antibody-310202415175230.jpg)
![Western Blot: OGG1 Antibody - BSA Free [NB100-106] - Immunoblot analysis of kidney lysates.(A) Blot membranes were incubated with the antibodies against Nrf2, p53 & 8-oxoguanine glycosylase alpha (OGG1 alpha ). The mean integrated optical density is related to actin for Nrf2 (B), p53 (C) & mature 8-oxoguanine glycosylase alpha (D) levels. Results are given as a mean ± S.E.M. KD4, KD6, KD8 – groups of Eker rats (Tsc2+/−) treated with HFKD for four, six or eight mo., respectively; ST – Eker rats fed with a standard diet; LE ST – wild-type Long Evans rats treated with a standard diet; LE KD – wild-type Long Evans rats treated with a ketogenic diet similarly to the KD6 group. *P < 0.05, **p < 0.01, ***p < 0.001 as compared to ST unless otherwise stated (horizontal line) for ANOVA with a Fisher post hoc test. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26892894), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-106_rabbit-polyclonal-ogg1-antibody-31020241537192.jpg)
![Western Blot: OGG1 Antibody - BSA Free [NB100-106] - EBNA1 expression is associated with upregulation of MTH1 & oxidative damage repair pathways. The expression of MTH1, OGG1, & MUTYH was investigated by western blots & qPCR in BJAB-tTAE1 cells upon addition & withdrawal of doxycycline. a Representative western blots illustrating the correlation between the reversible down- & upregulation of MTH1 & EBNA1 in BJAB-tTAE1 cells upon addition & withdrawal of doxycycline. GAPDH was used as loading control. b Densitometry quantification of MTH1 & EBNA1 expression in BJAB-tTAE1 cells. The mean intensity of the MTH1 & EBNA1 specific bands relative to GAPDH in three independent experiments is shown in the figure. c Regression analysis of the relationship between expression levels of MTH1 & EBNA1. The data from three independent experiments were used for the plot. d Representative western blots illustrating the expression of MTH1, MUTYH, & OGG1 in BJAB-tTAE1 cells cultured for two weeks in the presence or absence of doxycycline. e Fold change is the ratio between the intensity of the specific band in cells cultured without or with doxycycline. The mean ± SD of four independent experiments is shown. f qPCR analysis of the levels of MTH1, OGG1, & MUTYH transcripts in BJAB-tTAE1 cells cultured for 2 weeks in the presence or absence of doxycycline. The mean ± SE of the fold change in six independent experiments each performed in triplicate is shown Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31511648), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-106_rabbit-polyclonal-ogg1-antibody-3102024155529.jpg)
![Western Blot: OGG1 Antibody - BSA Free [NB100-106] - The antioxidant pathways are activated during EBV infection & are required for growth transformation. Freshly isolated B-lymphocytes infected with the transforming B95-8 strain of EBV were cultured for up to 2 weeks in the presence or absence of MTH1 inhibitors. Protein expression was monitored by western blots, cell proliferation & activation of the DDR were assessed by 3H-Thy incorporation & staining for gamma H2AX, respectively. a representative western blots illustrating the parallel increase of MTH1 & EBNA1 expression following EBV infection & mean ± SE of the intensity of the MTH1 specific band in five independent experiments. b Representative western blots illustrating the expression of MTH1, MUTYH & OGG1 in ex vivo untreated B-cell & freshly EBV infected & SAC induced B blasts cultured for comparable times & showing similar levels of cell proliferation. c Quantification of the specific bands. Relative expression is the ration between the intensity in the treated cells versus freshly harvested cells. The mean ± SE of three to four independent experiments is shown. d Inhibition of MTH1 prevents the establishment of EBV transformed lymphoblastoid cell lines. 3H-Thy incorporation was measured after culture of freshly EBV infected B-lymphocytes in the presence of the indicated amounts of MTH1 inhibitors. Depending on the condition of the cultures harvesting was done after ten to fifteen days. e Inhibition of MTH1 strongly enhances the induction of DNA damage in freshly EBV infected cells. DNA damage was detected by gamma H2AX staining. f Mean ± SE of the % gamma H2AX positive cells in three independent experiments. *P < 0.05; **P < 0.01 Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31511648), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-106_rabbit-polyclonal-ogg1-antibody-310202415523940.jpg)
![Immunohistochemistry: OGG1 Antibody - BSA Free [NB100-106] - Comparison of the expression of OGG1 (A) & PARP-1 (B) protein in normal colon tissue, polyp & cancer tissue of adenoma (AD, n = 68) & carcinoma (CRC, n = 103) patients.Immunohistochemical detection in paraffin embedded sections stained with hematoxylin & eosin. Center mark in the box indicates the medians of the samples. The length of each box (IQR, interquartile range) represents the range within which the central 50% of the values fell, with the vertical edges placed at the first & third quartiles. Whiskers show variability outside the upper & lower quartiles. P was obtained with the Mann-Whitney test. Representative examples of the levels of PARP-1 protein in tissues of CRC patients determined by Western analysis. The analysis was performed on tumor & normal tissues of 41 CRC patients (C). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/25526641), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-106_rabbit-polyclonal-ogg1-antibody-3102024165727.jpg)
![Western Blot: OGG1 Antibody - BSA Free [NB100-106] - HDAC1 modulates OGG1 activity.a, b Representative images & quantification of OGG1 acetylation assessed by WB analysis using anti-acetylated lysine (Ac-Lysine, 4G12). Recombinant OGG1 (100 ng) first acetylated by p300 (25 ng), & incubated w/ titrated amount of HDAC1 (25 & 50 ng). a, b Four replicates from four independent experiments. c Reaction scheme of OGG1 cleavage assay. 5′IRDye800CW-labeled oligonucleotides (33 nt) contain an 8-oxoG base at position 17 & complementary unlabeled strand used as OGG1 substrate. Recombinant OGG1 proteins incubated w/ OGG1 substrate & resolved by 20% denaturing urea PAGE. d, e Representative images & quantification of OGG1 cleavage activity on reaction samples shown in Fig. 3a. d, e Seven replicates from four independent experiments. Nuclear extracts from HEK cells overexpressing OGG1 used as a positive control. f Co-immunoprecipitation of OGG1 w/ HDAC1 in cortical nuclear extracts from 2-month-old wild-type mice (n = 2) from one experiment. The asterisks indicate nonspecific cross-reaction w/ IgG heavy & light chains. g, h Representative images & quantification of acetylation status of endogenous OGG1 in hippocampal lysates of 13M control (n = 4) & Hdac1 cKO (n = 4) animals. g, h Two independent experiments. i Representative images of OGG1 cleavage assay using hippocampal nuclear extracts of 13M control & Hdac1 cKO mice. j Quantification of cleaved 17-nt products after OGG1 cleavage assay using hippocampal nuclear extracts of 13M control (n = 6) & Hdac1 cKO (n = 4) animals. i, j Two independent experiments. All values are shown as mean ± SEM. Statistical analysis: b, e one-way ANOVA w/ Tukey’s post hoc test; h, j two-tailed Student’s t test. Source data are provided as a Source Data file. Image collected & cropped by CiteAb from following publication (//pubmed.ncbi.nlm.nih.gov/32424276), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-106_rabbit-polyclonal-ogg1-antibody-31020241682186.jpg)
![Western Blot: 53BP1 Antibody - BSA Free [NB100-904] - WRAP53beta plays an important role in recruitment of factors involved in HR and NHEJ to DNA breaks in A2780 cells. A2780 cells were transfected with siControl or siWRAP53#2 oligonucleotides for 48 h; exposed to IR (6 Gy), and 1 h later immunostained for WRAP53beta, gamma-H2AX, MDC1, RNF168, 53BP1, RAD51 and beta-actin. We could not assess the protein levels of BRCA1 due to a lack of antibodies that work for western blotting. The observed molecular weight is 275 kDa and the theoretical molecular weight for the whole endogenous protein is 214 kDa. Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/cddis2015250) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/53BP1-Antibody---BSA-Free-Western-Blot-NB100-904-img0015.jpg "Western Blot: 53BP1 Antibody - BSA Free [NB100-904] - WRAP53beta plays an important role in recruitment of factors involved in HR and NHEJ to DNA breaks in A2780 cells. A2780 cells were transfected with siControl or siWRAP53#2 oligonucleotides for 48 h; exposed to IR (6 Gy), and 1 h later immunostained for WRAP53beta, gamma-H2AX, MDC1, RNF168, 53BP1, RAD51 and beta-actin. We could not assess the protein levels of BRCA1 due to a lack of antibodies that work for western blotting. The observed molecular weight is 275 kDa and the theoretical molecular weight for the whole endogenous protein is 214 kDa. Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/cddis2015250) licensed under a CC-BY license.")
![Immunocytochemistry/Immunofluorescence: 53BP1 Antibody - BSA Free [NB100-904] - NIH3T3 cells were fixed in 4% paraformaldehyde for 10 minutes and permeabilized in 0.5% Triton X-100 in PBS for 5 minutes. The cells were incubated with anti- NB100-904 at 2 ug/ml overnight at 4C and detected with an anti-rabbit Dylight 488 (Green) at a 1:1000 dilution for 60 minutes. Alpha tubulin (DM1A) NB100-690 was used as a co-stain at a 1:1000 dilution and detected with an anti-mouse Dylight 550 (Red) at a 1:1000 dilution. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 100X objective and digitally deconvolved.](http://images.novusbio.com/fullsize/53BP1-Antibody---BSA-Free-Immunocytochemistry-Immunofluorescence-NB100-904-img0021.jpg)
![Immunohistochemistry: 53BP1 Antibody - BSA Free [NB100-904] - Staining of 53BP1 in human renal cancer cells using DAB with hematoxylin counterstain.](http://images.novusbio.com/fullsize/53BP1-Antibody---BSA-Free-Immunohistochemistry-NB100-904-img0008.jpg)
![Flow Cytometry: 53BP1 Antibody - BSA Free [NB100-904] - An intracellular stain was performed on Ntera2 cells with 53BP1 Antibody NB100-904 (blue) and a matched isotype control NBP2-24891 (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 1.0 ug/mL for 30 minutes at room temperature, followed by Rabbit IgG (H+L) Cross-Adsorbed Secondary Antibody, Dylight 550 (SA5-10033, Thermo Fisher).](http://images.novusbio.com/fullsize/53BP1-Antibody---BSA-Free-Flow-Cytometry-NB100-904-img0022.jpg)
![Western Blot: 53BP1 Antibody - BSA Free [NB100-904] - Western blot analysis of untreated U2OS cell lysate blotted with 53BP1 Antibody. The observed molecular weight here is ~220 kDa, and the theoretical molecular weight is 214 kDa.](http://images.novusbio.com/fullsize/53BP1-Antibody---BSA-Free-Western-Blot-NB100-904-img0011.jpg)
![<b>Biological Strategies Validation. </b>Immunocytochemistry/Immunofluorescence: 53BP1 Antibody - BSA Free [NB100-904] - AR suppression treatment suppresses DNA damage repair. (A) Cells were treated with AR suppression for 24 h followed by 2 Gy of IR treatment. Representative images of phospho-H2A histone family member X ( -H2AX) and p53-binding protein 1 (53BP1) staining 24 h post-IR of LNCaP cells (scale bar 10 um). Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31635359/) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/53BP1 Antibody - BSA Free-Immunocytochemistry-Immunofluorescence-NB100-904-img0023.jpg)
![Immunocytochemistry/Immunofluorescence: 53BP1 Antibody - BSA Free [NB100-904] - Immunofluorescence of 53BP1 Antibody in HeLa cells. Image from verified customer review.](http://images.novusbio.com/fullsize/53BP1-Antibody---BSA-Free-Immunocytochemistry-Immunofluorescence-NB100-904-img0009.jpg)
![Immunocytochemistry/Immunofluorescence: 53BP1 Antibody - BSA Free [NB100-904] - Immunofluorescence of 53BP1 Antibody in C33A cells. Image from verified customer review.](http://images.novusbio.com/fullsize/53BP1-Antibody---BSA-Free-Immunocytochemistry-Immunofluorescence-NB100-904-img0012.jpg)
![Immunocytochemistry/Immunofluorescence: 53BP1 Antibody - BSA Free [NB100-904] - HeLa cells were fixed for 10 minutes using 10% formalin and then permeabilized for 5 minutes using 1X PBS + 0.5% Triton X-100. The cells were incubated with 53BP1 Antibody conjugated to Alexa Fluor 488 (Catalog #NB100-904AF488) at 10ug/mL for 1 hour at room temperature. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 40X objective.](http://images.novusbio.com/fullsize/53BP1-Antibody---BSA-Free-Immunocytochemistry-Immunofluorescence-NB100-904-img0013.jpg)
![Immunocytochemistry/Immunofluorescence: 53BP1 Antibody - BSA Free [NB100-904] - Ntera2 cells were fixed in 4% paraformaldehyde for 10 minutes and permeabilized in 0.5% Triton X-100 in PBS for 5 minutes. The cells were incubated with anti-53BP1 Antibody NB100-904 at 2 ug/ml overnight at 4C and detected with an anti-rabbit Dylight 488 (Green) at a 1:1000 dilution for 60 minutes. Alpha tubulin (DM1A) NB100-690 was used as a co-stain at a 1:1000 dilution and detected with an anti-mouse Dylight 550 (Red) at a 1:1000 dilution. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 100X objective and digitally deconvolved.](http://images.novusbio.com/fullsize/53BP1-Antibody---BSA-Free-Immunocytochemistry-Immunofluorescence-NB100-904-img0019.jpg)
![Flow Cytometry: 53BP1 Antibody - BSA Free [NB100-904] - An intracellular stain was performed on HeLa cells (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 5 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to DyLight 550.](http://images.novusbio.com/fullsize/53BP1-Antibody---BSA-Free-Flow-Cytometry-NB100-904-img0014.jpg)
![Flow Cytometry: 53BP1 Antibody - BSA Free [NB100-904] - An intracellular stain was performed on HeLa cells with 53BP1 Antibody (Catalog #NB100-904AF647) (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 2.5 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to Alexa Fluor 647.](http://images.novusbio.com/fullsize/53BP1-Antibody---BSA-Free-Flow-Cytometry-NB100-904-img0017.jpg)
![Flow Cytometry: 53BP1 Antibody - BSA Free [NB100-904] - An intracellular stain was performed on HeLa cells with 53BP1 Antibody (Catalog #NB100-904C) (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 2.5 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to DyLight 650.](http://images.novusbio.com/fullsize/53BP1-Antibody---BSA-Free-Flow-Cytometry-NB100-904-img0018.jpg)
![Immunocytochemistry/ Immunofluorescence: 53BP1 Antibody - BSA Free [NB100-904] - Chromatin opening activates DDR via a mechanism that requires catalytically functional LOXL2 but can be independent of DNA damage. d gamma -H2AX & 53BP1 staining & foci quantification are shown after immunofluorescence w/ indicated antibodies in non-replicative conditions. Dot graphs indicate number of gamma -H2AX (left graph) & 53BP1 (right graph) foci in control & LOXL2 KD cells. Image collected & cropped by CiteAb from following publication (//pubmed.ncbi.nlm.nih.gov/31462706), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-904_rabbit-polyclonal-53bp1-antibody-31020241535691.jpg)
![Immunocytochemistry/ Immunofluorescence: 53BP1 Antibody - BSA Free [NB100-904] - Integrin-associated proteins affected cell cycle & DNA double strand repairA. Western blot & B. densitometric analysis of p53-wildtype A172 & U87MG cells 48 h after PINCH1, ILK or ILKAP knockdown. Non-specific siRNA served as the control. C. Percentage of BrdU positivity as a marker for S-phase cells at different time points after siRNA transfection. Representative images are shown. D. Immunofluorescence staining of 53BP1 (green) & gamma H2AX (red) & E. quantitative analysis of foci numbers in irradiated A172 & U87MG cells after PINCH1, ILK or ILKAP depletion. Nuclei were stained with DAPI (blue). Data are mean ± SD (n = 3; t-test; *P 10 IR-induced foci. Means±S.D. are shown, n=3. *P-value200 cells were counted per experiment). Expression levels of BRCA1 & 53BP1 were assessed by Western Blot on whole cell extracts 4 days after doxycycline treatment. A representative picture is shown in (C). The migration positions of molecular weight standards (in kDa) are indicated on the left. (D) Quantification of 3 Western blot experiments. Image collected & cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0123333), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-904_rabbit-polyclonal-53bp1-antibody-310202416284918.jpg)
![Immunocytochemistry/ Immunofluorescence: 53BP1 Antibody - BSA Free [NB100-904] - hWDR76 interaction network & subnuclear localization suggest conservation of Cmr1 function.(a) Domain organization of Cmr1 & human WDR76. Human WDR76 shares 29% sequence similarity with Cmr1 from S. cerevisiae. Filled boxes indicate WD40 repeats. NLS, putative nuclear localization signal. (b) Human WDR76 interacts with HELLS, SUGT1, XRCC5, XRCC6 & the CCT–TRiC complex. SILAC-labelled HeLa cells were transfected with GFP-WDR76 or empty vector. GFP-WDR76 & its interacting proteins were enriched using GFP-Trap resin. Proteins were resolved by SDS–PAGE & digested in-gel with trypsin. Peptides were analysed on a quadrupole Orbitrap mass spectrometer. The plot shows log(10) SILAC ratios of proteins associated with GFP-WDR76 compared with background. WDR76 is highlighted in red & several other interactors are also indicated. (c) Human WDR76 localizes into nuclear foci. Twenty-four hours after GFP-WDR76 transfection, U2OS cells were treated with 10 μM MG132 or 1.5 mM MMS for 2 h. Immunofluorescence analyses of 53BP1 were performed with anti-53BP1 antibody. DAPI was used to stain nuclei. Scale bar, 20 μm. (d) Human WDR76 does not co-localize with PCNA. Stably expressing RFP-PCNA U2OS cells were transfected with GFP-WDR76. 24 h after transfection, cells were fixed & stained with DAPI. Scale bar, 20 μm. (e) Model for the role of Cmr1 in promoting replication recovery. See Discussion for details. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/25817432), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-904_rabbit-polyclonal-53bp1-antibody-310202416284913.jpg)
![Immunocytochemistry/ Immunofluorescence: 53BP1 Antibody - BSA Free [NB100-904] - Overexpression of RNF8 restores repair of DNA double-strand breaks in splicing-deficient cells. (a) U2OS cells were treated with DMSO, pladienolide B or isoginkgetin for 16 h, irradiated (6 Gy, 1 h recovery) 1 h prior to termination of this treatment, & then subjected to western blotting for H2A, RNF8 & beta -actin. (b & c) U2OS cells were transfected with either GFP-RNF8 or GFP-Empty for 2 h, followed by addition of pladienolide B, isoginkgetin or DMSO, incubation for an additional 5 h, irradiation with 6 Gy, fixation 1 h later, & immunostaining for (b) conjugated ubiquitin (FK2 antibody) & (c) 53BP1. The numbers in white indicate the percentage of 100 transfected, i.e, green cells whose nuclei contained >10 IR-induced foci. Means±S.D. are shown, n=3. (d) U2OS cells were treated as above, except that fixation was performed 24 h after irradiation & the immunostaining was for gamma H2AX. Again, the white numbers indicate the percentage of 100 transfected, i.e, green cells whose nuclei contained >10 gamma H2AX foci. Means±S.D. are shown, n=3. (e) The efficiency of HR measured in direct repeated-GFP U2OS cells transfected with I-SceI in combination with either Flag-Empty or Flag-RNF8 for 24 h, followed by addition of DMSO or pladienolide B & incubation for another 24 h. Means±S.D. are shown, n=3. *P200 cells were counted per experiment). Expression levels of BRCA1 & 53BP1 were assessed by Western Blot on whole cell extracts 4 days after doxycycline treatment. A representative picture is shown in (C). The migration positions of molecular weight standards (in kDa) are indicated on the left. (D) Quantification of 3 Western blot experiments. Image collected & cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0123333), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-904_rabbit-polyclonal-53bp1-antibody-310202416284924.jpg)
![Immunocytochemistry/ Immunofluorescence: 53BP1 Antibody - BSA Free [NB100-904] - WRAP53 beta plays an important role in recruitment of factors involved in HR & NHEJ to DNA breaks in A2780 cells. (a) A2780 cells were transfected with siControl or siWRAP53#2 oligonucleotides for 48 h; exposed to IR (6 Gy), & 1 h later immunostained for gamma H2AX, MDC1, RNF168, FK2 (recognizes conjugated ubiquitin), BRCA1, 53BP1 & RAD51. (b) Quantification of the results in (a), as the percentage of 200 cells counted in each experiment whose nuclei contained >10 IR-induced foci. The error bars depict the S.E.M.; n=3, **P<0.01 & ***P<0.001, as determined by Student's t-test. (c) A2780 cells were treated as in (a) & then subjected to western blotting for WRAP53 beta , gamma H2AX, MDC1, RNF168, 53BP1, RAD51 & beta -actin. We could not assess the protein levels of BRCA1 due to a lack of antibodies that work for western blotting Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26426684), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-904_rabbit-polyclonal-53bp1-antibody-31020241628493.jpg)
![Immunohistochemistry-Paraffin: ATM Antibody (2C1) [NB100-309] - Human Testis (formalin-fixed, paraffin-embedded) stained with ATM antibody (2C1) [NB100-309] at 5 ug/ml followed by biotinylated anti-mouse IgG secondary antibody, alkaline phosphatase-streptavidin and chromogen.](http://images.novusbio.com/fullsize/ATM-Antibody-2C1-Immunohistochemistry-Paraffin-NB100-309-img0011.jpg "Immunohistochemistry-Paraffin: ATM Antibody (2C1) [NB100-309] - Human Testis (formalin-fixed, paraffin-embedded) stained with ATM antibody (2C1) [NB100-309] at 5 ug/ml followed by biotinylated anti-mouse IgG secondary antibody, alkaline phosphatase-streptavidin and chromogen.")
![Western Blot: ATM Antibody (2C1) [NB100-309] - Detection of human ATM protein using ATM antibody (2C1) [NB100-309] by western blot or immunoprecipitation. Theoretical molecular weight 351 kDa.](http://images.novusbio.com/fullsize/ATM-Antibody-2C1-Western-Blot-NB100-309-img0018.jpg)
![Immunohistochemistry-Paraffin: ATM Antibody (2C1) [NB100-309] - Human breast carcinoma. ATM stained by ATM antibody [2C1] diluted at 1:100.Antigen Retrieval: Citrate buffer, pH 6.0, 15 min.](http://images.novusbio.com/fullsize/ATM-Antibody-2C1-Immunohistochemistry-Paraffin-NB100-309-img0021.jpg)
![Western Blot: ATM Antibody (2C1) [NB100-309] - Analysis of ATM in U2OS sarcoma cells using ATM antibody (2C1) [NB100-309]. Theoretical molecular weight 351 kDa. Western blot image submitted by a verifeid customer review.](http://images.novusbio.com/fullsize/ATM-Antibody-2C1-Western-Blot-NB100-309-img0010.jpg)
![Immunohistochemistry-Paraffin: ATM Antibody (2C1) [NB100-309] - Human Kidney (formalin-fixed, paraffin-embedded) stained with ATM antibody (2C1) [NB100-309] at 5 ug/ml followed by biotinylated anti-mouse IgG secondary antibody, alkaline phosphatase-streptavidin and chromogen.](http://images.novusbio.com/fullsize/ATM-Antibody-2C1-Immunohistochemistry-Paraffin-NB100-309-img0012.jpg)
![<b>Genetic Strategies Validation. </b>Western Blot: ATM Antibody (2C1) [NB100-309] - Non-transfected (-) and transfected (+) HeLa whole cell extracts (60 ug) were separated by 5% SDS-PAGE, and the membrane was blotted with ATM antibody (2C1) [NB100-309] diluted at 1:500.](http://images.novusbio.com/fullsize/ATM-Antibody-2C1-Knockdown-Validated-NB100-309-img0017.jpg)
![<b>Genetic Strategies Validation. </b>Western Blot: ATM Antibody (2C1) [NB100-309] - Methylated EDSBs may be repaired by an ATM-dependent pathway. Immunoblots of ATM and DNA-PKcs in ATM shRNA-transfected HeLa cells, using ATM antibody (2C1) [NB100-309]. GAPDH is included as a loading control. Image collected and cropped by CiteAb from the following publication (//molecular-cancer.biomedcentral.com/articles/10.1186/1476-4598-9-70), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/ATM-Antibody-2C1-Western-Blot-NB100-309-img0019.jpg)
![Immunoprecipitation: ATM Antibody (2C1) [NB100-309] - MDA-MB-231 whole cell lysates were immunoprecipitated with 2 ug ATM Antibody (NB100-309), followed by Western blot (primary antibody: NB100-309 at 1:1000, 4C overnight. Western blot image submitted by a verified customer review.](http://images.novusbio.com/fullsize/ATM-Antibody-2C1-Western-Blot-NB100-309-img0020.jpg)
![<b>Biological Strategies Validation. </b>Western Blot: ATM Antibody (2C1) [NB100-309] - MCELNs decreased the DNA damage of H9C2 cells after radiation. Western blot images of p-ATM (NB100-306) and ATM (NB100-309) in H9C2 cells after 48 h of culture with indicated treatment. IR (-/+): 0/16 Gy X-ray; MCELNs (-/+): 0/10 ug/mL. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35509278/) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/nb100-309_mouse-monoclonal-atm-antibody-2c1-25520231514910.jpg)
![Western Blot: ATM Antibody (2C1) [NB100-309] - Western blot analysis of the extent of knockdown MRE11 & ATM, & the lack of effect of Mirin activation of ATM. The extent of shRNA-mediated knockdown of MRE11 & ATM are shown for (A) clones GFP-7F1 & GFP-6D1 & (B) clones EDS-7F2 & EDS-6J8. The extent of knockdown was determined by analyzing the intensity of the ATM & MRE11 bands relative to the intensity of the loading control GAPDH bands (see Table 1). (C) The effect of Mirin on activation of ATM was determined by analysis of phosphorylation of ATM in response to ionizing radiation. Cultures treated with DMSO alone, 20 μM Mirin, or knockdown of ATM were analyzed by western blot 30 min after exposure to 10 Gy of ionizing radiation. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26209132), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-309_mouse-monoclonal-atm-antibody-2c1-310202415371910.jpg)
![Western Blot: ATM Antibody (2C1) [NB100-309] - Rac1 inhibition abolishes IR-induced activation of both ATM & ATR signaling. (A) MCF-7 cells were treated with/without 20-Gy IR in the presence or absence of 100 μM NSC23766 & incubated for 1 hour at 37°C before analysis. To assess the ATM kinase activity, ATM was immunoprecipitated from cell lysate by using anti-ATM antibody (2C1) & assayed for ATM activity by using p53 recombinant protein as substrate. To measure the Chk2 activity, Chk2 was immunoprecipitated from cell lysate by using B-4 anti-Chk2 antibody & assayed for Chk2 activity by using Cdc25C recombinant protein as substrate. As controls, ATM & Chk2 protein levels in the immunoprecipitates (IP-WB) as well as in cell lysates (WB) were assessed with immunoblotting. (B) ATR & Chk1 were immunoprecipitated from cell lysates by using N-19 anti-ATR & G-4 anti-Chk1 antibody, respectively. ATR activity was assayed by using p53 recombinant protein substrate, & Chk1 activity assayed by using Cdc25C recombinant protein substrate. As controls, ATR & Chk1 protein levels in the immunoprecipitates (IP-WB), as well as in cell lysates (WB) were assessed with immunoblotting. (C) MCF-7 cells were exposed to IR at the indicated doses in the presence or absence of NSC23766, incubated for 1 hour, & assessed for Chk1 & Chk2 activities. *Kinase assay does not contain Cdc25C substrate. (D) T47D & ZR-75-1 cells were exposed to 10-Gy IR in the presence or absence of 100 μM NSC23766, incubated for 1 hour, & analyzed for Chk1 & Chk2 activities. Image collected & cropped by CiteAb from the following publication (//breast-cancer-research.biomedcentral.com/articles/10.1186/bcr3164), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-309_mouse-monoclonal-atm-antibody-2c1-310202415535119.jpg)
![Western Blot: ATM Antibody (2C1) [NB100-309] - Inhibition of Rac1 by N17Rac1 mutant or Rac1 siRNA diminishes IR-induced G2/M checkpoint activation. (A) MCF-7 cells were infected with Ad.N17Rac1 or Ad.Control for 24 hours & exposed to 15-Gy IR. Left panel: the cells were analyzed for DNA content 24 hours after IR. The result depicts the percentage of cells with 4N-DNA content & is shown as mean ± SD of quadruplicate samples. *P < 0.001 (n = 4), significant difference from the irradiated Ad.Control-infected cells. Right panel: Inset: at 15 minutes after IR, the infected cells were analyzed for Rac1 activities (Rac1-GTP) & protein levels (total Rac1). Bar graph: mitotic cells in the cell samples were analyzed 2 hours after IR. The result depicts the percentage of mitotic cells & is shown as mean ± SD of triplicate samples. **P = 0.002 (n = 3), significant difference from the irradiated Ad.Control-infected cells. (B) Upper panel: MCF-7 cells transfected with Rac1 siRNA (Rac1) or control siRNA (Control) were incubated for the indicated times & analyzed for protein levels of Rac1 & Actin. Lower panel: After 2-day incubation, the siRNA-transfected cells were exposed to IR, incubated for 24 hours, & assessed for DNA content. Results depict the percentage of cells with 4N-DNA content & represent the mean ± SD of three separate experiments in duplicate samples. *P < 0.001 (n = 6), significant difference from the irradiated Control-siRNA transfected cells. (C) After 2-day incubation, siRNA-transfected cells were treated with/without 20-Gy IR, incubated for 1 hour, & analyzed for ATM, ATR, Chk1, & Chk2 activities. Image collected & cropped by CiteAb from the following publication (//breast-cancer-research.biomedcentral.com/articles/10.1186/bcr3164), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-309_mouse-monoclonal-atm-antibody-2c1-310202415525285.jpg)
![Western Blot: ATM Antibody (2C1) [NB100-309] - HeLa whole cell extract and nuclear extracts (30 ug) were separated by 5% SDS-PAGE, and the membrane was blotted with ATM antibody [2C1] (NB100-309) diluted at 1:500. The HRP-conjugated anti-mouse IgG antibody was used to detect the primary antibody.](http://images.novusbio.com/fullsize/nb100-309_mouse-monoclonal-atm-antibody-2c1-91020242041241.jpg)
![Western Blot: ATM Antibody (2C1) [NB100-309] - Whole cell extract (30 ug) was separated by 5% SDS-PAGE, and the membrane was blotted with ATM antibody [2C1] (NB100-309) diluted at 1:1000.](http://images.novusbio.com/fullsize/nb100-309_mouse-monoclonal-atm-antibody-2c1-91020242063311.jpg)
![Western Blot: ATM Antibody [NB100-104] - Detection of ATM in HeLa nuclear extract using ATM antibody [NB100-104]. Theoretical molecular weight 351 kDa.](http://images.novusbio.com/fullsize/ATM-Antibody-Western-Blot-NB100-104-img0009.jpg "Western Blot: ATM Antibody [NB100-104] - Detection of ATM in HeLa nuclear extract using ATM antibody [NB100-104]. Theoretical molecular weight 351 kDa.")
![Immunohistochemistry-Paraffin: ATM Antibody [NB100-104] - Staining of human tonsil, germinal center and mantle zone with ATM Antibody [NB100-104].](http://images.novusbio.com/fullsize/ATM-Antibody-Immunohistochemistry-Paraffin-NB100-104-img0014.jpg)
![<b>Biological Strategies Validation. </b>Immunocytochemistry/Immunofluorescence: ATM Antibody [NB100-104] - GM00637 cells with KU55933 pretreatment (a) were exposed to 50 uM spermidine or CCCP, followed by immunofluorescence analyses of total and p-ATM on Ser-1981. The scale bar is 10 um. Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/srep24700) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/ATM-Antibody-Immunocytochemistry-Immunofluorescence-NB100-104-img0018.jpg)
![Flow Cytometry: ATM Antibody [NB100-104] - An intracellular stain was performed on HeLa cells with Dylight 550-conjugated ATM Antibody [NB100-104R] (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 5 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to DyLight 550.](http://images.novusbio.com/fullsize/ATM-Antibody-Flow-Cytometry-NB100-104-img0016.jpg)
![<b>Biological Strategies Validation. </b>Western Blot: ATM Antibody [NB100-104] - Analysis of double strand break repair in MCF-7 monolayer and mammosphere populations. Expression of proteins involved in the NHEJ pathway of DSB repair in response to increasing doses of ionizing radiation. Lysates were prepared from unirradiated cells and from cells harvested one hour after exposure to 1 or 10-Gy 60Co I3-radiation and analyzed by immunoblotting with antibodies against several DSB repair proteins. Phospho-ATM and phospho-DNA-PKcs refer to phosphorylation of these proteins at Ser1981 and Ser2056, respectively. Actin served as a loading control. Image collected and cropped by Citeab from the following publication (Senescence evasion by MCF-7 human breast tumor-initiating cells. Breast Cancer Res (2010)) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/ATM-Antibody-Western-Blot-NB100-104-img0017.jpg)
![Western Blot: ATM Antibody [NB100-104] - Detection of ATM in Raji whole cell lysate using [NB100-104]. Observed molecular weight ~300 kDa. Theoretical molecular weight 351 kDa.](http://images.novusbio.com/fullsize/ATM-Antibody-Western-Blot-NB100-104-img0001.jpg)
![Immunocytochemistry/Immunofluorescence: ATM Antibody [NB100-104] - HeLa cells were fixed for 10 minutes using 10% formalin and then permeabilized for 5 minutes using 1X TBS + 0.05% Triton X-100. Then cells were incubated with [NB100-104] at a 1:100 dilution overnight at 4C and detected with an anti-rabbit DyLight 488 (Green) at a 1:500 dilution. Alpha tubulin was used as a co-stain at a 1:1000 dilution and detected with an anti-mouse DyLight 550 (Red) at a 1:500 dilution. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 40X objective.](http://images.novusbio.com/fullsize/ATM-Antibody-Immunocytochemistry-Immunofluorescence-NB100-104-img0011.jpg)
![Flow Cytometry: ATM Antibody [NB100-104] - Analysis of PE conjugate of ATM Antibody [NB100-104PE]. An intracellular stain was performed on HeLa cells with ATM antibody [NB100-104PE] (blue) and a matched isotype control [NBP2-24893PE] (orange). Cells were fixed with 4% PFA and then permeablized with 0.1% saponin.](http://images.novusbio.com/fullsize/ATM-Antibody-Flow-Cytometry-NB100-104-img0012.jpg)
![Flow Cytometry: ATM Antibody [NB100-104] - An intracellular stain was performed on HepG2 cells with PE-conjugated ATM antibody [NB100-104PE] (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeablized with 0.1% saponin. Cells were incubated in an antibody dilution of 5 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to Phycoerythrin.](http://images.novusbio.com/fullsize/ATM-Antibody-Flow-Cytometry-NB100-104-img0015.jpg)
![Immunocytochemistry/ Immunofluorescence: ATM Antibody [NB100-104] - ATM is activated by spermidine in GM00637 cells.GM00637 cells with or without KU55933 pretreatment (a,b), & GM05849 cells (c) were exposed to 50 μM spermidine or CCCP, followed by immunofluorescence analyses of total & p-ATM on Ser-1981. The scale bar is 10 μm. Ratios of cells expressing p-ATM Ser-1981 to cells expressing total ATM were presented (d). 20–45 cells/condition from three experiments were collected. Values are mean ± SD, *p < 0.05 vs. control. Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/srep24700), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-104_rabbit-polyclonal-atm-antibody-31020241535641.jpg)
![Immunocytochemistry/ Immunofluorescence: ATM Antibody [NB100-104] - ATM is activated by spermidine in GM00637 cells.GM00637 cells with or without KU55933 pretreatment (a,b), & GM05849 cells (c) were exposed to 50 μM spermidine or CCCP, followed by immunofluorescence analyses of total & p-ATM on Ser-1981. The scale bar is 10 μm. Ratios of cells expressing p-ATM Ser-1981 to cells expressing total ATM were presented (d). 20–45 cells/condition from three experiments were collected. Values are mean ± SD, *p < 0.05 vs. control. Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/srep24700), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-104_rabbit-polyclonal-atm-antibody-310202415304298.jpg)
![Western Blot: ATM Antibody [NB100-104] - Depletion of SMARCAL1 induces DNA damage & checkpoint activation in iSML1 iPSCs. (A,B) The iSML1 iPSCs were cultured for 7 & 14 days in the presence of doxycycline (DOX) to induce SMARCAL1 downregulation & then immunostained. The graphs (top) show quantification of the number of gamma -H2AX-positive cells (A) or ATM-pSer1981-positive cells (B). Representative images from triplicate experiments are shown (bottom). (C) Immunoblot detection of the indicated DDR proteins in iSML1 iPSCs after 14 days of continuous treatment with DOX. Lamin B1 was used as the loading control. Data are mean±s.e.m. from three independent experiments. *P≤0.05, **P≤0.01, ***P≤0.001 (two-way ANOVA test). ns, not significant. Scale bars: 10 µm. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31515241), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-104_rabbit-polyclonal-atm-antibody-310202415371997.jpg)
![Western Blot: ATM Antibody [NB100-104] - Analysis of double strand break repair in MCF-7 monolayer & mammosphere populations. (a) Cells were exposed to 4 Gy 60Co gamma -radiation & the relative degree of double-strand breakage (DSB) was determined by the comet assay under neutral conditions immediately after exposure & at the times indicated after exposure. (b) The 'comets' (n of about 100) were categorized according to the NIH LISTSERV (Comet Assay Interest Group web site) in which type 1 comets display the least DNA damage & type 5 the most. The error bars represent the mean ± standard error of the mean in both panels. The comets of the unirradiated cells are labeled Cont. (c) Expression of proteins involved in the NHEJ pathway of DSB repair in response to increasing doses of ionizing radiation. Lysates were prepared from unirradiated cells & from cells harvested one hour after exposure to 1 or 10-Gy 60Co gamma -radiation & analyzed by immunoblotting with antibodies against several DSB repair proteins. Phospho-ATM & phospho-DNA-PKcs refer to phosphorylation of these proteins at Ser1981 & Ser2056, respectively. Actin served as a loading control. Image collected & cropped by CiteAb from the following publication (//breast-cancer-research.biomedcentral.com/articles/10.1186/bcr2583), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-104_rabbit-polyclonal-atm-antibody-310202415535196.jpg)
![Simple Western: TRF-2 Antibody (4A794.15) [NB100-56506] - Image shows a specific band for TRF2 in 1.0 mg/mL of HeLa lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system. Non-specific interaction with the 230 kDa Simple Western standard may be seen with this antibody.](http://images.novusbio.com/fullsize/TRF-2-Antibody-4A794-15-Simple-Western-NB100-56506-img0010.jpg "Simple Western: TRF-2 Antibody (4A794.15) [NB100-56506] - Image shows a specific band for TRF2 in 1.0 mg/mL of HeLa lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system. Non-specific interaction with the 230 kDa Simple Western standard may be seen with this antibody.")
![Western Blot: TRF-2 Antibody (4A794.15) [NB100-56506] - Analysis in human Jurkat cell lysate at 2 ug/mL. Goat anti-mouse Ig HRP secondary antibody and PicoTect ECL substrate solution were used.](http://images.novusbio.com/fullsize/TRF-2-Antibody-4A794-15-Western-Blot-NB100-56506-img0008.jpg)
![Immunohistochemistry-Paraffin: TRF-2 Antibody (4A794.15) [NB100-56506] - Transitional cell carcinoma, urinary bladder, stained with TRF2 antibody (4 ug/mL), peroxidase-conjugate and DAB chromogen. Note specific nuclear staining. Tumor/normal adjacent tissue array slide was used for this test. Staining of formalin-fixed tissues is enhanced by boiling tissue sections in 10 mM sodium citrate buffer, pH 6.0 for 10-20 min followed by cooling at RT for 20 min.](http://images.novusbio.com/fullsize/TRF-2-Antibody-4A794-15-Immunohistochemistry-Paraffin-NB100-56506-img0012.jpg)
![Immunocytochemistry/Immunofluorescence: TRF-2 Antibody (4A794.15) [NB100-56506] - Localization of candidate RNAs at telomeres. Localization of SNORD17 at telomeres in human U-2 OS cells. Cells were fixed and sequentially incubated with Abs against TRF-2 and AlexaFluor 488-conjugated anti-mouse IgG. Subsequently, the cells were hybridized with the RNA probes and subjected to fluorescence microscopy. Three different cells are shown. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0123387), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/TRF-2-Antibody-4A794-15-Immunocytochemistry-Immunofluorescence-NB100-56506-img0018.jpg)
![Flow Cytometry: TRF-2 Antibody (4A794.15) [NB100-56506] - Intracellular flow cytometric analysis of TRF2 in 10^6 human Jurkat cells using 0.1 ug of NB100-56506. The shaded histogram represents cells alone, blue represents isotype control and red represents NB100-56506, anti-TRF2.](http://images.novusbio.com/fullsize/TRF-2-Antibody-4A794-15-Flow-Cytometry-NB100-56506-img0001.jpg)
![Western Blot: TRF-2 Antibody (4A794.15) [NB100-56506] - Total protein from mouse 3T3 cells was separated on a 12% gel by SDS-PAGE, transferred to PVDF membrane and blocked in 5% non-fat milk in TBST. The membrane was probed with 2.0 ug/mL anti-TRF2 in 1% non-fat milk in TBST and detected with an anti-mouse HRP secondary antibody using chemiluminescence.](http://images.novusbio.com/fullsize/TRF-2-Antibody-4A794-15-Western-Blot-NB100-56506-img0016.jpg)
![Immunocytochemistry/Immunofluorescence: TRF-2 Antibody (4A794.15) [NB100-56506] - Localization of candidate RNAs at telomeres. Localization of NEAT1 at telomeres in human U-2 OS cells. Cells were fixed and sequentially incubated with Abs against TRF-2 and AlexaFluor 488-conjugated anti-mouse IgG. Subsequently, the cells were hybridized with the RNA probes and subjected to fluorescence microscopy. Three different cells are shown. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0123387), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/TRF-2-Antibody-4A794-15-Immunocytochemistry-Immunofluorescence-NB100-56506-img0019.jpg)
![Flow Cytometry: TRF-2 Antibody (4A794.15) [NB100-56506] - An intracellular stain was performed on A431 cells with TRF2 Antibody [4A794.15] NB100-56506 (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 1.0 ug/mL for 30 minutes at room temperature, followed by Mouse IgG (H+L) Cross-Adsorbed Secondary Antibody, Dylight 550 (35503, Thermo Fisher).](http://images.novusbio.com/fullsize/TRF-2-Antibody-4A794-15-Flow-Cytometry-NB100-56506-img0020.jpg)
![Immunocytochemistry/Immunofluorescence: TRF-2 Antibody (4A794.15) [NB100-56506] - Staining of TRF2-bound telomeres in human HeLa cells (Courtesy of Fotiadou, et al, 2004).](http://images.novusbio.com/fullsize/TRF-2-Antibody-4A794-15-Immunocytochemistry-Immunofluorescence-NB100-56506-img0005.jpg)
![Immunocytochemistry/Immunofluorescence: TRF-2 Antibody (4A794.15) [NB100-56506] - HeLa cells were fixed for 10 minutes using 10% formalin and then permeabilized for 5 minutes using 1X PBS + 0.5% Triton-X100. The cells were incubated with anti-TRF-2 (4A794.15) conjugated to FITC [NB100-56506F] at 5 ug/mL for 1 hour at room temperature. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 40X objective.](http://images.novusbio.com/fullsize/TRF-2-Antibody-4A794-15-Immunocytochemistry-Immunofluorescence-NB100-56506-img0017.jpg)
![Immunocytochemistry/ Immunofluorescence: TRF-2 Antibody (4A794.15) - BSA Free [NB100-56506] - ZBTB48‐dependent loss of MTFP1 phenocopies MTFP1 depletionFluorescence microscopy analysis of the structure & localization of the mitochondrial network in HeLa WT & ZBTB48 KO clones. Mitochondria are marked with the MitoTracker dye (red), & nuclei are counterstained with DAPI (blue). Scale bars represent 20 μm.The same analysis as in (A) for U2OS WT & ZBTB48 KO clones. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28500257), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-56506_mouse-monoclonal-trf-2-antibody-4a794-15-31020241534325.jpg)
![Western Blot: TRF-2 Antibody (4A794.15) - BSA Free [NB100-56506] - TRF2 delta B delta M expression induces chromosome end-to-end fusions in all inducible cell lines(A) Immunoblots of MCF-10A, TO, SH-TO & SV-TO cell lines with & without DOX & HEK 293T. After 96 h of DOX treatment, the inducible cell lines expressed the truncated TRF2 delta B delta M protein (50 kDa); in contrast, uninduced cell lines, MCF-10A parental cell line & HEK 293T cells displayed only the endogen TRF2 protein (66 kDa). Lamin B1 was used as loading control. (B) After sustained expression of TRF2 delta B delta M for 96 h there was a significant increase in aberrant metaphases only in TO cells when compared to uninduced matched cells. (C) Nevertheless, the efficacy of the inducible system was validated by the statistical increase of cells with end-to-end fusions in all inducible cell lines. (D) Moreover, a high incidence of fusions per cell was found in all modified cell lines after sustained TRF2 depletion. Data was presented as mean + SEM. (E) Example of TO, SH-TO & SV-TO karyotypes after 96 h of TRF2 delta B delta M expression. Open arrows indicate clonal aberrations in the parental MCF-10A cell line. Insets in the karyotype show rearranged chromosomes stained with centromeric (green) & telomeric (red) PNA probes. Note the presence of telomere FISH signals at the fusion point of chromatid- or chromosome-type end-to-end fusions. Image collected & cropped by CiteAb from the following publication (//www.oncotarget.com/lookup/doi/10.18632/oncotarget.25502), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-56506_mouse-monoclonal-trf-2-antibody-4a794-15-31020241682158.jpg)
![Immunocytochemistry/ Immunofluorescence: TRF-2 Antibody (4A794.15) - BSA Free [NB100-56506] - ZBTB48 ZnF11 necessary to bind to telomeres. Sequence‐specific DNA pull‐downs w/ either telomeric (TTAGGG)/a control sequence (GTGAGT) for FLAG‐ZBTB48 WT, domain deletion constructs for different zinc finger & combinations of deletion constructs w/ ZnF10/11 point mutants. Domain structures indicated - right.Sequence‐specific DNA pull‐downs for FLAG‐ZBTB48 WT & ZnF11 point mutant for telomeric repeat sequences of different phyla (green) & their respective scrambled controls (blue).Protein expression analysis of ZBTB48 by WB for cell lines used. GAPDH serves as a loading control.IF stainings for exogenous FLAG‐ZBTB48 WT & point mutants for ZnF10 & ZnF11 in U2OS cells. The same analysis as in Fig 1E performed & average co‐localization frequencies shown (n = 24–37 cells).Co‐localization analysis of endogenous ZBTB48/exogenous FLAG‐ZBTB48 WT w/ TRF2 in HeLa cells by IF (IF) staining. Image illustrating co‐localization between ZBTB48/FLAG‐ZBTB48 WT (green) & TRF2 (red) as a marker for telomeres is shown w/ DAPI (blue) used as nuclear counterstain. Co‐localization events indicated by white arrows. Quantification of frequency of co‐localization events (right) done after 3D reconstruction of acquired z‐stacks (n = 30 cells).Co‐localization analysis of endogenous ZBTB48/exogenous FLAG‐ZBTB48 WT w/ TRF2 in HeLa 1.3 cells by IF (IF) staining analogous to (E) (n = 30 cells).Co‐localization analysis of endogenous ZBTB48/exogenous FLAG‐ZBTB48 WT w/ TRF2 in HT1080 super‐telomerase cells by IF (IF) staining analogous to (E) (n = 30 cells).Data information: (D–G) Scale bars = 5 μm. Error bars indicate standard deviations, & P‐values based on Student's t‐test.Source data available online for this figure. Image collected & cropped by CiteAb from following publication (//pubmed.ncbi.nlm.nih.gov/28500257), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-56506_mouse-monoclonal-trf-2-antibody-4a794-15-31020241553721.jpg)