| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| Purified | NBP3-25349-0.025mg | |||
| Purified | NBP3-25349-0.05mg | |||
| BSA Free | NB100-142SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB100-143SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB500-170SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB110-57130SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB100-56506SS | |||
| Azide and BSA Free | NBP2-33212 | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB100-104SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| Unpurified | NB600-1252-0.1ml | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB110-89717SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB300-232SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB300-229SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB600-1335SS | |||
| Azide and BSA Free | NBP2-80745 | |||
![Simple Western: Mre11 Antibody [NB100-142] - Image shows a specific band for Mre11 in 0.5 mg/mL of HeLa lysate. A band appears at the theoretical molecular weight of 81 kDa for this product. This experiment was performed under reducing conditions using the 12-230 kDa separation system.](http://images.novusbio.com/fullsize/Mre11-Antibody-Simple-Western-NB100-142-img0010.jpg "Simple Western: Mre11 Antibody [NB100-142] - Image shows a specific band for Mre11 in 0.5 mg/mL of HeLa lysate. A band appears at the theoretical molecular weight of 81 kDa for this product. This experiment was performed under reducing conditions using the 12-230 kDa separation system.")
![Immunocytochemistry/Immunofluorescence: Mre11 Antibody [NB100-142] - IF analysis of Mre11 on HeLa. Image from verified customer review.](http://images.novusbio.com/fullsize/Mre11-Antibody-Immunocytochemistry-Immunofluorescence-NB100-142-img0009.jpg)
![<b>Genetic Strategies Validation. </b>Western Blot: Mre11 Antibody [NB100-142] - Mre11 and NBS1 contribute to OriP replication and EBV episome stability. D98/HR1 cells were transfected with siRNA for Mre11 or NBS1, or Luciferase control and assayed by immunoblot (IB) with antibodies specific for Mre11 (left pane) or NBS1 (right panel), or PCNA (lower panel) as a loading control. Image collected and cropped by CiteAb from the following publication (//journals.plos.org/plosone/article?id=10.1371/journal.pone.0001257) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/Mre11-Antibody-Knockdown-Validated-NB100-142-img0012.jpg)
![Immunohistochemistry: Mre11 Antibody [NB100-142] - Immunohistochemical staining of MRE11 in a human epidermis cross section.](http://images.novusbio.com/fullsize/Mre11-Antibody-Immunohistochemistry-NB100-142-img0004.jpg)
![Western Blot: Mre11 Antibody [NB100-142] - Western blot analysis of Mre11 on 50 ug of HeLa and MEF lysates, displaying bands at the molecular weight of 81 kDa.](http://images.novusbio.com/fullsize/Mre11-Antibody-Western-Blot-NB100-142-img0005.jpg)
![Immunocytochemistry/Immunofluorescence: Mre11 Antibody [NB100-142] - 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 anti-Mre11 [NB100-142] at a 1:500 dilution overnight at 4C and detected with an anti-rabbit DyLight 488 (Green) at a 1:500 dilution. Actin was detected with Phalloidin 568 (Red) at a 1:200 dilution. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 40X objective.](http://images.novusbio.com/fullsize/Mre11-Antibody-Immunocytochemistry-Immunofluorescence-NB100-142-img0011.jpg)
![Chromatin Immunoprecipitation: Mre11 Antibody [NB100-142] - Aggregated END-seq signal and MRE11 ChIP-seq RPM in WT (left) and Atm -/- (right). To fairly compare ChIP-seq signal between WT and Atm -/-, MRE11 scale is proportional to spike-in normalized END-seq RPM for each genotype. Individual hotspot examples (chr12:34,592,264-34,598,265) are shown below. Note that decreased MRE11 coverage is observed within NDR of Atm -/-. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32051414/) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/Mre11 Antibody-Chromatin Immunoprecipitation-NB100-142-img0013.jpg)
![<b>Genetic Strategies Validation. </b>Western Blot: Mre11 Antibody [NB100-142] - TIG-1 human primary fibroblasts, whole cell lysate (30 ug). Image from verified customer review.](http://images.novusbio.com/fullsize/Mre11-Antibody-Knockdown-Validated-NB100-142-img0008.jpg)
![Western Blot: Mre11 Antibody [NB100-142] - MRE11 associates with the DS region of OriP.A) DNA affinity purification assays were performed with Raji nuclear extracts & DNA templates derived from DS wt, DS nm-, or delta DS. Input & template bound proteins were analyzed by Western blot with antibodies to TRF2, MRE11, EBNA1, PCNA, & PARP1, as indicated. B) Schematic of template DNA used for DNA affinity purification in A, & their respective protein binding sites. C) ChIP assays to monitor EBNA1, TRF2, & MRE11 binding at OriP wt or OriP nm- in transfected 293 cells. Immunoprecipitated DNA was quantified by real time PCR relative to total input DNA recovered for each transfected cell. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/18040525), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-142_rabbit-polyclonal-mre11-antibody-310202415384114.jpg)
![Western Blot: Mre11 Antibody [NB100-142] - Immunoblotting analysis of IR-induced AKT (Ser473) activation. (A) The levels of AKT activation were measured by AKT Ser473 phosphorylation in 293T, 293T/eIF3f & 293T/eIF3f-hMSH4 cells treated with 10 Gy IR in comparison to untreated controls. Levels of p53 Ser15 phosphorylation & the total protein levels of AKT, hMRE11 & p53 were also analyzed. alpha -tubulin was used as a loading control. (B) The levels of Chk2 activation (Chk2 Thr68 phosphorylation) in 293T, 293T/eIF3f & 293T/eIF3f-hMSH4 cells in response to 10 Gy IR. Cell lysates were prepared at 1 hr post IR treatment. Untreated cells were analyzed as controls, while alpha -tubulin was used as a loading control. Image collected & cropped by CiteAb from the following publication (//molecular-cancer.biomedcentral.com/articles/10.1186/1476-4598-12-51), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-142_rabbit-polyclonal-mre11-antibody-310202415293334.jpg)
![Western Blot: Mre11 Antibody [NB100-142] - The DNA damage response at telomeres uncapped through TRF2 depletion does not require BRCA1 or CtIPImmortalized Brca1F/− MEFs were infected with retroviruses expressing the indicated shRNAs and/or Cre recombinase, followed by selection with puromycin for 72 h. Cell extracts were prepared 48 h later & analysed by Western blotting as indicated. SMC1 & tubulin were used as loading controls. *non-specific band.Cells treated as in (A) were fixed 48 h after selection & stained with an anti-53BP1 antibody (green). Telomeres were visualized with a Cy3-conjugated (CCCTAA)3-PNA probe (red). Yellow arrowheads point to 53BP1 foci that co-localize with telomeres.Quantification of TIFs in cells treated as in (B). A minimum of 200 nuclei were scored for each sample. Error bars represent SD of two independent experiments. P-values were calculated using an unpaired two-tailed t-test. *P ≤ 0.05; NS, P > 0.05. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/25582120), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-142_rabbit-polyclonal-mre11-antibody-31020241554548.jpg)
![Western Blot: Mre11 Antibody [NB100-142] - MRE11 & NBS1 contribute to OriP replication & EBV episome stability.A) D98/HR1 cells were transfected with siRNA for MRE11 or NBS1, or Luciferase control & assayed by immuno-blot (IB) with antibodies specific for MRE11 (left pane) or NBS1 (right panel), or PCNA (lower panel) as a loading control. B) Transient DNA replication assays of OriP-containing plasmids were analyzed by Southern blot. D98/HR1 cells were transfected with OriP plasmid & siRNA for either MRE11, NBS1, or luciferase control (as indicated above each lane). Hirt extracted plasmid DNA was digested with DpnI plus BamHI (top panel) or BamHI only (lower panel) & probed with OriP specific probes. DNA was quantified by PhosphorImager analysis & the replication value was determined as the ratio of DpnI/BamHI to BamHI recovered products. Quantification shown below is a summary of at least four independent replication assays (data not shown). C)) EBV episomes from latently infected D98/HR1 cells were analyzed by pulse field electrophoresis & Southern blotting after transfection of siRNA for control (siLuc), MRE11, or NBS1. Raji cells were used as a control for EBV episome size & abundance. The percentage of EBV episomes relative to the EBV DNA retained in the well is calculated below. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/18040525), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-142_rabbit-polyclonal-mre11-antibody-310202416574.jpg)
![Western Blot: Mre11 Antibody [NB100-142] - Evidence that MRE11 & NBS1 are required for EBV episome maintenance.A) OriP plasmid maintenance assays were performed in MRE11 mutant (ATLD3) & reconstituted (ATLD3/wtMRE11) cell lines (left panel) or NBS1 mutant (GM7166) & reconstituted (GM7166/wtNBS1) cell lines (right panel). Plasmids containing OriP & EBNA1 were monitored by Southern blotting of Hirt lysates at 1 (lower panel) & 7 (upper panel) days post-transfection. Phosphorimager quantification of four independent experiments as shown in panal A where maintenance is measured as the ratio of day 7 to day 1 for OriP plasmid detection is shown below. B) EBV transformed B-lymphocytes were analyzed by PFG & Southern blotting for the presence of episomal forms of the EBV genome. Raji, Namalwa, NBS1 (GM15808), NBS1 (GM07078), LCL3472, & LCLAW7 DNA was loaded at equal concentrations & analyzed by ethidium staining of PFG (lower panel) or by Southern blot (upper panel) with EBV specific probe. C) Western blot of the same cell lines used for PFG analysis shown in panel B was probed with antibodies specific for NBS1 (antibody 143 & antibody 277), MRE11, or loading control Actin. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/18040525), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-142_rabbit-polyclonal-mre11-antibody-31020241612675.jpg)
![Western Blot: Mre11 Antibody [NB100-142] - Involvement of CBP & p300 in the transcription of the BRCA1 & RAD51 genes.(A) Down-regulation of BRCA1 & RAD51 proteins upon depletion of CBP and/or p300. H1299 cells were transfected for 48 hr with non-targeting (siNT), CBP (siCBP), p300 (sip300), or CBP+p300 (siC+p) siRNAs. The cells were harvested & whole cell extracts were subjected to immunoblotting. (B, C) Reduction of BRCA1 & RAD51 transcripts in CBP- & p300-depleted cells. H1299 cells were transfected for 48 hr with non-targeting (siNT), CBP (siCBP), p300 (sip300), or CBP+p300 (siC+p) siRNAs. Cells were harvested & subjected to quantitative real-time PCR for the detection of BRCA1 (B) & RAD51 (C) mRNAs. Expression levels were normalized against the levels of GAPDH mRNA. Data represent the mean ± SD. (D) H1299 cells were transfected for 48 hr with non-targeting (siNT), CBP (siCBP), p300 (sip300), or CBP+p300 (siC+p) siRNAs, & stained with propidium iodide (PI). The percentage of cells in each cell cycle phase was determined by FACS. Percentages of cells in G1, S, & G2/M are shown. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/23285190), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-142_rabbit-polyclonal-mre11-antibody-310202415525210.jpg)
![Western Blot: Nbs1 Antibody [NB100-143] - Lysates of HeLa human cervical epithelial carcinoma parental cell line and Nbs1 knockout (KO) HeLa cell line. PVDF membrane was probed with 1:1000 of Rabbit Anti-Human Polyclonal [NB100-143] followed by HRP-conjugated Anti-Rabbit IgG Secondary Antibody (HAF008). Specific band was detected for Nbs1 at approximately 95 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/Nbs1-Antibody-Knockout-Validated-NB100-143-img0015.jpg "<b>Genetic Strategies Validation. </b>Western Blot: Nbs1 Antibody [NB100-143] - Lysates of HeLa human cervical epithelial carcinoma parental cell line and Nbs1 knockout (KO) HeLa cell line. PVDF membrane was probed with 1:1000 of Rabbit Anti-Human Polyclonal [NB100-143] followed by HRP-conjugated Anti-Rabbit IgG Secondary Antibody (HAF008). Specific band was detected for Nbs1 at approximately 95 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: Nbs1 Antibody [NB100-143] - Western Blot with Nbs1 Antibody [NB100-143]. KSHV LANA recruits MRN (Mre11-Rad50-NBS1) complex. Co-immunoprecipitation of endogenous LANA and MRN proteins in BC3 cells. Cells were lysed using TBS-T buffer and the cell lysate was incubated with benzonase. After centrifugation, supernatant was incubated overnight with anti-LANA or IgG-control beads. The precipitated complexes were analyzed for the presence of endogenous Rad50, Mre11 and NBS1 by SDS-PAGE and immunoblotting. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.ppat.1006335), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/Nbs1-Antibody-Western-Blot-NB100-143-img0016.jpg)
![Immunocytochemistry/Immunofluorescence: Nbs1 Antibody [NB100-143] - ICC/IF analysis of Nbs1 in HeLa cells with Nbs1 Antibody [NB100-143]. Image from verified customer review.](http://images.novusbio.com/fullsize/Nbs1-Antibody-Immunocytochemistry-Immunofluorescence-NB100-143-img0011.jpg)
![Immunohistochemistry-Paraffin: Nbs1 Antibody [NB100-143] - FFPE human testis using Nbs1 antibody [NB100-143] at 1:200 on a Bond Rx autostainer (Leica Biosystems). The assay involved 20 minutes of heat induced antigen retrieval (HIER) using 10 mM sodium citrate buffer (pH 6.0) and endogenous peroxidase quenching with peroxide block. The sections were incubated with primary antibody for 30 minutes and Bond Polymer Refine Detection (Leica Biosystems) with DAB was used for signal development followed by counterstaining with hematoxylin. Whole slide scanning and capturing of representative images was performed using Aperio AT2 (Leica Biosystems). Staining was performed by Histowiz.](http://images.novusbio.com/fullsize/Nbs1-Antibody-Immunohistochemistry-Paraffin-NB100-143-img0014.jpg)
![Western Blot: Nbs1 Antibody [NB100-143] - Analysis of HeLa whole cell lysate [NB800-PC1] using rabbit polyclonal NBS1 antibody [NB100-143]. Observed Molecular Weight at ~95 kDa.](http://images.novusbio.com/fullsize/Nbs1-Antibody-Western-Blot-NB100-143-img0010.jpg)
![<b>Genetic Strategies Validation. </b>Western Blot: Nbs1 Antibody [NB100-143] - Detection of NBS1 in Human Bone Osteosarcoma Epithelial Cells (U2OS whole cell lysate) using Nbs1 Antibody [NB100-143] at a dilution of 1:1000. Specificity was confirmed using a siRNA anti-NBS1 (targeting sequence: GGAAGAAACGUGAACUCAA). Image provided by Sebastien Britton of the Institute of Pharmacology and Structural Biology.](http://images.novusbio.com/fullsize/Nbs1-Antibody-Western-Blot-NB100-143-img0012.jpg)
![Western Blot: Nbs1 Antibody [NB100-143] - Western Blot with Nbs1 Antibody [NB100-143]. TIG-1 human primary fibroblasts, whole cell lysate (30 ug). Image from verified customer review.](http://images.novusbio.com/fullsize/Nbs1-Antibody-Western-Blot-NB100-143-img0013.jpg)
![Immunocytochemistry/Immunofluorescence: Nbs1 Antibody [NB100-143] - Staining of HeLa cells using Nbs1 Antibody [NB100-143].](http://images.novusbio.com/fullsize/Nbs1-Antibody-Immunocytochemistry-Immunofluorescence-NB100-143-img0009.jpg)
![<b>Genetic Strategies Validation. </b>Immunocytochemistry/ Immunofluorescence: Nbs1 Antibody [NB100-143] - TOPBP1 recruitment in response to rDNA breaks. TOPBP1 localization 2 h after I-Ppo1 transfection in NBS1-delta-N cells and NBS1-delta-N cells complemented with wild-type and mutant NBS1-mNG (percentage of cells with > 2 TOPBP1 caps are indicated; one of two experiments is shown). Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31913317/) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/Nbs1 Antibody-Knockdown Validated-NB100-143-img0017.jpg)
![Immunocytochemistry/ Immunofluorescence: Nbs1 Antibody [NB100-143] - Replication centers of the integrated HPV recruit Mre11-Nbs1-Rad50 complex & Ku70/80 heterodimer.HeLa cells were transfected & analyzed as described previously. Co-immunostaining of HPV18 E1 (Alexa Fluor 568, second column) & the following proteins are presented: Mre11, Nbs1, Rad50, & Ku70/80 proteins (Alexa Fluor 488, first column). The localizations of the E1 & the respective DNA repair proteins are also shown in the third column as a merged image & DAPI stained nuclei are presented in the fourth column. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/19390600), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-143_rabbit-polyclonal-nbs1-antibody-310202415291962.jpg)
![Immunocytochemistry/ Immunofluorescence: Nbs1 Antibody [NB100-143] - Loss of MUS81 activates DNA damage responseA. MUS81 depleted U2OS cells accumulate NBS1 foci defining sites of DNA damage. B. Partial co-localization of NBS1 foci & RPA foci in MUS81-depleted cells. C. Co-localization of RPA foci to ssDNA regions. Cells were labelled with BrdU for 3 days concomitant with MUS81 depletion. BrdU was detected at ssDNA regions by immunofluorescence. D. NBS1 foci arise in cells that are both positive & negative for Cyclin A expression. Scale bars, 5 μm. E. NBS1 foci form largely at non-telomeric loci. F. Partial co-localization of NBS1 foci with PML nuclear bodies. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26415217), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-143_rabbit-polyclonal-nbs1-antibody-310202415395910.jpg)
![Immunocytochemistry/ Immunofluorescence: Nbs1 Antibody [NB100-143] - Loss of MUS81 activates DNA damage responseA. MUS81 depleted U2OS cells accumulate NBS1 foci defining sites of DNA damage. B. Partial co-localization of NBS1 foci & RPA foci in MUS81-depleted cells. C. Co-localization of RPA foci to ssDNA regions. Cells were labelled with BrdU for 3 days concomitant with MUS81 depletion. BrdU was detected at ssDNA regions by immunofluorescence. D. NBS1 foci arise in cells that are both positive & negative for Cyclin A expression. Scale bars, 5 μm. E. NBS1 foci form largely at non-telomeric loci. F. Partial co-localization of NBS1 foci with PML nuclear bodies. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26415217), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-143_rabbit-polyclonal-nbs1-antibody-310202415293317.jpg)
![Immunocytochemistry/ Immunofluorescence: Nbs1 Antibody [NB100-143] - Loss of MUS81 activates DNA damage responseA. MUS81 depleted U2OS cells accumulate NBS1 foci defining sites of DNA damage. B. Partial co-localization of NBS1 foci & RPA foci in MUS81-depleted cells. C. Co-localization of RPA foci to ssDNA regions. Cells were labelled with BrdU for 3 days concomitant with MUS81 depletion. BrdU was detected at ssDNA regions by immunofluorescence. D. NBS1 foci arise in cells that are both positive & negative for Cyclin A expression. Scale bars, 5 μm. E. NBS1 foci form largely at non-telomeric loci. F. Partial co-localization of NBS1 foci with PML nuclear bodies. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26415217), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-143_rabbit-polyclonal-nbs1-antibody-31020241534354.jpg)
![Immunocytochemistry/ Immunofluorescence: Nbs1 Antibody [NB100-143] - Loss of MUS81 activates DNA damage responseA. MUS81 depleted U2OS cells accumulate NBS1 foci defining sites of DNA damage. B. Partial co-localization of NBS1 foci & RPA foci in MUS81-depleted cells. C. Co-localization of RPA foci to ssDNA regions. Cells were labelled with BrdU for 3 days concomitant with MUS81 depletion. BrdU was detected at ssDNA regions by immunofluorescence. D. NBS1 foci arise in cells that are both positive & negative for Cyclin A expression. Scale bars, 5 μm. E. NBS1 foci form largely at non-telomeric loci. F. Partial co-localization of NBS1 foci with PML nuclear bodies. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26415217), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-143_rabbit-polyclonal-nbs1-antibody-31020241539451.jpg)
![Immunocytochemistry/ Immunofluorescence: Nbs1 Antibody [NB100-143] - HPV16 E2 partially colocalizes with the MRN complex proteins Mre11 & Nbs1. C33a cells were transfected with an HPV16 E2 expression plasmid, fixed in ice-cold methanol, & stained with an E2-specific antibody (green). DNA was stained with Hoechst 33342 (blue). (A) Endogenous Nbs1 was detected with an Nbs1-specific antibody (red/gray). (B) Endogenous Mre11 was detected with an Mre11-specific rabbit antibody (red/gray). Bar, 5 μm. Digital zoom is shown at the bottom. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28031358), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-143_rabbit-polyclonal-nbs1-antibody-310202415392545.jpg)
![Immunocytochemistry/ Immunofluorescence: Nbs1 Antibody [NB100-143] - Loss of MUS81 activates DNA damage responseA. MUS81 depleted U2OS cells accumulate NBS1 foci defining sites of DNA damage. B. Partial co-localization of NBS1 foci & RPA foci in MUS81-depleted cells. C. Co-localization of RPA foci to ssDNA regions. Cells were labelled with BrdU for 3 days concomitant with MUS81 depletion. BrdU was detected at ssDNA regions by immunofluorescence. D. NBS1 foci arise in cells that are both positive & negative for Cyclin A expression. Scale bars, 5 μm. E. NBS1 foci form largely at non-telomeric loci. F. Partial co-localization of NBS1 foci with PML nuclear bodies. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26415217), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-143_rabbit-polyclonal-nbs1-antibody-310202415175283.jpg)
![Western Blot: Nbs1 Antibody [NB100-143] - UFL1 regulates the ATM signaling. a U2OS cells expressing UFL1 tet-on shRNA1 were irradiated with 2 Gy IR. Thirty minutes later, cells were lysed & blotted with indicated antibodies. b Representative picture of gamma H2AX, 53BP1, & BRCA1 foci in control (Dox-) & UFL1 knockdown (Dox+) U2OS cells 1 h after 0.5 Gy treatment. Scale bars, 10 µm. c–e Quantification of intensities of gamma H2AX, 53BP1, & BRCA1 foci in control (Dox-) & UFL1 knockdown (Dox+) U2OS cells. Data presented as mean ± SD of n = 50 cells. **p 100 cells. Error bars = SD. *** p-value <0.0001, unpaired two-tailed t-test.DOI://dx.doi.org/10.7554/eLife.07270.005Inhibition of oxidative stress reduces cell migration and invasion.ROS inhibitor NAC reduces cell migration to a similar extent as ATM-depletion. siATM and siNC control MDA-MB-231 cells were either untreated or treated with NAC and analyzed as in Figure 2D for cell migration. Right panel: Western blot of ATM depletion and quantification of cell migration for each sample.DOI://dx.doi.org/10.7554/eLife.07270.006 Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/26030852), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-143_rabbit-polyclonal-nbs1-antibody-knockdown-validated-13220261817564.jpg)
![Immunocytochemistry/Immunofluorescence: Ki67/MKI67 Antibody [NB500-170] - HeLa 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- NB500-170 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/Ki67-MKI67-Antibody-Immunocytochemistry-Immunofluorescence-NB500-170-img0025.jpg "Immunocytochemistry/Immunofluorescence: Ki67/MKI67 Antibody [NB500-170] - HeLa 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- NB500-170 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.")
![<b>Genetic Strategies Validation. </b>Simple Western: Ki67/MKI67 Antibody [NB500-170] - Detection of Ki67/MKI67 by Simple WesternTM. Simple Western lane view shows lysates of HeLa parental cell line and Ki67 knockout (KO) HeLa cell line. A specific band was detected for Ki67/MKI67 at approximately 320 kDa (as indicated) in the parental cell line, but is not detectable in the knockout HeLa cell line using 20 ug/mL of Rabbit Anti-Ki67/MKI67 Polyclonal Antibody (Catalog # NB500-170). GAPDH is shown as a loading control. This experiment was conducted under reducing conditions and using the 12-230 kDa separation system.](http://images.novusbio.com/fullsize/Ki67-MKI67-Antibody-Knockout-Validated-NB500-170-img0023.jpg)
![Immunohistochemistry: Ki67/MKI67 Antibody [NB500-170] - Senescent MSPCs are characterized by loss of nestin expression. Double-immunofluorescence images of femoral metaphysis sections from 4-, 6-, 8-, and 12-week-old male Nestin-GFP mice using antibodies against GFP (green) and Ki67 (red). DAPI stains nuclei blue. GP growth plate. PS primary spongiosa. Quantification of the percentage of GFP+ cells that express Ki67. Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/s41467-017-01509-0) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/Ki67-MKI67-Antibody-Immunocytochemistry-Immunofluorescence-NB500-170-img0022.jpg)
![Immunohistochemistry-Paraffin: Ki67/MKI67 Antibody [NB500-170] - Ki-67/MKI67 Antibody [NB500-170] - Tissue section of human tonsil using 1:50 dilution of rabbit anti-KI67 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 Ki67 antibody generated a specific nuclear staining in the cells in germinal centers of the tested tonsil tissue.](http://images.novusbio.com/fullsize/Ki-67-MKI67-Antibody-Immunohistochemistry-Paraffin-NB500-170-img0019.jpg)
![Immunohistochemistry-Paraffin: Ki67/MKI67 Antibody [NB500-170] - Ki-67/MKI67 Antibody [NB500-170] - Human tonsil using 1:200 dilution of rabbit anti-KI67 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 Ki67 antibody generated a specific nuclear staining in the cells in germinal centers of the tested tonsil tissue.](http://images.novusbio.com/fullsize/Ki-67-MKI67-Antibody-Immunohistochemistry-Paraffin-NB500-170-img0020.jpg)
![Western Blot: Ki67/MKI67 Antibody - BSA Free [NB500-170] - Whole cell lysates from SUM159, MDA-MB-231 and MCF-7 cells were loaded with 30 ug/lane. 10% SDS-PAGE. Ki67/MKI67 antibody (NB500-170) was used for primary antibody: 1:2000, 4C, overnight. Image from verified customer review.](http://images.novusbio.com/fullsize/Ki67-MKI67-Antibody---BSA-Free-Western-Blot-NB500-170-img0028.jpg)
![Immunocytochemistry/Immunofluorescence: Ki67/MKI67 Antibody [NB500-170] - 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-Ki67/MKI67 Antibody NB500-170 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/Ki67-MKI67-Antibody-Immunocytochemistry-Immunofluorescence-NB500-170-img0026.jpg)
![Flow Cytometry: Ki67/MKI67 Antibody - BSA Free [NB500-170] - An intracellular stain was performed on U-251 MG cells with Ki67/MKI67 Antibody NB500-170AF594 (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 2.5 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to Alexa Fluor 594.](http://images.novusbio.com/fullsize/Ki67-MKI67-Antibody---BSA-Free-Flow-Cytometry-NB500-170-img0027.jpg)
![Western Blot: Ki67/MKI67 Antibody [NB500-170] - Ki-67/MKI67 Antibody [NB500-170] - Analysis of A431 (A) and Hek293 (B) cell lysate using Ki67 antibody (NB500-170) at 2 ug/ml.](http://images.novusbio.com/fullsize/Ki-67-MKI67-Antibody-Western-Blot-NB500-170-img0017.jpg)
![Immunocytochemistry/Immunofluorescence: Ki67/MKI67 Antibody [NB500-170] - Ki67 antibody was tested at 1:25 in HeLa cells with FITC (green). Nuclei and actin were counterstained with Dapi (blue) and Phalloidin (red).](http://images.novusbio.com/fullsize/Ki-67-MKI67-Antibody-Immunocytochemistry-Immunofluorescence-NB500-170-img0014.jpg)
![Immunocytochemistry/Immunofluorescence: Ki67/MKI67 Antibody [NB500-170] - Confocal immunofluorescent analysis of MCF7 cells using Ki67 antibody (NB500-170, 1:5). An Alexa Fluor 488-conjugated Goat to rabbit IgG was used as secondary antibody (green). Actin filaments were labeled with Alexa Fluor 568 phalloidin (red). DAPI was used to stain the cell nuclei (blue).](http://images.novusbio.com/fullsize/Ki-67-MKI67-Antibody-Immunocytochemistry-Immunofluorescence-NB500-170-img0016.jpg)
![Immunocytochemistry/Immunofluorescence: Ki67/MKI67 Antibody [NB500-170] - A431 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- NB500-170 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/Ki67-MKI67-Antibody-Immunocytochemistry-Immunofluorescence-NB500-170-img0024.jpg)
![Immunohistochemistry-Paraffin: Ki67/MKI67 Antibody [NB500-170] - Ki-67/MKI67 Antibody [NB500-170] - Human tonsil.](http://images.novusbio.com/fullsize/Ki-67-MKI67-Antibody-Immunohistochemistry-Paraffin-NB500-170-img0015.jpg)
![Immunohistochemistry: Ki67/MKI67 Antibody - BSA Free [NB500-170] - PKD2 enzymatic deficiency had no effect on the proliferation or apoptosis of intestinal epithelial cells in mice exposed to DSS.(a) Representative 200× immunohistochemical images (left) & quantification of Ki-67+ proliferating intestinal epithelial cells (right) in wild-type & PKD2SSAA/SSAA mice. Bar represents 5 μm. (b) Representative 200× immunohistochemical images (left) & quantification of cleaved Caspase-3+ apoptotic intestinal epithelial cells (right) in wild-type & PKD2SSAA/SSAA mice. Bar represents 5 μm. Results are representative of three separate experiments with three mice per group. All p > 0.05 as measured by one way-ANOVA among four groups. Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/srep34079), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb500-170_rabbit-polyclonal-ki67-mki67-antibody-3102024153437.jpg)
![Immunohistochemistry: Ki67/MKI67 Antibody - BSA Free [NB500-170] - Deletion of Vangl2, but not Vangl1, in the mammary gland results in narrow ducts & low cell turnover. (A) RT-qPCR analysis of Vangl1 & Vangl2 mRNA levels in the mammary glands of MMTV-Cre, MMTV-Cre;Vangl2flox/+ & MMTV-Cre;Vangl2flox/flox at 10 weeks of age. (B) Representative images of 10 week old, carmine stained mammary glands & quantification of total branch number from MMTV-Cre, MMTV-Cre;Vangl2flox/+ & MMTV-Cre;Vangl2flox/flox mice (n = 3 mice per genotype). (C) Histological analysis by H&E staining show normal duct formation in 10 week old MMTV-Cre & MMTV-Cre;Vangl2flox/+ glands, whereas ducts from MMTV-Cre;Vangl2flox/flox glands are narrow & have significantly diminished lumens (n = 3 mice/genotype). (D) Immunostaining in mammary ducts show normal distribution of luminal (Cytokeratin 8 (K8), green), & basal (K5), red; SMA magenta) cell populations. (E) Immunofluorescence of adhesion junctional protein E-Cadherin (CDH1, green) & apical membrane marker pERM (red). (F,G) Immunostaining in 10 week old MMTV-Cre;Vangl2+/+ & MMTV-Cre;Vangl2flox/flox glands & quantitation of (F) Ki67 & (G) Cleaved Caspase 3 (n = 3–5 mice per genotype). Lu indicates lumen. * indicates non-magnified duct. Data are represented as mean +/− SEM. Scale bar represents 100 μm (C,F,G) 50 μm (D) & 10 μm (E). Student’s t-test *p < 0.05 & ****p < 0.0001. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31068622), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb500-170_rabbit-polyclonal-ki67-mki67-antibody-310202416171470.jpg)
![Immunocytochemistry/ Immunofluorescence: Ki67/MKI67 Antibody - BSA Free [NB500-170] - Senescent MSPCs are characterized by loss of nestin expression. a, b Representative images of GFP immunofluorescence staining (green) & quantitative analysis of GFP+ cells in femoral primary spongiosa from 4, 6, 8, & 12-week-old male Nestin-GFP mice. Images in upper panels in a are lower power w/ boxes outlining area of higher power in lower panels. Numbers of GFP+ cells per mm2 tissue area in primary spongiosa (N. GFP+ cells/PS.Ar) b. 4W, 6W, 8W, & 12W represent 4-, 6-, 8-, & 12-week-old mice, respectively. DAPI stains nuclei blue. c, d Representative images of flow cytometry analysis (c) & % of CD45−GFP+ cells (d) in femoral metaphysis from 4-, 6-, 8-, & 12-week-old male Nestin-GFP mice. e, f Double-immunofluorescence images of femoral metaphysis sections from 4-, 6-, 8-, & 12-week-old male Nestin-GFP mice using antibodies against GFP (green) & Ki67 (red) e. DAPI stains nuclei blue. GP growth plate. PS primary spongiosa. Quantification of % of GFP+ cells that express Ki67 f. Five mice per group. Data are represented as mean ± s.e.m. *P < 0.05 as determined by ANOVA. g Diagram showing isolation of Nestin-GFP+ (red) & Nestin-GFP− (purple) mesenchymal stem/progenitor cells (MSPCs) by fluorescence-activated cell sorting. Detailed information on isolation of MSPCs from femoral metaphysis from Nestin-GFP mice are described in Supplementary Fig. 3 & Methods section. h–j The sorted cells cultured, & SA-beta Gal staining (h), BrdU incorporation (i), & p16INK4a immunostaining (j) performed, & representative images shown. k–m Quantification of % of cells that express SA-beta Gal (k), BrdU (l), & p16INK4a (m). n = 5. Data are represented as mean ± s.e.m. *P < 0.01 as determined by Student’s t-tests Image collected & cropped by CiteAb from following publication (//pubmed.ncbi.nlm.nih.gov/29101351), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb500-170_rabbit-polyclonal-ki67-mki67-antibody-310202416175292.jpg)
![Immunocytochemistry/ Immunofluorescence: Ki67/MKI67 Antibody - BSA Free [NB500-170] - Cellular senescence occurs in primary spongiosa of long bone during late puberty. a–e Representative senescence-associated beta -galactosidase (SA-beta Gal) staining (blue) & quantitative analysis of SA-beta Gal+ cells in femoral metaphysis (a–c) & diaphysis (d, e) sections from increasing ages of male mice. 4, 6, 8, & 12W represent 4-, 6-, 8-, & 12-week-old mice, respectively. Images in a are lower power with boxes outlining the area of higher power in b. Numbers of SA-beta Gal+ cells per mm2 tissue area in primary spongiosa (N. SA-beta Gal+ cells/PS.Ar) (c) & diaphysis (N. SA-beta Gal+ cells/DP.Ar) (e). Counterstained with eosin (pink). f, g Representative images of immunofluorescence staining (f) & quantitative analysis of ki67+ (g) cells (red) in femoral primary spongiosa from 4, 6, 8, & 12-week-old male mice. DAPI stains nuclei blue. Images in upper panels in f are lower power with boxes outlining the area of higher power in lower panels. Five mice per group. Data are represented as mean ± s.e.m. Ar tissue area, DP diaphysis, GP growth plate, N number, PS primary spongiosa. *P < 0.01 as determined by ANOVA Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29101351), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb500-170_rabbit-polyclonal-ki67-mki67-antibody-310202416175289.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)
![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 "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.")
![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)
![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)
![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)
![Immunocytochemistry/Immunofluorescence: Ki67/MKI67 Antibody (SP6) - Unpurified [NB600-1252] - T47D cells form functional 3D spheroids in a scaffold-free system. Sections of 3D microtissues grown for 12 days were incubated with DAPI and an antibody against Ki67 (green) to stain proliferative cells analyzed by fluorescence microscopy. Nuclei were visualized with DAPI (blue). Image collected and cropped by CiteAb from the following publication (//doi.wiley.com/10.1002/cam4.630), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/Ki67-MKI67-Antibody-SP6-Unpurified-Immunocytochemistry-Immunofluorescence-NB600-1252-img0008.jpg "Immunocytochemistry/Immunofluorescence: Ki67/MKI67 Antibody (SP6) - Unpurified [NB600-1252] - T47D cells form functional 3D spheroids in a scaffold-free system. Sections of 3D microtissues grown for 12 days were incubated with DAPI and an antibody against Ki67 (green) to stain proliferative cells analyzed by fluorescence microscopy. Nuclei were visualized with DAPI (blue). Image collected and cropped by CiteAb from the following publication (//doi.wiley.com/10.1002/cam4.630), licensed under a CC-BY license.")
![Immunohistochemistry: Ki67/MKI67 Antibody (SP6) - Unpurified [NB600-1252] - PW-12 is efficacious in an orthotopic flank tumor model of MYCN-amplified medulloblastoma. Mice were implanted with 6 x 106 SmoWT medulloblastoma cells in the hindflank. Animals were treated for 7 days with 25 mg/kg of PW-12 (n = 5) or vehicle alone (n = 5). Histology on H&E stain is consistent with medulloblastoma (H&E, 20x). Tumor cell proliferation (Ki67, 40x) was decreased, apoptosis (cleaved-caspase-3, 40x) increased, MYCN (20x) expression downregulated, and vascularity decreased in PW-12 treated tumors as confirmed by histology and cell quantification for apoptosis and cell proliferation. Image collected and cropped by CiteAb from the following publication (//www.frontiersin.org/Cancer_Molecular_Targets_and_Therapeutics/10.3389/fonc.2015.00111/abstract), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/Ki67-MKI67-Antibody-SP6-Unpurified-Immunohistochemistry-NB600-1252-img0007.jpg)
![Immunohistochemistry-Paraffin: Ki67/MKI67 Antibody (SP6) - Unpurified [NB600-1252] - Formalin fixed paraffin embedded human tonsil stained with Ki-67 antibody.](http://images.novusbio.com/fullsize/Ki67-MKI67-Antibody-SP6-Unpurified-Immunohistochemistry-Paraffin-NB600-1252-img0001.jpg)
![Immunohistochemistry-Paraffin: Ki67/MKI67 Antibody (SP6) - Unpurified [NB600-1252] - Ki-67/MKI67 Antibody (SP6) [NB600-1252] - Formalin fixed paraffin embedded human tonsil stained with Ki-67 antibody.](http://images.novusbio.com/fullsize/Ki67-MKI67-Antibody-SP6-Unpurified-Immunohistochemistry-Paraffin-NB600-1252-img0002.jpg)
![Immunohistochemistry: Ki67/MKI67 Antibody (SP6) - Unpurified [NB600-1252] - Paraffin-embedded alcohol fixed rat spleen tissue (20x). Antigen retrieval pH 9. Ki67 dilution 1:100 incubation ON 4C. This image was submitted via customer review.](http://images.novusbio.com/fullsize/Ki67-MKI67-Antibody-SP6-Unpurified-Immunohistochemistry-NB600-1252-img0005.jpg)
![Immunohistochemistry: Ki67/MKI67 Antibody (SP6) - Unpurified [NB600-1252] - PW-12 is efficacious in a GEM model of MYCN-amplified neuroblastoma. Tumor-bearing TH-MYCN mice were treated for 14 days with either 25 mg/kg of PW-12 (n = 3) or vehicle alone (n = 3). Histology for Ki67 and c-Caspase 3 shows increase in apoptosis and decrease in proliferation in treated tumors. Image collected and cropped by CiteAb from the following publication (//www.frontiersin.org/Cancer_Molecular_Targets_and_Therapeutics/10.3389/fonc.2015.00111/abstract), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/Ki67-MKI67-Antibody-SP6-Unpurified-Immunohistochemistry-NB600-1252-img0006.jpg)
![Immunohistochemistry: Ki67/MKI67 Antibody (SP6) - Unpurified [NB600-1252] - Ki-67/MKI67 Antibody (SP6) [NB600-1252] - Ki67 staining in mouse thyroid tissue at pre-tumor stage (green). Dilution is 1:100. This image was submitted via customer Review.](http://images.novusbio.com/fullsize/Ki67-MKI67-Antibody-SP6-Unpurified-Immunohistochemistry-NB600-1252-img0003.jpg)
![Immunohistochemistry-Paraffin: Ki67/MKI67 Antibody (SP6) - Unpurified [NB600-1252] - Ki-67 (NB600-1252) immunoreactivity in an FFPE section of mouse small intestine. Primary antibody was diluted 1:100 and left on sections for 1h at room temperature. Secondary antibody was Horse Anti-Rabbit HRP. Image from verified customer review.](http://images.novusbio.com/fullsize/nb600-1252_rabbit-monoclonal-ki67-mki67-antibody-sp6-unpurified-immunohistochemistry-paraffin-204202311437.jpg)
![Immunohistochemistry-Paraffin: Rabbit Monoclonal Ki67/MKI67 Antibody (SP6) - Unpurified [NB600-1252] - Image depicting Ki67/MKI67 immunoreactivity in a FFPE section of human tonsil. NB600-1252 was diluted 1-100 and left on tissue sections for 30m at room temperature. Secondary was horse anti rabbit HRP polymer. Image from a verified customer review.](http://images.novusbio.com/fullsize/nb600-1252_rabbit-monoclonal-ki67-mki67-antibody-sp6-unpurified-immunohistochemistry-paraffin-2442024135233..png)
![Immunohistochemistry-Paraffin: Rabbit Monoclonal Ki67/MKI67 Antibody (SP6) - Unpurified [IMGENEX: IMG-80336] [NB600-1252] - Images depicting Ki67/MKI67 immunoreactivity in FFPE sections of canine cecum and skin. NB600-1252 was diluted 1-100 and left on tissue sections for 30m at room temperature. Image from a verified customer review.](http://images.novusbio.com/fullsize/nb600-1252_rabbit-monoclonal-ki67-mki67-antibody-sp6-unpurified-imgenex-img-80336-immunohistochemistry-paraffin-1052024152017..jpg)
![Immunohistochemistry-Paraffin: Ki67/MKI67 Antibody (SP6) - Unpurified [NB600-1252] - Immunohistochemistry of tissue slices treated with trastuzumab & docetaxel. (Ki-67, arrows; A-C) & (cleaved caspase-3, arrows; D-F) were quantified by counting the number of positively stained cells in 4 fields of view at x40. Images are representative of untreated (A, D), trastuzumab at 100 µg/ml (B & E) & docetaxel at 100 nM (C & F). Images were digitally scanned ×40 (AlexaSoft X-PRO). Image collected & cropped by CiteAb from the following publication (//www.spandidos-publications.com/10.3892/or.2015.4074), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-1252_rabbit-monoclonal-ki67-mki67-antibody-sp6-unpurified-310202415371921.jpg)
![Immunohistochemistry: Ki67/MKI67 Antibody (SP6) - Unpurified [NB600-1252] - (A–C) Inflammatory cell infiltration & cell division in the nasal RM were evaluated using immunohistochemical staining (brown). Tissue sections were counterstained with the nuclear dye hematoxylin (blue). Representative immunohistochemical images of neutrophils (A), CD3+ lymphocytes (B), & Ki67+ dividing cells (C) (400× magnification), & comparative charts of cell counts in each group. *P < 0.01; **P < 0.01; ****P < 0.0001 (n = 6, one-way analysis of variance). OVA, ovalbumin; CSS, cigarette smoke solution. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32132898), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-1252_rabbit-monoclonal-ki67-mki67-antibody-sp6-unpurified-310202415284528.jpg)
![Immunohistochemistry: Ki67/MKI67 Antibody (SP6) - Unpurified [NB600-1252] - In vivo anti-tumor effect of Y-TR1 in the NOD/SCID mouse xenograft model using CD26 positive MM cell line JMN. (A) Y-TR1 administered intraperitoneally 4 mg/kg/dose, three times per week, for a total of nine doses from day zero of subcutaneous inoculation of 1 × 107 JMN cells. Average estimated tumor volume on day 55 compared among three groups (control, YS110, Y-TR1, n = 10) w/ Fisher’s protected least protected difference multiple comparison test. Mean tumor volume of the Y-TR1 group significantly lower (* p < 0.05) than that of the control or YS110 group. Mean tumor volume of the YS110 group not significantly altered compared w/ the control. An experiment out of two w/ similar results is shown; (B) Y-TR1 administered intraperitoneally 8 mg/kg/dose, three times per week, for a total of nine doses. The average estimated tumor weight on day 42 compared among three groups (control, 14D10, YS110, Y-TR1, n = 10) w/ Fisher’s protected least protected difference multiple comparison test. Mean tumor weight of the YS110 or Y-TR1 groups significantly lower (* p < 0.05 or ** p < 0.025, respectively) than that of the control group. Mean tumor weight of the Y-TR1 group significantly lower (* p < 0.05) than that of the YS110 group. An experiment out of two w/ similar results is shown; (C) histological analysis of xenograft tumors of JMN cells. JMN-derived tumors show histopathology of sarcomatoid mesothelioma. (×20). a: Hematoxylin & eosin staining. b: Immunohistochemical staining w/ anti-human CD26 antibody revealed CD26 expression in tumor cells. c–e: MIB-1 (Ki67) staining showed a decreased number of MIB-1-positive cells in Y-TR1-treated tumors compared to IgG1- or YS110-treated tumors. Scale bar: 10 μm. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31398954), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-1252_rabbit-monoclonal-ki67-mki67-antibody-sp6-unpurified-310202416165616.jpg)
![Immunohistochemistry: Ki67/MKI67 Antibody (SP6) - Unpurified [NB600-1252] - Representative images of immunohistological staining (brown) of OMP-positive (OMP+) cells (A), SOX2+ ORN progenitor cells (B), GAP43+ immature ORNs (C), Ki67+ proliferating cells (D), & cleaved Cas3+ apoptotic cells (E). Each cell except for many OMP+ cells is indicated by arrows. Tissue sections were counterstained with the nuclear dye hematoxylin (blue). Numbers of SOX2+ ORN progenitors & Ki67+ actively proliferating cells per mm of the basal layer & OMP+ mature ORNs, GAP43+ immature ORNs, & Cas3+ apoptotic cells per mm of the OE in saline or rhIGF-1-treated mice. Open circles, rectangles, & triangles represent the values for each mouse in the saline, low-IGF-1, & high-IGF-1 treated groups (each n = 6), respectively. The horizontal lines represent the mean value for each group. ∗P < 0.05; ∗∗P < 0.01; ∗∗∗P < 0.001; & ∗∗∗∗P < 0.0001 (one-way ANOVA). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30515092), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-1252_rabbit-monoclonal-ki67-mki67-antibody-sp6-unpurified-310202416182632.jpg)
![Immunohistochemistry: Ki67/MKI67 Antibody (SP6) - Unpurified [NB600-1252] - (A) Serum immunoglobin E (IgE) levels of the control & cigarette smoke solution (CSS)-treated mice were determined by enzyme linked immunosorbent assay. (B) Representative images of Sirius red staining for eosinophils & periodic acid-Schiff & Alcian blue (PAS/AB) staining for goblet cells in the nasal RM of the control mice & mice treated with 10 doses of CSS (CSS 10). (C) Representative immunohistochemical images of neutrophils & Ki67+ dividing cells in the nasal RM (400× magnification), & comparative charts of Ki67+ cell counts (n = 6, Mann–Whitney U test). (D) Representative images of olfactory marker protein (OMP)+ mature olfactory receptor neurons (ORNs) in two different areas of the olfactory epithelium: the nasal septum & upper lateral area. There were no significant differences in the number of OMP+ mature ORNs between the control & CSS-treated mice (n = 6, Mann–Whitney U test). OVA, ovalbumin. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32132898), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-1252_rabbit-monoclonal-ki67-mki67-antibody-sp6-unpurified-310202416173541.jpg)
![Immunohistochemistry: Ki67/MKI67 Antibody (SP6) - Unpurified [NB600-1252] - (A,B) Representative images of hematoxylin & eosin (H&E)-stained sections of the olfactory epithelium from young adult mice (A, 40× magnification; B, 400× magnification). A black line in (A) indicates the range for counting the number of each cell type. The box in (A) indicates the region of the olfactory epithelium shown at a representative higher magnification in (B). Differences in the number of OMP+ mature olfactory receptor neurons (ORNs) (C), SOX2+ ORN progenitors (D), Ki-67+ proliferating cells (E), GAP43+ immature ORNs (F), & cleaved Cas3+ apoptotic cells (G) in the OE were evaluated by immunohistological staining (brown). Tissue sections were counterstained with the nuclear dye hematoxylin (blue). Representative images (400× magnification) of tissues stained with antibodies against olfactory marker protein (OMP), SRY (sex determining region Y)-box 2 (SOX2), Ki-67 (antigen identified by monoclonal antibody Ki-67), growth associated protein 43 (GAP43), & cleaved caspase 3 (CAS3) are shown. The number of cells per mm of basal layer length (C–G) was counted manually. Data represent the mean ± SD. **P < 0.01 (n = 6, Mann–Whitney U-test). Image collected & cropped by CiteAb from the following publication (//journal.frontiersin.org/article/10.3389/fnagi.2018.00086/full), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-1252_rabbit-monoclonal-ki67-mki67-antibody-sp6-unpurified-310202416161841.jpg)
![Immunocytochemistry/Immunofluorescence: Ki67/MKI67 Antibody - BSA Free [NB110-89717] - 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- NB110-89717 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/Ki67-MKI67-Antibody---BSA-Free-Immunocytochemistry-Immunofluorescence-NB110-89717-img0023.jpg "Immunocytochemistry/Immunofluorescence: Ki67/MKI67 Antibody - BSA Free [NB110-89717] - 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- NB110-89717 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.")
![Immunohistochemistry: Ki67/MKI67 Antibody - BSA Free [NB110-89717] - KLF4 ablation leads to abnormal proliferation and differentiation in small intestinal epithelium. Higher magnification IHC staining of highlighted frames. Small intestine from Klf4-/- mice induced by tamoxifen for different time endurances were stained by H&E and PAS, and also immunohistochemistry staining was performed with anti-Ki67, anti-Lysozyme, anti-DCAMKL-1, and anti-PCNA antibodies respectively. Bottom panel: IHC staining with ZO-1 antibody in one-month knockout intestine tissue. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0032492) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/Ki67-MKI67-Antibody---BSA-Free-Immunohistochemistry-NB110-89717-img0020.jpg)
![Flow Cytometry: Ki67/MKI67 Antibody - BSA Free [NB110-89717] - An intracellular stain was performed on HeLa cells with Ki-67/MKI67 antibody NB110-89717PE (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 2.5 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to Phycoerythrin.](http://images.novusbio.com/fullsize/Ki67-MKI67-Antibody---BSA-Free-Flow-Cytometry-NB110-89717-img0017.jpg)
![Immunocytochemistry/Immunofluorescence: Ki67/MKI67 Antibody - BSA Free [NB110-89717] - Immunofluorescences against MyHC (red) and Ki67/MKI67 (green) revealing differences in proliferation and differentiation in relation to different PrP concentration. alpha-MEM supplemented with: Ctrl (20% FBS), Low (5 x 10^5 platelets/ml), Medium (1 x 10^6 platelets/ml), and High (1.5 x 10^6 platelets/ml); nuclei were counterstained in blue by DAPI. Scale bars: MyHC = 200 um; Ki67 = 100 um. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/33041857/) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/Ki67-MKI67 Antibody - BSA Free-Immunocytochemistry-Immunofluorescence-NB110-89717-img0024.jpg)
![Immunocytochemistry/Immunofluorescence: Ki67/MKI67 Antibody - BSA Free [NB110-89717] - 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 anti-Ki-67/MKI67 at 2 ug/ml overnight at 4C and detected with an anti-rabbit DyLight 488 (green) at a 1:500 dilution. Nuclei were counterstained with DAPI (blue). Cells were imaged using a 40X objective.](http://images.novusbio.com/fullsize/Ki67-MKI67-Antibody---BSA-Free-Immunocytochemistry-Immunofluorescence-NB110-89717-img0015.jpg)
![Immunocytochemistry/Immunofluorescence: Ki67/MKI67 Antibody - BSA Free [NB110-89717] - A431 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-Ki67/MKI67 Antibody NB110-89717 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/Ki67-MKI67-Antibody---BSA-Free-Immunocytochemistry-Immunofluorescence-NB110-89717-img0022.jpg)
![Immunohistochemistry-Paraffin: Ki67/MKI67 Antibody - BSA Free [NB110-89717] - Analysis of Ki-67 in paraffin embedded mouse prostate tissue using anti-Ki-67 antibody. Image from verified customer review.](http://images.novusbio.com/fullsize/Ki67-MKI67-Antibody---BSA-Free-Immunohistochemistry-Paraffin-NB110-89717-img0009.jpg)
![Immunohistochemistry: Ki67/MKI67 Antibody - BSA Free [NB110-89717] - Ki-67/MKI67 Antibody [NB110-89717] - Analysis of a mouse intestine cross section. The antibody was used at a dilution of 1:250. Detection: DAB staining. Epitope Retrieval Buffer-High pH was substituted for Epitope Retrieval Buffer-Reduced pH.](http://images.novusbio.com/fullsize/Ki67-MKI67-Antibody---BSA-Free-Immunohistochemistry-NB110-89717-img0010.jpg)
![Immunohistochemistry-Paraffin: Ki67/MKI67 Antibody - BSA Free [NB110-89717] - Staining of a cross section of mouse spleen. Detection: DAB staining using Immunohistochemistry Accessory Kit. Epitope Retrieval Buffer-High pH was substituted for Epitope Retrieval Buffer-Reduced pH.](http://images.novusbio.com/fullsize/Ki67-MKI67-Antibody---BSA-Free-Immunohistochemistry-Paraffin-NB110-89717-img0012.jpg)
![Immunohistochemistry: Ki67/MKI67 Antibody - BSA Free [NB110-89717] - Ki67 Antibody [NB110-89717] - FFPE section of mouse Peyer's patch. Antibody: Affinity purified rabbit anti-mouse Ki-67 used at a dilution of 1:250. Detection: DAB staining using Immunohistochemistry Accessory Kit. Epitope Retrieval Buffer-High pH was substituted for Epitope Retrieval Buffer-Reduced pH.](http://images.novusbio.com/fullsize/Ki67-MKI67-Antibody---BSA-Free-Immunohistochemistry-NB110-89717-img0014.jpg)
![Immunohistochemistry: Ki67/MKI67 Antibody - BSA Free [NB110-89717] - Ki-67/MKI67 Antibody [NB110-89717] - Detection of Ki67 in FFPE mouse intestine using NB110-89717.](http://images.novusbio.com/fullsize/Ki67-MKI67-Antibody---BSA-Free-Immunohistochemistry-NB110-89717-img0006.jpg)
![Immunohistochemistry-Paraffin: Ki67/MKI67 Antibody - BSA Free [NB110-89717] - Analysis of Ki-67 in human prostate xenograft control (left) and treated (right) using anti-Ki-67 antibody. Image from verified customer review.](http://images.novusbio.com/fullsize/Ki67-MKI67-Antibody---BSA-Free-Immunohistochemistry-Paraffin-NB110-89717-img0019.jpg)
![Flow Cytometry: Ki67/MKI67 Antibody - BSA Free [NB110-89717] - An intracellular stain was performed on U-937 cells with NB110-89717PE (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 Phycoerythrin.](http://images.novusbio.com/fullsize/Ki67-MKI67-Antibody---BSA-Free-Flow-Cytometry-NB110-89717-img0016.jpg)
![Flow Cytometry: Ki67/MKI67 Antibody - BSA Free [NB110-89717] - Ki-67/MKI67 Antibody [NB110-89717] - Staining of mouse bone marrow cells using NB110-89717 at a dilution of 1:100. Photo courtesy of product review by verified customer.](http://images.novusbio.com/fullsize/Ki67-MKI67-Antibody---BSA-Free-Flow-Cytometry-NB110-89717-img0004.jpg)
![<b>Genetic Strategies Validation. </b>Simple Western: Ki67/MKI67 Antibody - BSA Free [NB110-89717] - Detection of Ki67/MKI67 by Simple WesternTM. Simple Western lane view shows lysates of HeLa parental cell line and Ki67 knockout (KO) HeLa cell line. A specific band was detected for Ki67/MKI67 at approximately 312 kDa (as indicated) in the parental cell line, but is not detectable in the knockout HeLa cell line using 20 ug/mL of Rabbit Anti-Ki67/MKI67 Polyclonal Antibody (Catalog # NB110-89717). GAPDH is shown as a loading control. This experiment was conducted under reducing conditions and using the 12-230 kDa separation system.](http://images.novusbio.com/fullsize/Ki67-MKI67-Antibody---BSA-Free-Knockout-Validated-NB110-89717-img0021.jpg)
![Immunocytochemistry/ Immunofluorescence: Ki67/MKI67 Antibody - BSA Free [NB110-89717] - Long term Sonidegib treatment in mouse reduces taste buds (TB) & SHH ligand in circumvallate papilla (CV) whereas proliferation & innervation are retained. Immunofluorescent antibody detection of SHH ligand (red) & K8 (green) for TB cells; K8 (red) for TB cells & Ki67 (green) for cell proliferation; & K8 (red) with NF (green) for GL innervation or P2X3 (green) for GL taste fibers, after Vehicle or 48d Sonidegib treatment. For SHH/K8, large dotted lines indicate the basal lamina. Small dotted lines outline the surface epithelium. Inset (K8/P2X3) shows an image of nerves extending into CV epithelial basal lamina (arrow). Scale bar: 50 μm, applies to all images. Inset at 2×. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30385780), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-89717_rabbit-polyclonal-ki67-mki67-antibody-310202415175296.jpg)
![Immunohistochemistry: Ki67/MKI67 Antibody - BSA Free [NB110-89717] - KLF4 ablation leads to abnormal proliferation & differentiation in small intestinal epithelium.(A) Small intestine from Klf4−/− mice induced by tamoxifen for different time endurances were stained by H&E & PAS, & also immunohistochemistry staining was performed with anti-Ki67, anti-Lysozyme, anti-DCAMKL-1, & anti-PCNA antibodies respectively. (B) Statistic analysis of IHC staining results from (A). (*, P<0.05) (C) IHC staining from (A) in higher magnification of highlighted frames. Bottom panel: IHC staining with ZO-1 antibody in one-month knockout intestine tissue. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/22384261), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-89717_rabbit-polyclonal-ki67-mki67-antibody-310202415394542.jpg)
![Immunohistochemistry: Ki67/MKI67 Antibody - BSA Free [NB110-89717] - KLF4 ablation leads to abnormal proliferation & differentiation in small intestinal epithelium.(A) Small intestine from Klf4−/− mice induced by tamoxifen for different time endurances were stained by H&E & PAS, & also immunohistochemistry staining was performed with anti-Ki67, anti-Lysozyme, anti-DCAMKL-1, & anti-PCNA antibodies respectively. (B) Statistic analysis of IHC staining results from (A). (*, P<0.05) (C) IHC staining from (A) in higher magnification of highlighted frames. Bottom panel: IHC staining with ZO-1 antibody in one-month knockout intestine tissue. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/22384261), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-89717_rabbit-polyclonal-ki67-mki67-antibody-310202415175256.jpg)
![Immunocytochemistry/ Immunofluorescence: Ki67/MKI67 Antibody - BSA Free [NB110-89717] - Culture conditions influence cell behavior. Immunofluorescences against MyHC (red) & Ki67 (green) reveal the remarkable differences in terms of differentiation & proliferation employing Cyto-Grow commercial medium compared with alpha -MEM (nuclei labeled in blue by DAPI). The respective quantifications are reported as fusion index & rate of proliferating nuclei (Ki67 positive). Statistical analysis: one-way ANOVA & Tukey’s test. **p < 0.01, ***p < 0.001 (n = 3). Scale bars: MyHC = 200 μm; Ki67 = 100 μm. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/33041857), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-89717_rabbit-polyclonal-ki67-mki67-antibody-310202415284548.jpg)
![Immunocytochemistry/ Immunofluorescence: Ki67/MKI67 Antibody - BSA Free [NB110-89717] - Paclitaxel in combination with MWE retarded tumor growth in a human bladder carcinoma TSGH 8301 xenograft model.(a) TSGH 8301 cells (1 × 107 cells/mouse) were injected into the right inguinal region of a nude mouse to form tumor xenografts. When the tumor size reached approximately 250 to 300 mm3, the mice were randomly divided into 4 groups & received the following treatments: paclitaxel combined with MWE, MWE alone, paclitaxel alone & sterile deionized water (control group). Tumor size was monitored every week, & the results are expressed as the percentage of the size at week 0 (the day treatment started) for each group. (b) The levels of total (t-PTEN) & phospho-PTEN (p-PTEN) & Caspase 3 in the tumor specimens were determined by Western blotting & then quantified using beta -actin as the protein loading control; the results are expressed as a percentage of the control. (c) Immunohistochemical examination of p-PTEN in the tumor sections obtained from the indicated treatment. (d) & (e) Fluorescent immunohistochemical detection of Ki67 & TUNEL examination in the xenografts obtained from the indicated treatment. (f ) Western blotting analysis of the levels of Cyclin B1, Cdc2 & Aurora A in xenograft tumors. Arrow indicates the Ki67 or TUNEL positive cells. One-way ANOVA with post-hoc Dunnett’s test was used to calculate the p value for each treatment compared to paclitaxel alone, (+p < 0.05;++p < 0.01) at each time point (**indicates p < 0.01 & *indicates p < 0.05). Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/srep20417), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-89717_rabbit-polyclonal-ki67-mki67-antibody-31020241621846.jpg)
![Immunocytochemistry/ Immunofluorescence: Ki67/MKI67 Antibody - BSA Free [NB110-89717] - Sonidegib treatment reduces taste buds (TB), SHH ligand & proliferation in rat fungiform papilla (FP) while innervation is retained. (a) Immunofluorescent antibody detection of SHH ligand (red) & K19 (green) for TB cells; K18 (red) for TB cells & Ki67 (green) for cell proliferation, after Vehicle, 16d or 28d Sonidegib treatments. SHH is reduced in association with TB, K19+ cell loss. Asterisks (*) indicate nonspecific SHH immunoproduct in cornified surface cells in 16d Sonidegib image. The Vehicle, K18/Ki67 image shows 3 regions positive for Ki67+ cells (Apical, Basal & Perigemmal). Proliferating cells are lost in Apical FP region after 16–28d Sonidegib. (b) Number of Ki67+ cells in Apical & Basal regions of FP in Vehicle- & Sonidegib-treated mice. Numbers of tongues analyzed are in parentheses. For each tongue 8–10 FP were analyzed. Sonidegib treatment reduces apical epithelial cell proliferation in FP compared to Vehicle. Statistical analysis was one-way ANOVA with Tukey HSD posthoc comparisons (*p ≤ 0.05, compared to Vehicle, APICAL). (c) Immunofluorescent antibody detection of K19 or K18 (red) for TB cells & NF (green) for lingual & CT innervation or P2X3 (green) for CT nerve fibers. Innervation was retained after Sonidegib exposure. Asterisks (*) indicate nonspecific P2X3 immunoproduct in surface layer in Vehicle image. (d) Enlarged images from 28d Sonidegib papillae. Arrows point to NF+ or P2X3+ fibers in the FP epithelium. Throughout, white dotted lines indicate the basal lamina. Yellow dotted lines indicate surface of epithelium. (a,c) Scale bar: 50 μm, applies to all images. (d) Scale bar: 25 μm, applies to both images. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30385780), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-89717_rabbit-polyclonal-ki67-mki67-antibody-310202416205161.jpg)
![Immunocytochemistry/ Immunofluorescence: Ki67/MKI67 Antibody - BSA Free [NB110-89717] - SPIN1 controls proliferation & apoptosis of liposarcoma cell-derived tumors in BALB/c nude mice(A) Analysis of tumors from BALB/c nude mice (n = 15) 10 days after subcutaneous injection of T778 cells expressing control miRNA (miCtrl) or miRNA against SPIN1 [miSPIN1(1)]. Scale bar = 5 mm. (B) Average tumor weight of mice shown in (A) (C) Quantitative RT-PCR analysis of SPIN1, GDNF, & RET expression in T778 cell-derived tumors treated with the indicated miRNA. (D) Western blot analysis of SPIN1, RET, & RETph levels in T778 cell-derived tumors treated with the indicated miRNA. alpha -Tubulin & GFP were used as loading controls. (E) Detection of Ki67 by immunofluorescence in T778 cell-derived tumors treated with the indicated miRNA. Scale bar = 100 μm. (F) Quantification of Ki67 staining shown in (E). (G) TUNEL assay for detection of apoptotic cells in T778 cell-derived tumors treated with the indicated miRNA. Scale bar = 100 μm. (H) Quantification of TUNEL staining shown in (G) (B, C, F, H) Error bars represent +/– SEM, *p < 0.05, **p < 0.01. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/25749382), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-89717_rabbit-polyclonal-ki67-mki67-antibody-31020241620513.jpg)
![Immunocytochemistry/ Immunofluorescence: Ki67/MKI67 Antibody - BSA Free [NB110-89717] - Sonidegib treatment in rat reduces taste buds (TB) & SHH ligand in circumvallate papilla (CV) whereas cell proliferation & GL innervation are retained. Immunofluorescent antibody detection of SHH ligand (red) & K19 (green) for TB cells; K18 (red) for TB cells & Ki67 (green) for cell proliferation; K19 (red) for TB cells & NF (green) for innervation; and, K18 (red) for TB cells & P2X3 (green) for taste nerve fibers, after Vehicle or 36d Sonidegib treatment. White dotted lines outline the epithelium. Asterisk in SHH/K19, 36d Sonidegib indicates nonspecific K19 immunostaining. Arrow points to the P2X3+ nerves extending into CV epithelium after Sonidegib treatment. SHH is reduced in association with TB cells. Cell proliferation is maintained & nerves fibers are retained after Sonidegib treatment. Scale bar: 50μm, applies to all images, except K19/NF. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30385780), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-89717_rabbit-polyclonal-ki67-mki67-antibody-31020241621233.jpg)
![Immunocytochemistry/ Immunofluorescence: Ki67/MKI67 Antibody - BSA Free [NB110-89717] - Overexpression of Chibby expression inhibits cell proliferation & invasion of HCC cells. (A) Adenovirus-mediated ectopic expression of Chibby & enhanced the expression of Chibby in Huh7 cells. After 48 h of infection with adenoviral vectors (Ad-GFP or Ad-Chibby) at different multiplicity of infection, the protein lysates from the Huh7 cells were harvested to determine the ectopic gene expression using Western blot analysis. Ad-GFP was designed as the control vector. (B) Representative immunofluorescent images of Ki67 in Huh7-normal control, Huh7-Ad-GFP, & Huh7-Ad-Chibby cells. (C,D) The enhancement of Chibby in Huh7 cells transfected with Ad-Chibby suppressed cell proliferation & invasiveness by colon-formation assay & the Boyden chamber system, respectively. Data represent mean ± SE from three independent analyses. Scale bar, 100 μm, * p < 0.05 & ** p < 0.01 vs. Ad-GFP group. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32192213), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-89717_rabbit-polyclonal-ki67-mki67-antibody-310202416212380.jpg)
![Immunocytochemistry/ Immunofluorescence: Ki67/MKI67 Antibody - BSA Free [NB110-89717] - High doses of metformin inhibit the proliferation of C2C12 cells without inducing apoptosis.(a) C2C12 cells were treated with different doses of metformin in growth medium (GM) & the total number of cells was counted after 1, 2, 3 & 4 days of treatment by immunofluorescence microsopy. The initial number of plated cells was the same in each growth condition. Statistical significance was evaluated by the Student’s t-test (*p<0.05) (b) TUNEL assay. C2C12 cells were treated with 100μM, 2mM & 10mM metformin for 48h. As positive control for the TUNEL assay C2C12 myoblasts were incubated with DNΑse I before staining and, as negative control, cells were stained with the label solution without the addition of the reaction enzyme terminal deoxynucleotidyl transferase (TdT). (c) Total protein extracts of C2C12 myoblasts treated with 100μM, 2mM & 10mM were analyzed by SDS-PAGE for the expression of the apoptotic markers cl-caspase 3 & cl-caspase 7. For the induction of apoptosis in the positive control was used staurosporine 1μM for 4 hours. GAPDH is used as loading control (d) Proliferating C2C12 myoblasts, were plated at the same initial number (4*104 in GM in 9,5 cm2 area wells), incubated with 100μM, 2mM & 10mM metformin for 48h. The percentage of cells expressing Ki67 was measured by Cell Profiler cell image analysis software. Statistical significance was evaluated by the Student’s t-test (*p<0.05). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28859084), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-89717_rabbit-polyclonal-ki67-mki67-antibody-310202416212356.jpg)
![Immunocytochemistry/Immunofluorescence: SCP3/SYCP3 Antibody [NB300-232] - Chromosome spread for sycp3. ICC/IF image submitted by a verified customer review.](http://images.novusbio.com/fullsize/SCP3-SYCP3-Antibody-Immunocytochemistry-Immunofluorescence-NB300-232-img0013.jpg "Immunocytochemistry/Immunofluorescence: SCP3/SYCP3 Antibody [NB300-232] - Chromosome spread for sycp3. ICC/IF image submitted by a verified customer review.")
![Immunohistochemistry-Paraffin: SCP3/SYCP3 Antibody [NB300-232] - IHC analysis of a formalin fixed and paraffin embedded tissue section of Mouse testis using SCP3 antibody at 1:1000 dilution. The signal was detected using HRP-DAB detection method and the nuclei were counterstained with hematoxylin. The antibody generated a specific signal of SCP3 in the spermatogonial cells and the spermatocytes. The signal was strongest in the nuclei of spermatogonial cells.](http://images.novusbio.com/fullsize/SCP3-SYCP3-Antibody-Immunohistochemistry-Paraffin-NB300-232-img0011.jpg)
![Immunocytochemistry/Immunofluorescence: SCP3/SYCP3 Antibody [NB300-232] - Exposure to DEHP impairs meiotic progression of oocytes from pachytene to diplotene. Immunolabeling of the oocyte chromosomes with anti-SYCP3 antibody (red) and Hoechst 33342 (blue). All experiments were repeated at least three times independently. (* P600 spermatocytes in each stage. b, c The immunostaining of SYCP3 in the testicular sections (b) & surface-spread chromatin preparations of Uhrf1 deletion & control mice (c); d the percentage of spermatocytes with abnormal SYCP3 location. e Double immunofluorescence of testicular spread preparations of the adult mice, SYCP3 (green) & SYCP1 (red). f The percentage of spermatocytes with abnormal SYCP1 location. Lep leptotene, Zyg zygotene, Pac pachytene, Dip diplotene. Data are presented as mean ± SEM of three mice. ***p ≤ 0.001. Scale bar, 25 μm in b, 5 μm in c, e. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32081844), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-232_rabbit-polyclonal-scp3-sycp3-antibody-31020241621832.jpg)
![Immunocytochemistry/ Immunofluorescence: SCP3/SYCP3 Antibody - BSA Free [NB300-232] - Dynamic expression of germ cell markers in human fetal ovaries. (A) Histological sections of human ovaries at W10.5, W14, W17 & W21.5, immunostained for the early germ cell marker (nuclear) POU5F1 (red) & late germ cell marker (cytoplasmic) DDX4 (green). In zone 1, most germ cells are POU5F1+DDX4−/low; in zone 2 & 3, most germ cells are DDX4+. Several germ cells in zone 3 have developed into primordial follicles. Inserts are magnifications of the dotted boxes. (B) Histological sections of human ovaries at W10.5, W14, W17 & W21.5, immunostained for the meiotic markers H2AFX (red) & SYCP3 (green). Inserts are magnifications of the dotted boxes. Note the presence of autofluorescent red blood cells. Scale bars are 200 µm & in the magnified inserts 20 µm. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26834021), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-232_rabbit-polyclonal-scp3-sycp3-antibody-31020241620376.jpg)
![Immunocytochemistry/ Immunofluorescence: SCP3/SYCP3 Antibody - BSA Free [NB300-232] - CYP51 regulates the expression of the meiosis-specific cohesin subunits REC8 & STAG3. (A,B) RS21745 treatment decreased REC8 & STAG3 expression. Ovaries at 14.5 dpc were cultured with 10 μM RS21745 for 3 days in vitro. (A) Expression of the cohesin subunits following RS21745 treatment by qRT-PCR. All qRT-PCR values were normalized to beta -actin & were expressed as a relative ratio to the control; the means±s.e.m. of 3 values are shown. (B) Expression of REC8 & STAG3 following RS21745 treatment by western blotting GAPDH was used as internal reference. (C–F) Inhibition of CYP51 disturbed the distribution of both REC8 & STAG3 on the chromosomes. (C,E) In the control groups, REC8 & STAG3 expression was observed at high levels in zygotene oocytes. In the CYP51 inhibition groups, the cohesin signals were absent in zygotene cells. (D,F) The percentage of REC8-positive or STAG3-positive oocytes at the zygotene stage was recorded. Unidentified germ cells were not included in the analyses. Scale bars: 10 μm. The data are presented as the means±s.e.m. of 3–9 ovaries per group. Asterisk (*) denotes a statistically significant difference between the control & the treatment groups. ***P<0.001 (t-test). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30420384), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-232_rabbit-polyclonal-scp3-sycp3-antibody-310202416212332.jpg)
![Immunocytochemistry/ Immunofluorescence: SCP3/SYCP3 Antibody - BSA Free [NB300-232] - Induction of meiosis is compromised in the cortical germ cells of D17 embryos subject to oestrogen level alterations. (A) D17 (HH43) left gonad sections immunostained for gamma H2AX (green) & P63 (red); nuclei are counterstained with DAPI (blue). (B) Sections from the D17 (HH43) left gonad shown in A immunostained for gamma H2AX (green) & SYCP3 (red). ZW-WT, ZW wild type; ZW-Fa, ZW treated with fadrozole from D7-7.5 (HH31); ZW-E2, ZW treated with beta -oestradiol at D7-7.5; ZZ-E2, ZZ treated with beta -oestradiol at D7-7.5; ZW-Fa(sr), ZW, partially sex-reversed gonad, treated with fadrozole at D4; ZZ-E2(sr), ZZ, partially sex-reversed gonad, treated with beta -oestradiol at D4. All gonadal models have a cortical domain containing germ cells. In ZW-Fa ovary & ZW-E2 ovary, most cortical germ cells express SYCP3 like the ZW-WT control. In ZW-Fa(sr) ovotestis, very few germ cells express gamma H2AX & SYCP3 (orange dotted circled areas). In ZZ-E2(sr) ovotestis & ZZ-E2 testis overlain by a cortex, some cortical germ cells express gamma H2AX but none expresses SYCP3. White dotted line highlights the cortical domain borders. See Fig. S4 for the medullary structure of the ZZ-E2, ZW-Fa(sr) & ZZ-E2(sr) models. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32001442), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-232_rabbit-polyclonal-scp3-sycp3-antibody-310202416212348.jpg)
![Immunocytochemistry/ Immunofluorescence: SCP3/SYCP3 Antibody - BSA Free [NB300-232] - Exposure to DEHP impairs meiotic progression of oocytes from pachytene to diplotene. (a) Immunolabeling of the oocyte chromosomes with anti-SYCP3 antibody (red) & Hoechst 33342 (blue). (b) Effect of DEHP on meiotic progression of oocytes throughout prophase I stages; percentage of each group is presented as mean±SD. Control: 36.27±0.80% pachytene & 54.99±0.66% diplotene; 10 μM & 100 μM DEHP 57.79±4.22% & 56.62±6.62% pachytene & 39.79±4.22% & 36.62±6.62% diplotene, respectively. (c) Representative WB showing the effect of DEHP on the expression of germ cell (DAZL) & meiotic (STRA8 & SCP3) specific proteins. (d) Effect of DEHP on the levels of mRNA in the ovarian tissues of germ cell (Mvh & Dazl), meiotic (Stra8, Rec8, Scp1 & Scp3). All experiments were repeated at least three times independently. (* P<0.05; ** P<0.01) Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28771232), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-232_rabbit-polyclonal-scp3-sycp3-antibody-310202416212391.jpg)
![Immunocytochemistry/ Immunofluorescence: SCP3/SYCP3 Antibody - BSA Free [NB300-232] - Loss of lamin C2 has no effect on meiotic telomere attachment.(A) 3D-preserved swab preparations showing wildtype (A) & knockout (A′) spermatocytes simultaneously labelled with anti-TRF1 & SUN1 antibodies. As in the wildtype, in lamin C2−/− spermatocytes virtual all telomeres appear to be attached to the NE as indicated by co-localisation of TRF1 & SUN1 signals. Scale bars 5 µm. (B) Quantifications of co-localised & non-co-localised TRF1/SUN1 signals (see A) revealed that ratios of co-localised to non-co-localised spots comparing wildtype & knockout spermatocytes show no significant difference (wildtype n = 33; lamin C2−/− n = 45; Pearson's Chi2 test p-value: 0.799). (C,D) Chromosome spread preparations of pachytene-like lamin C2−/− spermatocytes showing that all telomeres are associated with SUN1. In (C) TeloFISH & in (D) anti-SUN1 staining in co-localisation with SYCP3. Scale bars 10 µm. Image collected & cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pgen.1003261), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-232_rabbit-polyclonal-scp3-sycp3-antibody-310202416212363.jpg)
![Immunohistochemistry: SCP3/SYCP3 Antibody - BSA Free [NB300-232] - FANCM expression in human fetal ovaries.(A) Relative FANCM mRNA abundance was measured by RT-qPCR in human fetal ovaries from 5 to 32 weeks post-fertilization (wpf). (B) Germ cells (D2-40+) & somatic cells (D2-40-) were sorted from three ovaries ranging from 8 to 12 wpf & FANCM expression was measured. ACTB was used to normalize FANCM expression in all samples. Dots represent different ovaries & the mean is indicated by the line. (C) Immunohistochemistry of FANCM in human fetal & adult ovaries. Fetal ovaries at 8 & 22 wpf & adult ovaries were studied. FANCM positive cells appear in yellow/brown color (monoclonal FANCM CV5.1 antibody, Novus Biologicals, Abingdon, UK). Ovarian sections were counterstained with hematoxylin (blue staining). Oo, oogonia; Pa, oocyte at the pachytene stage of meiosis I, D, oocyte at the diplotene stage of meiosis I; Pr, oocyte in primordial follicle. (D) Co-staining in 22 wpf ovaries, for FANCM (purple) & DDX4 (brown) confirmed the germ cell identity of FANCM-positive cells (left). Successive staining for FANCM & SYCP3 in the same section (panels a & b). Negative control performed with non-immune mouse IgG (right). Scale bar: 10 μm. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29231814), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-232_rabbit-polyclonal-scp3-sycp3-antibody-3102024162184.jpg)
![Immunocytochemistry/ Immunofluorescence: SCP3/SYCP3 Antibody - BSA Free [NB300-232] - Loss of lamin C2 has no effect on meiotic telomere attachment.(A) 3D-preserved swab preparations showing wildtype (A) & knockout (A′) spermatocytes simultaneously labelled with anti-TRF1 & SUN1 antibodies. As in the wildtype, in lamin C2−/− spermatocytes virtual all telomeres appear to be attached to the NE as indicated by co-localisation of TRF1 & SUN1 signals. Scale bars 5 µm. (B) Quantifications of co-localised & non-co-localised TRF1/SUN1 signals (see A) revealed that ratios of co-localised to non-co-localised spots comparing wildtype & knockout spermatocytes show no significant difference (wildtype n = 33; lamin C2−/− n = 45; Pearson's Chi2 test p-value: 0.799). (C,D) Chromosome spread preparations of pachytene-like lamin C2−/− spermatocytes showing that all telomeres are associated with SUN1. In (C) TeloFISH & in (D) anti-SUN1 staining in co-localisation with SYCP3. Scale bars 10 µm. Image collected & cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pgen.1003261), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-232_rabbit-polyclonal-scp3-sycp3-antibody-310202416212314.jpg)
![Simple Western: SCP1 Antibody [NB300-229] - Simple Western lane view shows a specific band for SCP1 in 0.5 mg/ml of Human Testis (left) and Mouse Testis (right) lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system.](http://images.novusbio.com/fullsize/SCP1-Antibody-Simple-Western-NB300-229-img0010.jpg "Simple Western: SCP1 Antibody [NB300-229] - Simple Western lane view shows a specific band for SCP1 in 0.5 mg/ml of Human Testis (left) and Mouse Testis (right) lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system.")
![Western Blot: SCP1 Antibody [NB300-229] - Meiotic chromosome spreads from wild type and Fance mutant (MT) primary spermatocytes isolated from the testes at 20 dpp. Each chromatin spread was staged by analyzing SYCP3 (red) and SYCP1 (green), which are axial element and central region components of the synaptonemal complex respectively. Most of the Fance mutant spermatocytes displayed normal synapsis (middle panels); however a sub-set displayed synapsis abnormalities including an association between non-homologous chromosome ends (arrow head) and abnormal SYCP3 structures (arrows). Dearth and Delayed Maturation of Testicular Germ Cells in Fanconi Anemia E Mutant Male Mice. PLoS One (2016)](http://images.novusbio.com/fullsize/SCP1-Antibody-Western-Blot-NB300-229-img0014.jpg)
![Immunocytochemistry/Immunofluorescence: SCP1 Antibody - BSA Free [NB300-229] - Double immunofluorescence of testicular spread preparations of the adult mice, SYCP3 (green) and SCP1 (red). Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32081844/) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/SCP1-Antibody---BSA-Free-Immunocytochemistry-Immunofluorescence-NB300-229-img0017.jpg)
![Immunohistochemistry-Paraffin: SCP1 Antibody [NB300-229] - Punctate staining of murine SCP1 in mouse ovary using NB300-229.](http://images.novusbio.com/fullsize/SCP1-Antibody-Immunohistochemistry-Paraffin-NB300-229-img0008.jpg)
![Immunocytochemistry/Immunofluorescence: SCP1 Antibody [NB300-229] - SCP1 labeled in mouse pachytene preparation (red), using NB300-229. CDK2 staining, near teleomeres, is also present (green).](http://images.novusbio.com/fullsize/SCP1-Antibody-Immunocytochemistry-Immunofluorescence-NB300-229-img0007.jpg)
![Immunocytochemistry/Immunofluorescence: SCP1 Antibody [NB300-229] - Spermatocytes cells fixed in PFA. Detected with anti-mouse 594. ICC/IF image submitted by a verified customer review.](http://images.novusbio.com/fullsize/SCP1-Antibody-Immunocytochemistry-Immunofluorescence-NB300-229-img0012.jpg)
![Immunocytochemistry/Immunofluorescence: SCP1 Antibody [NB300-229] - Mouse spermatozoa. Green: SCP1 staining. ICC/IF image submitted by a verified customer review.](http://images.novusbio.com/fullsize/SCP1-Antibody-Immunocytochemistry-Immunofluorescence-NB300-229-img0013.jpg)
![Immunocytochemistry/Immunofluorescence: SCP1 Antibody [NB300-229] - Mouse spermatocyte. Red: scp1 colocalized with scp3 (green). ICC/IF image submitted by a verified customer review.](http://images.novusbio.com/fullsize/SCP1-Antibody-Immunocytochemistry-Immunofluorescence-NB300-229-img0015.jpg)
![Immunocytochemistry/Immunofluorescence: SCP1 Antibody - BSA Free [NB300-229] - Immunostaining of SCP3/SYCP3 (NB300-231) and SCP1 on adult Cxxc1 het and CKO chromosome spreads. Green, SCP3/SYCP3; orange, SCP1. Scale bar, 10 um. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30365547/) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/SCP1-Antibody---BSA-Free-Immunocytochemistry-Immunofluorescence-NB300-229-img0016.jpg)
![Chromatin Immunoprecipitation: SCP1 Antibody - BSA Free [NB300-229] - Meiotic spreads.Meiotic chromosome spreads from wild type & Fance mutant (MT) primary spermatocytes isolated from the testes at 20 dpp. Each chromatin spread was staged by analyzing SYCP3 (red) & SYCP1 (green), which are axial element & central region components of the synaptonemal complex respectively. Most of the Fance mutant spermatocytes displayed normal synapsis (middle panels); however a sub-set displayed synapsis abnormalities including an association between non-homologous chromosome ends (arrow head) & abnormal SYCP3 structures (arrows). Image collected & cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0159800), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-229_rabbit-polyclonal-scp1-antibody-310202415345326.jpg)
![Immunocytochemistry/ Immunofluorescence: SCP1 Antibody - BSA Free [NB300-229] - Meiotic progression & chromosome paring in XX, XO & XY oocytes.(A) Meiotic progression in XX, XO & XY oocytes. The graphs show the percentages of the meiotic stage at the day of culture indicated. L, leptotene; Z, zygotene; P, pachytene; D, diplotene. (B) Pairing of homologous chromosomes in XX, XO & XY oocytes. Images show the immunofluorescence analysis of SYCP3 (white) & SYCP1 (red), & FISH analysis of the X chromosome (green) & Y chromosome (purple). The dashed squares in the merged images are shown at high magnification (right). The numbers of samples showing the phenotype are shown with the total number tested (left). Arrowheads indicate asynapsed bivalents at the end of the chromosomes. Scale bars, 10 μm. (C) Pairing rates of autosomes & sex chromosomes. Each value was calculated from three independent experiments (see also Materials & Methods). P values were calculated by Tukey’s HSD test. ***P600 spermatocytes in each stage. b, c The immunostaining of SYCP3 in the testicular sections (b) & surface-spread chromatin preparations of Uhrf1 deletion & control mice (c); d the percentage of spermatocytes with abnormal SYCP3 location. e Double immunofluorescence of testicular spread preparations of the adult mice, SYCP3 (green) & SYCP1 (red). f The percentage of spermatocytes with abnormal SYCP1 location. Lep leptotene, Zyg zygotene, Pac pachytene, Dip diplotene. Data are presented as mean ± SEM of three mice. ***p ≤ 0.001. Scale bar, 25 μm in b, 5 μm in c, e. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32081844), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-229_rabbit-polyclonal-scp1-antibody-310202416212369.jpg)
![Western Blot: GADD153/CHOP Antibody (9C8) [NB600-1335] - Ethanol feeding increases CHOP expression. Image from verified customer review.](http://images.novusbio.com/fullsize/GADD153-CHOP-Antibody-9C8-Western-Blot-NB600-1335-img0011.jpg "Western Blot: GADD153/CHOP Antibody (9C8) [NB600-1335] - Ethanol feeding increases CHOP expression. Image from verified customer review.")
![Immunohistochemistry-Paraffin: GADD153/CHOP Antibody (9C8) [NB600-1335] - FFPE tissue section of mouse brain using 1:100 dilution of GADD153/CHOP antibody. The signal was developed using HRP-DAB based detection method which followed counterstaining of the nuclei with hematoxylin. The antibody generated a cytoplasmic and nuclear staining of CHOP in various cell types in the tested section.](http://images.novusbio.com/fullsize/GADD153-CHOP-Antibody-9C8-Immunohistochemistry-Paraffin-NB600-1335-img0010.jpg)
![Flow Cytometry: GADD153/CHOP Antibody (9C8) [NB600-1335] - An intracellular stain was performed on SK-MEL-28 cells with GADD153/CHOP Antibody (9C8) NB600-1335 (blue) and a matched isotype control MAB004 (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, followed by Mouse IgG (H+L) Cross-Adsorbed Secondary Antibody, Dylight 550 (84540, Thermo Fisher).](http://images.novusbio.com/fullsize/GADD153-CHOP-Antibody-9C8-Flow-Cytometry-NB600-1335-img0012.jpg)
![<b>Biological Strategies Validation. </b>Western Blot: GADD153/CHOP Antibody (9C8) [NB600-1335] - GADD153/CHOP expression in HeLa cells treated with 2.5 ug/mL tunicamycin for 4 hours (Lane 1) and untreated (Lane 2).](http://images.novusbio.com/fullsize/GADD153-CHOP-Antibody-9C8-Western-Blot-NB600-1335-img0001.jpg)
![<b>Biological Strategies Validation. </b>Western Blot: GADD153/CHOP Antibody (9C8) [NB600-1335] - Analysis of endogenous CHOP/GADD153 from primary human fibroblasts using NB600-1335. Lane 1: Untreated cells, Lane 2: Cells treated with tunicamycin for 10 hours.](http://images.novusbio.com/fullsize/GADD153-CHOP-Antibody-9C8-Western-Blot-NB600-1335-img0004.jpg)
![Western Blot: GADD153/CHOP Antibody (9C8) [NB600-1335] - Analysis of CHOP in rat heart tissue lysate. Image courtesy of product review submitted by Lee Hsiao-Wei.](http://images.novusbio.com/fullsize/GADD153-CHOP-Antibody-9C8-Western-Blot-NB600-1335-img0005.jpg)
![Immunohistochemistry-Paraffin: GADD153/CHOP Antibody (9C8) [NB600-1335] - FFPE tissue section of mouse brain using 1:100 dilution of GADD153/CHOP antibody. The signal was developed using HRP-DAB based detection method which followed counterstaining of the nuclei with hematoxylin. The antibody generated a cytoplasmic and nuclear staining of CHOP in various cell types in the tested section.](http://images.novusbio.com/fullsize/GADD153-CHOP-Antibody-9C8-Immunohistochemistry-Paraffin-NB600-1335-img0008.jpg)
![Simple Western: GADD153/CHOP Antibody (9C8) [NB600-1335] - Image shows a specific band for CHOP/GADD153 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/GADD153-CHOP-Antibody-9C8-Simple-Western-NB600-1335-img0007.jpg)
