| 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 | NB600-101SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NBP1-97308SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB100-56571SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB110-57130SS | |||
| BSA Free | NB110-57130 | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB600-101SS | |||
| BSA Free | NB600-101 | |||
![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: Calreticulin Antibody [NB600-101] - Western blot shows lysates of HeLa human cervical epithelial carcinoma parental cell line and Calreticulin knockout (KO) HeLa cell line. PVDF membrane was probed with 1:1500 of Rabbit Anti-Human Calreticulin Polyclonal Antibody (Catalog # NB600-101) followed by HRP-conjugated Anti-Rabbit IgG Secondary Antibody (Catalog #HAF008). Specific band was detected for Calreticulin at approximately 55 kDa (as indicated) in the parental HeLa cell line, but is not detectable in the knockout HeLa cell line. This experiment was conducted under reducing conditions.](http://images.novusbio.com/fullsize/Calreticulin-Antibody-Knockdown-Validated-NB600-101-img0011.jpg "<b>Genetic Strategies Validation. </b>Western Blot: Calreticulin Antibody [NB600-101] - Western blot shows lysates of HeLa human cervical epithelial carcinoma parental cell line and Calreticulin knockout (KO) HeLa cell line. PVDF membrane was probed with 1:1500 of Rabbit Anti-Human Calreticulin Polyclonal Antibody (Catalog # NB600-101) followed by HRP-conjugated Anti-Rabbit IgG Secondary Antibody (Catalog #HAF008). Specific band was detected for Calreticulin at approximately 55 kDa (as indicated) in the parental HeLa cell line, but is not detectable in the knockout HeLa cell line. This experiment was conducted under reducing conditions.")
![<b>Genetic Strategies Validation. </b>Western Blot: Calreticulin Antibody [NB600-101] - Human kidney lysate.](http://images.novusbio.com/fullsize/Calreticulin-Antibody-Western-Blot-NB600-101-img0006.jpg)
![Immunocytochemistry/Immunofluorescence: Calreticulin Antibody [NB600-101] - Immunofluorescence staining of Calreticulin in HCT15 colon cancer cells using NB600-101. Secondary antibody was conjugated with Alexa Fluor 488. Photo courtesy of Dr. Birkenkamp Demtroeder, Arhus University Hospital.](http://images.novusbio.com/fullsize/Calreticulin-Antibody-Immunocytochemistry-Immunofluorescence-NB600-101-img0005.jpg)
![Immunohistochemistry-Paraffin: Calreticulin Antibody [NB600-101] - Analysis of a FFPE tissue section of human thyroid gland using 1:50 dilution of Calreticulin antibody. The signal was developed using HRP-DAB based detection method which followed counterstaining of the nuclei with hematoxylin. This representative section shows a strong positivity of Calreticulin in the follicular epithelial cells, wherein the signal was found to be very intense in the perinuclear region of the cells which correlates well with Endoplasmic reticulum localization of this protein. The para-follicular cells, endothelial cells of blood vessels (not the RBCs though) and the loose connective tissue in the section showed a weak cytoplasmic staining. Some staining was observed in the follicles/colloids also which is potentially the secreted form of Calreticulin.](http://images.novusbio.com/fullsize/Calreticulin-Antibody-Immunohistochemistry-Paraffin-NB600-101-img0010.jpg)
![Immunocytochemistry/Immunofluorescence: Calreticulin Antibody [NB600-101] - The Calreticulin antibody NB600-101 was tested in HeLa cells at a 1:250 dilution against DyLight 488 (Green). Alpha-tubulin and nuclei were counterstained against DyLight 550 (Red) and DAPI (Blue), respectively.](http://images.novusbio.com/fullsize/Calreticulin-Antibody-Immunocytochemistry-Immunofluorescence-NB600-101-img0007.jpg)
![Immunohistochemistry-Paraffin: Calreticulin Antibody [NB600-101] - Analysis of a FFPE tissue section of human thyroid gland using 1:50 dilution of Calreticulin antibody. The signal was developed using HRP-DAB based detection method which followed counterstaining of the nuclei with hematoxylin. This representative section shows a strong positivity of Calreticulin in the follicular epithelial cells, wherein the signal was found to be very intense in the perinuclear region of the cells which correlates well with Endoplasmic reticulum localization of this protein. The para-follicular cells, endothelial cells and the loose connective tissue in the section showed a weak cytoplasmic staining. Some staining was observed in the follicles/colloids also which is potentially the secreted form of Calreticulin.](http://images.novusbio.com/fullsize/Calreticulin-Antibody-Immunohistochemistry-Paraffin-NB600-101-img0009.jpg)
![Simple Western: Calreticulin Antibody [NB600-101] - Lane view shows a specific band for Calreticulin 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/Calreticulin-Antibody-Simple-Western-NB600-101-img0008.jpg)
![Immunohistochemistry: GLP-1R Antibody [NBP1-97308] - Analysis of GLP1R in mouse pancreas using DAB with hematoxylin counterstain.](http://images.novusbio.com/fullsize/GLP-1R-Antibody-Immunohistochemistry-NBP1-97308-img0009.jpg "Immunohistochemistry: GLP-1R Antibody [NBP1-97308] - Analysis of GLP1R in mouse pancreas using DAB with hematoxylin counterstain.")
![<b>Biological Strategies Validation and Genetic Strategies Validation.</b>Western Blot: GLP-1R Antibody [NBP1-97308] - Liraglutide reduces apoptosis of hCMSCs via PKA/i2-catenin pathway. The expression of GLP-1R and apoptotic proteins Bax, Bcl-2, cleaved caspase-9, and cleaved caspase-3 were detected by western blot with Si-GLP-1R and liraglutide. Image collected and cropped by Citeab from the following publication (Mesenchymal stem cells combined with liraglutide relieve acute lung injury through apoptotic signaling restrained by PKA/-catenin. Stem Cell Res Ther (2020) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/GLP-1R-Antibody-Western-Blot-NBP1-97308-img0015.jpg)
![Simple Western: GLP-1R Antibody [NBP1-97308] - Simple Western lane view shows a specific band for GLP-1R in 0.5 mg/ml of Human Pancreas (left) and Mouse Pancreas (right) 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/GLP-1R-Antibody-Simple-Western-NBP1-97308-img0006.jpg)
![Western Blot: GLP-1R Antibody [NBP1-97308] - Total protein from Human and Mouse brain and SHSY-5Y 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-GLP1R in 1% non-fat milk in TBST and detected with an anti-rabbit HRP secondary antibody using chemiluminescence.](http://images.novusbio.com/fullsize/GLP-1R-Antibody-Western-Blot-NBP1-97308-img0014.jpg)
![<b>Biological Strategies Validation. </b>Western Blot: GLP-1R Antibody [NBP1-97308] - Expression of GLP-1R in three MSCs at different time points under the stimulation of LPS. The expression of GLP-1R in hCMSCs, hBMSCs, and hAMSCs in the control group and in 30 ug/mL LPS stimulation for 24 h, 48 h, and 72 h at protein. Fluorescence intensity of GLP-1R in hCMSCs Image collected and cropped by Citeab from the following publication (Mesenchymal stem cells combined with liraglutide relieve acute lung injury through apoptotic signaling restrained by PKA/-catenin. Stem Cell Res Ther (2020) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/GLP-1R-Antibody-Western-Blot-NBP1-97308-img0016.jpg)
![Immunocytochemistry/Immunofluorescence: GLP-1R Antibody [NBP1-97308] - GLP1R-1 antibody was tested in HeLa cells with FITC (green). Nuclei and alpha-tubulin were counterstained with DAPI (blue) and Dylight 550 (red).](http://images.novusbio.com/fullsize/GLP-1R-Antibody-Immunocytochemistry-Immunofluorescence-NBP1-97308-img0004.jpg)
![Immunohistochemistry-Paraffin: GLP-1R Antibody [NBP1-97308] - Tissue section of mouse pancreas using 1:200 dilution of rabbit anti-GLP1R antibody. The staining was developed with HRP labeled anti-rabbit IgG secondary antibody and DAB reagent, and nuclei of cells were counter-stained with hematoxylin. This GLP1R antibody primarily generated a specific membrane cytoplasmic staining of apparently beta cells in the Islets of Langerhans. The cells of lobular/inter-lobular ducts and the acinar cells were largely negative for GLP1R.](http://images.novusbio.com/fullsize/GLP-1R-Antibody-Immunohistochemistry-Paraffin-NBP1-97308-img0011.jpg)
![Western Blot: GLP-1R Antibody [NBP1-97308] - Analysis of GLP1R in human pancreas cell lysate.](http://images.novusbio.com/fullsize/GLP-1R-Antibody-Western-Blot-NBP1-97308-img0008.jpg)
![Immunocytochemistry/Immunofluorescence: GLP-1R Antibody [NBP1-97308] - Neuro2a cells were fixed for 10 minutes using 10% formalin and then permeabilized for 5 minutes using 1X PBS + 0.05% Triton-X100. The cells were incubated with anti-GLP-1R at 5 ug/ml 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/GLP-1R-Antibody-Immunocytochemistry-Immunofluorescence-NBP1-97308-img0012.jpg)
![Immunohistochemistry-Paraffin: GLP-1R Antibody [NBP1-97308] - Tissue section of mouse pancreas using 1:200 dilution of rabbit anti-GLP1R antibody. The staining was developed with HRP labeled anti-rabbit IgG secondary antibody and DAB reagent, and nuclei of cells were counter-stained with hematoxylin. This GLP1R antibody primarily generated a specific membrane cytoplasmic staining of apparently beta cells in the Islets of Langerhans.](http://images.novusbio.com/fullsize/GLP-1R-Antibody-Immunohistochemistry-Paraffin-NBP1-97308-img0010.jpg)
![Western Blot: GLP-1R Antibody - BSA Free [NBP1-97308] - Liraglutide reduces apoptosis of hCMSCs via PKA/ beta -catenin pathway. a Western blot & b RT-qPCR verify the knockdown effects of three Si-GLP-1R in hCMSCs. c, d Western blot was used to detect of beta -catenin & p-beta -catenin expression under the stimulation of LPS by adding 20 μM H89 or 100 nM Si-GLP-1R & liraglutide. e The expression of apoptotic proteins Bax, Bcl-2, cleaved caspase-9, & cleaved caspase-3 was detected by western blot with PKA inhibitor H89 & liraglutide. f The expression of GLP-1R & apoptotic proteins Bax, Bcl-2, cleaved caspase-9, & cleaved caspase-3 were detected by western blot with Si-GLP-1R & liraglutide. Error bars represent mean ± SD from three independent experiments. Compared with Si-con group, ***P < 0.001 Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32429994), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nbp1-97308_rabbit-polyclonal-glp-1r-antibody-310202415175291.jpg)
![Western Blot: TLR3 Antibody [NB100-56571] - Myocardial infarction (MI) increased TLR3 expression and its physical association with Trif in mouse myocardium. Heart samples were taken from infarct area at 4 weeks after MI. (A) and (B) show mRNA and protein levels of TLR3 in sham and MI hearts. n = 4 mice/group. Data are means +/- S.D. AP < 0.01 versus sham. Image collected and cropped by CiteAb from the following publication (//doi.wiley.com/10.1111/jcmm.13328) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/TLR3-Antibody-Western-Blot-NB100-56571-img0009.jpg "<b>Biological Strategies Validation and Orthogonal Strategies Validation.</b>Western Blot: TLR3 Antibody [NB100-56571] - Myocardial infarction (MI) increased TLR3 expression and its physical association with Trif in mouse myocardium. Heart samples were taken from infarct area at 4 weeks after MI. (A) and (B) show mRNA and protein levels of TLR3 in sham and MI hearts. n = 4 mice/group. Data are means +/- S.D. AP < 0.01 versus sham. Image collected and cropped by CiteAb from the following publication (//doi.wiley.com/10.1111/jcmm.13328) licensed under a CC-BY license.")
![<b>Biological Strategies Validation and Orthogonal Strategies Validation.</b>Immunohistochemistry-Frozen: TLR3 Antibody [NB100-56571] - Frozen mouse eye tissue sections stained with TLR3, a retinal pigment epithelium (RPE) marker and DAPI. Top panel: TLR3 (red) colocalized with the RPE (green) marker. Bottom panel: Tissue stained with isotype control (no TLR3 Ab), RPE and DAPI. Data courtesy of Kleinman et al.](http://images.novusbio.com/fullsize/TLR3-Antibody-Immunohistochemistry-Frozen-NB100-56571-img0002.jpg)
![Flow Cytometry: TLR3 Antibody [NB100-56571] - Analysis using the FITC conjugate of NB100-56571. Staining of TLR3 in Balb/c mouse splenocytes using this antibody at 1 ug/10^6 cells. Green represents rabbit IgG isotype control this antibody; red represents anti-TLR3 antibody.](http://images.novusbio.com/fullsize/TLR3-Antibody-Flow-Cytometry-NB100-56571-img0008.jpg)
![Western Blot: TLR3 Antibody [NB100-56571] - Analysis of TLR3 in mouse spleen tissue lysate using NB100-56571 at 2 ug/ml.](http://images.novusbio.com/fullsize/TLR3-Antibody-Western-Blot-NB100-56571-img0005.jpg)
![Immunohistochemistry: TLR3 Antibody [NB100-56571] - Pig lung poisoned through aspiration with gastric juice and organophosphate (dimethoate EC40) after 48 hours of IC ventilation. Image from verified customer review.](http://images.novusbio.com/fullsize/TLR3-Antibody-Immunohistochemistry-NB100-56571-img0006.jpg)
![Flow Cytometry: TLR3 Antibody [NB100-56571] - Intracellular flow analysis of TLR3 in Balb/c mouse splenocytes and mouse RAW cells using TLR3 antibody (red) and isotype control antibody (green) at 1 ug/10^6 cells.](http://images.novusbio.com/fullsize/TLR3-Antibody-Flow-Cytometry-NB100-56571-img0001.jpg)
![<b>Genetic Strategies Validation. </b>Western Blot: TLR3 Antibody [NB100-56571] - siRNA was transfected at 50 nM for 48 hrs, and poly(I:C) was added at 100 ug/ml for 4 hrs before cell harvest. Negative control (NC) siRNA served as control. RNAiMAX transfection reagent was used in all the siRNA experiments. Panel shows the knockdown effects of siRNAs. Image collected and cropped by CiteAb from the following publication (//doi.wiley.com/10.1111/jcmm.13328) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/TLR3-Antibody-Knockdown-Validated-NB100-56571-img0010.jpg)
![Western Blot: TLR3 Antibody [NB100-56571] - Myocardial infarction (MI) increased TLR3 expression & its physical association with Trif in mouse myocardium. Heart samples were taken from infarct area at 4 weeks after MI. (A) & (B) show mRNA & protein levels of TLR3 in sham & MI hearts. n = 4 mice/group. Data are means ± S.D. AP < 0.01 versus sham. (C) Representative immunohistochemistry images of heart sections stained for TLR3 (brown colour). An isotype IgG control was performed to verify the specificity of TLR3 reactivity. (D) Lysates of heart tissue were immunoprecipitated with anti‐TLR3 antibodies (IP: TLR3), followed by SDS–PAGE & immunoblotting (IB) with indicated antibodies. IP with isotype IgG (IP: IgG) was performed as a control to exclude the non‐specific binding of antibodies to cellular proteins. Green arrows indicate non‐specific bands. The association between TLR3 & Trif, but not MyD88, was detectable in sham myocardium & was increased in infarct myocardium. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28945004), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-56571_rabbit-polyclonal-tlr3-antibody-310202415523938.jpg)
![Western Blot: TLR3 Antibody [NB100-56571] - Myocardial infarction (MI) increased TLR3 expression & its physical association with Trif in mouse myocardium. Heart samples were taken from infarct area at 4 weeks after MI. (A) & (B) show mRNA & protein levels of TLR3 in sham & MI hearts. n = 4 mice/group. Data are means ± S.D. AP < 0.01 versus sham. (C) Representative immunohistochemistry images of heart sections stained for TLR3 (brown colour). An isotype IgG control was performed to verify the specificity of TLR3 reactivity. (D) Lysates of heart tissue were immunoprecipitated with anti‐TLR3 antibodies (IP: TLR3), followed by SDS–PAGE & immunoblotting (IB) with indicated antibodies. IP with isotype IgG (IP: IgG) was performed as a control to exclude the non‐specific binding of antibodies to cellular proteins. Green arrows indicate non‐specific bands. The association between TLR3 & Trif, but not MyD88, was detectable in sham myocardium & was increased in infarct myocardium. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28945004), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-56571_rabbit-polyclonal-tlr3-antibody-3102024165731.jpg)
![Immunohistochemistry: TLR3 Antibody [NB100-56571] - Myocardial infarction (MI) increased TLR3 expression & its physical association with Trif in mouse myocardium. Heart samples were taken from infarct area at 4 weeks after MI. (A) & (B) show mRNA & protein levels of TLR3 in sham & MI hearts. n = 4 mice/group. Data are means ± S.D. AP < 0.01 versus sham. (C) Representative immunohistochemistry images of heart sections stained for TLR3 (brown colour). An isotype IgG control was performed to verify the specificity of TLR3 reactivity. (D) Lysates of heart tissue were immunoprecipitated with anti‐TLR3 antibodies (IP: TLR3), followed by SDS–PAGE & immunoblotting (IB) with indicated antibodies. IP with isotype IgG (IP: IgG) was performed as a control to exclude the non‐specific binding of antibodies to cellular proteins. Green arrows indicate non‐specific bands. The association between TLR3 & Trif, but not MyD88, was detectable in sham myocardium & was increased in infarct myocardium. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28945004), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-56571_rabbit-polyclonal-tlr3-antibody-310202415535158.jpg)
![Western Blot: TLR3 Antibody [NB100-56571] - TLR3‐knockout (TLR3‐KO) attenuated cardiac autophagy induced by MI. The infarct & remote tissues were separately sampled from the left ventricle after 4 weeks of MI. Accordingly, anterior & posterior tissues of the left ventricle were sampled from sham hearts as controls. (A) Representative Western blot images & quantitative analyses of autophagy markers. n = 4–8/group. Quantitative data are fold changes of WT‐sham. aP < 0.05, AP < 0.01 versus respective WT‐sham; bP < 0.05, BP < 0.01 versus respective WT‐MI. (B) Representative electron microphotographs of ultrathin sections of resin‐embedded heart biopsies. Arrows indicate autophagic vacuoles. (C) Lysates of infarct tissue were immunoprecipitated (IP), followed by SDS–PAGE & immunoblotting (IB) with indicated antibodies. IP with isotype IgG served as a control. Green arrows indicate non‐specific bands. Representative images were taken from four independent experiments. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28945004), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-56571_rabbit-polyclonal-tlr3-antibody-310202415525214.jpg)
![Western Blot: TLR3 Antibody [NB100-56571] - A TLR3 agonist polyinosinic‐polycytidylic acid (poly(I:C)) induced autophagy in cultured cardiomyocytes through a TRIF‐dependent pathway. (A) Poly(I:C) increased autophagy markers in cultured H9c2 rat ventricular cells. (B) Poly(I:C) stimulated autophagosome formation but did not affect autophagic flux. Primary cultured neonatal rat ventricular myocytes (NRVMs) were transfected with a tandem mRFP‐GFP‐LC3 adenovirus for 24 hrs, followed by treatment with poly(I:C) (100 μg/ml, 4 hrs). Autophagosomes & autolysosomes were, respectively, visualized as yellow‐ & red‐only punctas under a confocal microscope. (C) An autophagic flux inhibitor chloroquine (CQ) induced accumulations of LC3‐II & p62/SQSTM1 proteins in H9c2 myocytes receiving poly(I:C) (100 μg/ml, 4 hrs). CQ was applied at 10 μM, immediately prior to poly(I:C). (D) Effects of indicated siRNA on poly(I:C)‐induced changes in autophagy markers in NRVMs. All the siRNAs were transfected at 50 nM for 48 hrs, & poly(I:C) was added at 100 μg/ml for 4 hrs before cell harvest. Negative control (NC) siRNA served as control. RNAiMAX transfection reagent was used in all the siRNA experiments. The upper panel shows the knockdown effects of siRNAs, & the lower panel shows representative Western blot images (presented from four independent experiments) & densitometry quantitative data (normalized into ‘fold of vehicle group’). All quantitative data are expressed as means ± S.D. aP < 0.05, AP < 0.01 versus vehicle; bP < 0.05, BP < 0.01 versus poly(I:C). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28945004), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-56571_rabbit-polyclonal-tlr3-antibody-3102024168394.jpg)
![Immunocytochemistry/Immunofluorescence: Calnexin Antibody (1563) [NBP2-43765] - HeLa cells were fixed in ice-cold MeOH for 5 min. Green: Calnexin stained by Calnexin antibody [1563] diluted at 1:500. Red: Calnexin, stained by Calnexin antibody [C3], C-term diluted at 1:500. Blue: Hoechst 33342 staining.](http://images.novusbio.com/fullsize/Calnexin-Antibody-1563-Immunocytochemistry-Immunofluorescence-NBP2-43765-img0007.jpg "Immunocytochemistry/Immunofluorescence: Calnexin Antibody (1563) [NBP2-43765] - HeLa cells were fixed in ice-cold MeOH for 5 min. Green: Calnexin stained by Calnexin antibody [1563] diluted at 1:500. Red: Calnexin, stained by Calnexin antibody [C3], C-term diluted at 1:500. Blue: Hoechst 33342 staining.")
![Western Blot: Calnexin Antibody (1563) [NBP2-43765] - Analysis of A. 30 ug 293T whole cell lysate/extract B. 30 ug A431 whole cell lysate/extract C. 30 ug HeLa whole cell lysate/extract D. 30 ug HepG2 whole cell lysate/extract 7.5 % SDS-PAGE Calnexin antibody [1563] dilution: 1:1000.](http://images.novusbio.com/fullsize/Calnexin-Antibody-1563-Western-Blot-NBP2-43765-img0001.jpg)
![Western Blot: Calnexin Antibody (1563) [NBP2-43765] - Analysis of A. 30 ug PC-12 whole cell lysate/extract B. 30 ug Rat-2 whole cell lysate/extract 7.5 % SDS-PAGE Calnexin antibody [1563] dilution: 1:500](http://images.novusbio.com/fullsize/Calnexin-Antibody-1563-Western-Blot-NBP2-43765-img0002.jpg)
![Immunocytochemistry/ Immunofluorescence: Calnexin Antibody (1563) [NBP2-43765] - Calnexin antibody [GT1563] detects Calnexin protein at cytoplasm by immunofluorescent analysis.Sample: Neuro2A cells were fixed in 4% paraformaldehyde at RT for 15 min.Green: Calnexin stained by Calnexin antibody [GT1563] (NBP2-43765) diluted at 1:500.Blue: Fluoroshield with DAPI .](http://images.novusbio.com/fullsize/nbp2-43765_mouse-monoclonal-calnexin-antibody-1563-91020242001038.jpg)
![Western Blot: Calnexin Antibody (1563) [NBP2-43765] - Analysis of A. 50 ug mouse liver lysate/extract 7.5 % SDS-PAGE Calnexin antibody [1563] dilution: 1:1000](http://images.novusbio.com/fullsize/Calnexin-Antibody-1563-Western-Blot-NBP2-43765-img0003.jpg)
![<b>Genetic Strategies Validation. </b>Western Blot: Calnexin Antibody (1563) [NBP2-43765] - Non-transfected (-) and transfected (+) 293T whole cell extracts (15 ug) were separated by 7.5% SDS-PAGE, and the membrane was blotted with Calnexin antibody [1563] (NBP2-43765).](http://images.novusbio.com/fullsize/Calnexin-Antibody-1563-Western-Blot-NBP2-43765-img0006.jpg)
![Western Blot: Calnexin Antibody (1563) [NBP2-43765] - Various tissue extracts (50 ug) were separated by 7.5% SDS-PAGE, and the membrane was blotted with Calnexin antibody [GT1563] (NBP2-43765) diluted at 1:1000. The HRP-conjugated anti-mouse IgG antibody was used to detect the primary antibody.](http://images.novusbio.com/fullsize/nbp2-43765_mouse-monoclonal-calnexin-antibody-1563-91020242075941.jpg)
![Western Blot: Calnexin Antibody (1563) [NBP2-43765] - Non-transfected (-) and transfected (+) 293T whole cell extracts (30 ug) were separated by 7.5% SDS-PAGE, and the membrane was blotted with Calnexin antibody [GT1563] (NBP2-43765) diluted at 1:5000. The HRP-conjugated anti-mouse IgG antibody was used to detect the primary antibody.](http://images.novusbio.com/fullsize/nbp2-43765_mouse-monoclonal-calnexin-antibody-1563-910202420134012.jpg)
![<b>Genetic Strategies Validation. </b>Non-transfected (-) and transfected (+) 293T whole cell extracts (15 ug) were separated by 7.5% SDS-PAGE, and the membrane was blotted with Calnexin antibody [GT1563] (NBP2-43765) diluted at 1:6000.](http://images.novusbio.com/fullsize/nbp2-43765_mouse-monoclonal-calnexin-antibody-1563-western-blot-261120251833102.jpg)
![Calnexin antibody [GT1563] detects Calnexin protein by immunofluorescent analysis.Sample: HeLa cells were fixed in ice-cold MeOH for 5 min.Green: Calnexin stained by Calnexin antibody [GT1563] (NBP2-43765) diluted at 1:500.Red: Calnexin, stained by Calnexin antibody [C3], C-term diluted at 1:500.Blue: Hoechst 33342 staining.](http://images.novusbio.com/fullsize/nbp2-43765_mouse-monoclonal-calnexin-antibody-1563-immunocytochemistry-immunofluorescence-261120251847323.jpg)
![Immunohistochemistry: TLR (Intracellular) Screening Antibody Pack [NBP2-25085] - The expression of TLR-7 in the hippocampal brain region. The immunofluorescence of TLR7 recognized by Alexa 488, green. GFAP recognized by Alexa 594, red. NEUN recognized by Alexa 633, (blue) and merged image in the hippocampal region. NeuN and GFAP were applied to show the distribution of TLR7 within neuronal and supportive tissue populations. Scale bar 80 um. Image collected and cropped by CiteAb from the following publication (//doi.org/10.1371/journal.pone.0222818) licensed under a CC-BY license. TLR7 Antibody [NBP2-24906]](http://images.novusbio.com/fullsize/TLR-Intracellular-Screening-Antibody-Pack-Immunohistochemistry-NBP2-25085-img0007.jpg "Immunohistochemistry: TLR (Intracellular) Screening Antibody Pack [NBP2-25085] - The expression of TLR-7 in the hippocampal brain region. The immunofluorescence of TLR7 recognized by Alexa 488, green. GFAP recognized by Alexa 594, red. NEUN recognized by Alexa 633, (blue) and merged image in the hippocampal region. NeuN and GFAP were applied to show the distribution of TLR7 within neuronal and supportive tissue populations. Scale bar 80 um. Image collected and cropped by CiteAb from the following publication (//doi.org/10.1371/journal.pone.0222818) licensed under a CC-BY license. TLR7 Antibody [NBP2-24906]")
![Flow Cytometry: TLR (Intracellular) Screening Antibody Pack [NBP2-25085] - Expression of TLR3 and TLR8 in Fravel, L363, OPM1, RPMI8226, XG1, and NCI-H929 as determined by flow cytometry. HCMLs were stained using an intracellular staining protocol with TLR3 and TLR8 antibodies followed by relevant secondary fluorescent-conjugated antibodies. Filled histograms (purple) represent the isotype controls and the open histograms (red) indicate TLR8. Data are representative for analysis of >= 2 independent experiments. Image collected and cropped by CiteAb from the following publication (//doi.org/10.1371/journal.pone.0060671) licensed under a CC-BY license. TLR3 Antibody (40C1285.6) [NBP2-24875] and TLR8 Antibody (44C143) [NBP2-24917]](http://images.novusbio.com/fullsize/TLR-Intracellular-Screening-Antibody-Pack-Flow-Cytometry-NBP2-25085-img0006.jpg)
![<b>Genetic Strategies Validation. </b>Western Blot: TLR (Intracellular) Screening Antibody Pack [NBP2-25085] - 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. TLR9 Antibody (26C593.2) [NBP2-24729]](http://images.novusbio.com/fullsize/TLR-Intracellular-Screening-Antibody-Pack-Knockdown-Validated-NBP2-25085-img0010.jpg)
![Western Blot: TLR (Intracellular) Screening Antibody Pack [NBP2-25085] - All the cell lines displayed a strong expression of TLR3 and TLR8 proteins. To confirm the immunoreactivity of the antibody, different positive controls were included. Beta-actin was served as loading control and was used to normalize expression levels between cells. Data are representative for analysis of >=2 independent experiments. Image collected and cropped by CiteAb from the following publication (//doi.org/10.1371/journal.pone.0060671) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/TLR-Intracellular-Screening-Antibody-Pack-Western-Blot-NBP2-25085-img0008.jpg)
![Immunocytochemistry/Immunofluorescence: TLR (Intracellular) Screening Antibody Pack [NBP2-25085] - 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. TLR9 Antibody (26C593.2) [NBP2-24729]](http://images.novusbio.com/fullsize/TLR-Intracellular-Screening-Antibody-Pack-Immunocytochemistry-Immunofluorescence-NBP2-25085-img0011.jpg)
![Simple Western: TLR (Intracellular) Screening Antibody Pack [NBP2-25085] - 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. TLR9 Antibody (26C593.2) [NBP2-24729]](http://images.novusbio.com/fullsize/TLR-Intracellular-Screening-Antibody-Pack-Simple-Western-NBP2-25085-img0009.jpg)
![Western Blot: Enolase 1 Antibody [NBP1-31324] - Various whole cell extracts (30 ug) were separated by 10% SDS-PAGE, and the membrane was blotted with ENO1 antibody [N3C3] diluted at 1:1000. The HRP-conjugated anti-rabbit IgG antibody (NBP2-19301) was used to detect the primary antibody.](http://images.novusbio.com/fullsize/Enolase-1-Antibody-Western-Blot-NBP1-31324-img0012.jpg "Western Blot: Enolase 1 Antibody [NBP1-31324] - Various whole cell extracts (30 ug) were separated by 10% SDS-PAGE, and the membrane was blotted with ENO1 antibody [N3C3] diluted at 1:1000. The HRP-conjugated anti-rabbit IgG antibody (NBP2-19301) was used to detect the primary antibody.")
![Immunocytochemistry/Immunofluorescence: Enolase 1 Antibody [NBP1-31324] - HeLa cells were fixed in 4% paraformaldehyde at RT for 15 min. Green: ENO1 protein stained by ENO1 antibody [N3C3] diluted at 1:200. Red: alpha Tubulin, a cytoskeleton marker, stained by alpha Tubulin antibody [B-5-1-2] diluted at 1:10000. Blue: Hoechst 33342 staining.](http://images.novusbio.com/fullsize/Enolase-1-Antibody-Immunocytochemistry-Immunofluorescence-NBP1-31324-img0008.jpg)
![Immunohistochemistry-Paraffin: Enolase 1 Antibody [NBP1-31324] - Paraffin-embedded gastric tissue, using antibody at 1:100 dilution.](http://images.novusbio.com/fullsize/Enolase-1-Antibody-Immunohistochemistry-Paraffin-NBP1-31324-img0003.jpg)
![Western Blot: Enolase 1 Antibody [NBP1-31324] - Sample (50 ug of whole cell lysate) A: Mouse brain 10% SDS PAGE; antibody diluted at 1:1000.](http://images.novusbio.com/fullsize/Enolase-1-Antibody-Western-Blot-NBP1-31324-img0004.jpg)
![Western Blot: Enolase 1 Antibody [NBP1-31324] - Sample (30 ug of whole cell lysate) A: A431 B: H1299 10% SDS PAGE, antibody diluted at 1:3000.](http://images.novusbio.com/fullsize/Enolase-1-Antibody-Western-Blot-NBP1-31324-img0005.jpg)
![<b>Genetic Strategies Validation. </b>Western Blot: Enolase 1 Antibody [NBP1-31324] - Non-transfected (-) and transfected (+) 293T whole cell extracts (30 ug) were separated by 10% SDS-PAGE, and the membrane was blotted with ENO1 antibody [N3C3].](http://images.novusbio.com/fullsize/Enolase-1-Antibody-Western-Blot-NBP1-31324-img0007.jpg)
![Western Blot: Enolase 1 Antibody [NBP1-31324] - Rat tissue extract (50 ug) was separated by 10% SDS-PAGE, and the membrane was blotted with ENO1 antibody [N3C3] diluted at 1:1000. The HRP-conjugated anti-rabbit IgG antibody (NBP2-19301) was used to detect the primary antibody, and the signal was developed with Trident ECL plus-Enhanced.](http://images.novusbio.com/fullsize/Enolase-1-Antibody-Western-Blot-NBP1-31324-img0010.jpg)
![Western Blot: Enolase 1 Antibody [NBP1-31324] - Sample (30 ug of whole cell lysate) A: zebrafish eye 10% SDS PAGE NBP1-31324 diluted at 1:1000](http://images.novusbio.com/fullsize/nbp1-31324_rabbit-polyclonal-enolase-1-antibody-910202420134090.jpg)
![Immunohistochemistry: Enolase 1 Antibody [NBP1-31324] - Immunohistochemical analysis of paraffin-embedded zebrafish tissue, using Enolase 1 antibody [N3C3] (NBP1-31324) at 1:300 dilution.](http://images.novusbio.com/fullsize/nbp1-31324_rabbit-polyclonal-enolase-1-antibody-91020242041252.jpg)
![Immunohistochemistry: Enolase 1 Antibody [NBP1-31324] - Enolase 1 antibody [N3C3] detects Eno1 protein on zebrafish by whole mount immunohistochemical analysis. Sample: 2 days-post-fertilization zebrafish embryo. Enolase 1 antibody [N3C3] (NBP1-31324) dilution: 1:100.](http://images.novusbio.com/fullsize/nbp1-31324_rabbit-polyclonal-enolase-1-antibody-910202420134054.jpg)