| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB100-106SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB100-116SS | |||
| Azide and BSA Free | NBP2-80578 | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB100-101SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| Azide and BSA Free | NBP2-80905 | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB100-109SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB100-108SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| Azide and BSA Free | NBP2-27335 | |||
| BSA Free | NB100-56599SS | |||
| Azide and BSA Free | NBP2-27335SS | |||
![Immunohistochemistry-Paraffin: OGG1 Antibody [NB100-106] - Analysis of OGG1 in human skin tissues. Image courtesy of product review by Arash Javeri.](http://images.novusbio.com/fullsize/OGG1-Antibody-Immunohistochemistry-Paraffin-NB100-106-img0023.jpg "Immunohistochemistry-Paraffin: OGG1 Antibody [NB100-106] - Analysis of OGG1 in human skin tissues. Image courtesy of product review by Arash Javeri.")
![Western Blot: OGG1 Antibody [NB100-106] - - Analysis of Ogg1 expression in Jurkat whole cell lysate.](http://images.novusbio.com/fullsize/OGG1-Antibody-Western-Blot-NB100-106-img0024.jpg)
![Immunohistochemistry: OGG1 Antibody [NB100-106] - Figure 5 IHC-P analysis of hOGG1 protein expression in serous ovarian cancer: (A) Normal ovarian tissue treated with anti-hOGG1 antibody, biotinylated anti-rabbit IgG secondary antibody, and avidin-biotin-peroxidase complex, and counterstained with p-dimethylaminobenzaldehyde reagent (magnification 100 x); (B) serous cystadenoma with positive staining (magnification 200 x); (C) LG-SOC tissue with moderate positive staining (magnification 200 x); and (D) HG-SOC with negative staining (magnification 200 x). Black arrow pointed at the immunostained epithelial cells. Image collected and cropped by CiteAb from the following publication (//ovarianresearch.biomedcentral.com/articles/10.1186/1757-2215-6-74), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/OGG1-Antibody-Immunohistochemistry-NB100-106-img0032.jpg)
![Immunocytochemistry/Immunofluorescence: OGG1 Antibody [NB100-106] - A431 cells were fixed for 10 minutes using 10% formalin and then permeabilized for 5 minutes using 1X TBS + 0.5% Triton-X100. The cells were incubated with anti-hOgg1 [NB100-106] at a 1:200 dilution overnight at 4C and detected with an anti-rabbit Dylight 488 (Green) at a 1:500 dilution. Alpha Tubulin (DM1A) [NB100-690] was used as a co-stain at a 1:1000 dilution and detected with an anti-mouse Dylight 550 (Red) at a 1:500 dilution. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 40X objective.](http://images.novusbio.com/fullsize/OGG1-Antibody-Immunocytochemistry-Immunofluorescence-NB100-106-img0020.jpg)
![Immunohistochemistry-Frozen: OGG1 Antibody [NB100-106] - Detection of OGG1 in formaldehyde-fixed frozen sections of the substantia nigra from a Rhesus macaque (Macaca mulatta) using NB100-106 at 10 ug/mL. Photo courtesy of Glen Kisby, Oregon Health Sciences University.](http://images.novusbio.com/fullsize/OGG1-Antibody-Immunohistochemistry-Frozen-NB100-106-img0021.jpg)
![Flow (Intracellular): OGG1 Antibody [NB100-106] - An intracellular stain was performed on HeLa cells with NB100-106C (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 2.5 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to Dylight 650.](http://images.novusbio.com/fullsize/OGG1-Antibody-Flow-Intracellular-NB100-106-img0028.jpg)
![Immunohistochemistry: OGG1 Antibody [NB100-106] - The H&E staining ((a)-(c)) and IHC staining for oxidative DNA damage, 8-oxo-dGuo ((d)-(g)), and DNA repair enzyme hOGG1 ((h)-(j)) in control subjects and tumor and nontumor lesions of BCC patients. Values given are mean +/- SD. The statistical significance of differences between the control and case and between adjacent epidermis and tumor lesions of BCC patients was evaluated by nonparametric variables with Kruskal-Wallis test followed by Dunnett's post hoc test. * P < 0.05, *P < 0.01, *P < 0.001 compared to control; ##P < 0.01, ###P < 0.001 compared to tumor lesions of BCC patients. Image collected and cropped by CiteAb from the following publication (//www.hindawi.com/journals/omcl/2016/5934024/), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/OGG1-Antibody-Immunohistochemistry-NB100-106-img0033.jpg)
![Western Blot: OGG1 Antibody [NB100-106] - The protein expression levels of HVL and LVL sorted cells by western blotting. The ATM, phospho-ATM, GPX2, MRE11, OGG1, and XPC levels were measured by western blot analysis. The figure is representative of three independent experiments. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0164281), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/OGG1-Antibody-Western-Blot-NB100-106-img0034.jpg)
![Immunohistochemistry-Paraffin: OGG1 Antibody [NB100-106] - Comparison of the expression of OGG1 protein in normal colon tissue, polyp and cancer tissue of adenoma (AD, n = 68) and carcinoma (CRC, n = 103) patients. Immunohistochemical detection in paraffin embedded sections stained with hematoxylin and eosin. Center mark in the box indicates the medians of the samples. The length of each box (IQR, interquartile range) represents the range within which the central 50% of the values fell, with the vertical edges placed at the first and third quartiles. Whiskers show variability outside the upper and lower quartiles. P was obtained with the Mann-Whitney test. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0115558), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/OGG1-Antibody-Immunohistochemistry-Paraffin-NB100-106-img0035.jpg)
![Flow Cytometry: OGG1 Antibody [NB100-106] - An intracellular stain was performed on HeLa cells with OGG1 Antibody NB100-106 (blue) and a matched isotype control NBP2-24891 (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 1.0 ug/mL for 30 minutes at room temperature, followed by Rabbit IgG (H+L) Cross-Adsorbed Secondary Antibody, Dylight 550 (SA5-10033, Thermo Fisher).](http://images.novusbio.com/fullsize/OGG1-Antibody-Flow-Cytometry-NB100-106-img0036.jpg)
![Immunohistochemistry: OGG1 Antibody [NB100-106] - Staining of human tonsil, germinal center and mantle zone.](http://images.novusbio.com/fullsize/OGG1-Antibody-Immunohistochemistry-NB100-106-img0022.jpg)
![Flow Cytometry: OGG1 Antibody [NB100-106] - Baseline Ogg1 expression in human PBMC from a healthy donor. Image from verified.customer review.](http://images.novusbio.com/fullsize/OGG1-Antibody-Flow-Cytometry-NB100-106-img0026.jpg)
![Flow Cytometry: OGG1 Antibody [NB100-106] - An intracellular stain was performed on Jurkat Cells with NB100-106 and a matched isotype control. Cells were fixed with 4% PFA and then permeablized with 0.1% saponin. Cells were incubated in an antibody dilution of 2.5 ug/mL for 30 minutes at room temperature, followed by Rabbit IgG (H+L) Cross-Adsorbed Secondary Antibody, Dylight 550.](http://images.novusbio.com/fullsize/OGG1-Antibody-Flow-Cytometry-NB100-106-img0029.jpg)
![Western Blot: OGG1 Antibody - BSA Free [NB100-106] - The protein expression levels of HVL & LVL sorted cells by western blotting.(A) The ATM, phospho-ATM, GPX2, MRE11, OGG1, & XPC levels were measured by western blot analysis. The figure is representative of three independent experiments. (B) The relative fold activity was quantified using AlphaImage software & normalized to the expression of the internal actin control. *P < 0.05, **P < 0.01. Image collected & cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0164281), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-106_rabbit-polyclonal-ogg1-antibody-310202415345339.jpg)
![Immunohistochemistry: OGG1 Antibody - BSA Free [NB100-106] - IHC-P analysis of hOGG1 protein expression in serous ovarian cancer: (A) Normal ovarian tissue treated with anti-hOGG1 antibody, biotinylated anti-rabbit IgG secondary antibody, & avidin-biotin-peroxidase complex, & counterstained with p-dimethylaminobenzaldehyde reagent (magnification 100 x); (B) serous cystadenoma with positive staining (magnification 200 x); (C) LG-SOC tissue with moderate positive staining (magnification 200 x); & (D) HG-SOC with negative staining (magnification 200 x). Black arrow pointed at the immunostained epithelial cells. Image collected & cropped by CiteAb from the following publication (//ovarianresearch.biomedcentral.com/articles/10.1186/1757-2215-6-74), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-106_rabbit-polyclonal-ogg1-antibody-310202415291933.jpg)
![Immunohistochemistry: OGG1 Antibody - BSA Free [NB100-106] - The H&E staining ((a)–(c)) & IHC staining for oxidative DNA damage, 8-oxo-dGuo ((d)–(g)), DNA repair enzyme, hOGG1 ((h)–(k)), & antioxidant proteins, CAT ((l)–(o)), GCLC ((p)–(s)), GPx ((t)–(w)), Nrf2 ((x)–(aa)), & MnSOD ((ab)–(ae)), in control subjects & tumor & nontumor lesions of BCC patients. Values given are mean ± SD. The statistical significance of differences between the control & case & between adjacent epidermis & tumor lesions of BCC patients was evaluated by nonparametric variables with Kruskal-Wallis test followed by Dunnett's post hoc test. ∗P < 0.05, ∗∗P < 0.01, ∗∗∗P < 0.001 compared to control; ##P < 0.01, ###P < 0.001 compared to tumor lesions of BCC patients. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27057281), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-106_rabbit-polyclonal-ogg1-antibody-31020241538247.jpg)
![Immunohistochemistry: OGG1 Antibody - BSA Free [NB100-106] - IHC-P analysis of hOGG1 protein expression in serous ovarian cancer: (A) Normal ovarian tissue treated with anti-hOGG1 antibody, biotinylated anti-rabbit IgG secondary antibody, & avidin-biotin-peroxidase complex, & counterstained with p-dimethylaminobenzaldehyde reagent (magnification 100 x); (B) serous cystadenoma with positive staining (magnification 200 x); (C) LG-SOC tissue with moderate positive staining (magnification 200 x); & (D) HG-SOC with negative staining (magnification 200 x). Black arrow pointed at the immunostained epithelial cells. Image collected & cropped by CiteAb from the following publication (//ovarianresearch.biomedcentral.com/articles/10.1186/1757-2215-6-74), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-106_rabbit-polyclonal-ogg1-antibody-310202415392553.jpg)
![Western Blot: OGG1 Antibody - BSA Free [NB100-106] - EBNA1 promotes the upregulation of oxidative DNA damage repair pathways in EBV converted cell lines & EBV positive BLs. a Representative western blots illustrating the expression of MTH1, OGG1, & MUTYH in pairs of EBV-negative & -positive cell lines. GAPDH was used as loading control. b Densitometry quantification of the specific bands. The intensity of the specific band in EBV positive cells relative the EBV-negative parental is shown. Mean ± SE of four independent experiments. c Representative western blots illustrating the expression of EBNA1, MTH1, OGG1, & MUTYH in the Mutu cell lines. d Densitometry quantification of expression in the EBV positive cell lines relative to the EBV-negative Mutu-30. Mean ± SE of four independent experiments Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31511648), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-106_rabbit-polyclonal-ogg1-antibody-310202415363736.jpg)
![Western Blot: OGG1 Antibody - BSA Free [NB100-106] - EBNA1 promotes the upregulation of oxidative DNA damage repair pathways in EBV converted cell lines & EBV positive BLs. a Representative western blots illustrating the expression of MTH1, OGG1, & MUTYH in pairs of EBV-negative & -positive cell lines. GAPDH was used as loading control. b Densitometry quantification of the specific bands. The intensity of the specific band in EBV positive cells relative the EBV-negative parental is shown. Mean ± SE of four independent experiments. c Representative western blots illustrating the expression of EBNA1, MTH1, OGG1, & MUTYH in the Mutu cell lines. d Densitometry quantification of expression in the EBV positive cell lines relative to the EBV-negative Mutu-30. Mean ± SE of four independent experiments Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31511648), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-106_rabbit-polyclonal-ogg1-antibody-31020241535637.jpg)
![Immunohistochemistry: OGG1 Antibody - BSA Free [NB100-106] - IHC-P analysis of hOGG1 protein expression in serous ovarian cancer: (A) Normal ovarian tissue treated with anti-hOGG1 antibody, biotinylated anti-rabbit IgG secondary antibody, & avidin-biotin-peroxidase complex, & counterstained with p-dimethylaminobenzaldehyde reagent (magnification 100 x); (B) serous cystadenoma with positive staining (magnification 200 x); (C) LG-SOC tissue with moderate positive staining (magnification 200 x); & (D) HG-SOC with negative staining (magnification 200 x). Black arrow pointed at the immunostained epithelial cells. Image collected & cropped by CiteAb from the following publication (//ovarianresearch.biomedcentral.com/articles/10.1186/1757-2215-6-74), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-106_rabbit-polyclonal-ogg1-antibody-310202415293311.jpg)
![Immunohistochemistry: OGG1 Antibody - BSA Free [NB100-106] - IHC-P analysis of hOGG1 protein expression in serous ovarian cancer: (A) Normal ovarian tissue treated with anti-hOGG1 antibody, biotinylated anti-rabbit IgG secondary antibody, & avidin-biotin-peroxidase complex, & counterstained with p-dimethylaminobenzaldehyde reagent (magnification 100 x); (B) serous cystadenoma with positive staining (magnification 200 x); (C) LG-SOC tissue with moderate positive staining (magnification 200 x); & (D) HG-SOC with negative staining (magnification 200 x). Black arrow pointed at the immunostained epithelial cells. Image collected & cropped by CiteAb from the following publication (//ovarianresearch.biomedcentral.com/articles/10.1186/1757-2215-6-74), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-106_rabbit-polyclonal-ogg1-antibody-310202415175230.jpg)
![Western Blot: OGG1 Antibody - BSA Free [NB100-106] - Immunoblot analysis of kidney lysates.(A) Blot membranes were incubated with the antibodies against Nrf2, p53 & 8-oxoguanine glycosylase alpha (OGG1 alpha ). The mean integrated optical density is related to actin for Nrf2 (B), p53 (C) & mature 8-oxoguanine glycosylase alpha (D) levels. Results are given as a mean ± S.E.M. KD4, KD6, KD8 – groups of Eker rats (Tsc2+/−) treated with HFKD for four, six or eight mo., respectively; ST – Eker rats fed with a standard diet; LE ST – wild-type Long Evans rats treated with a standard diet; LE KD – wild-type Long Evans rats treated with a ketogenic diet similarly to the KD6 group. *P < 0.05, **p < 0.01, ***p < 0.001 as compared to ST unless otherwise stated (horizontal line) for ANOVA with a Fisher post hoc test. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26892894), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-106_rabbit-polyclonal-ogg1-antibody-31020241537192.jpg)
![Western Blot: OGG1 Antibody - BSA Free [NB100-106] - EBNA1 expression is associated with upregulation of MTH1 & oxidative damage repair pathways. The expression of MTH1, OGG1, & MUTYH was investigated by western blots & qPCR in BJAB-tTAE1 cells upon addition & withdrawal of doxycycline. a Representative western blots illustrating the correlation between the reversible down- & upregulation of MTH1 & EBNA1 in BJAB-tTAE1 cells upon addition & withdrawal of doxycycline. GAPDH was used as loading control. b Densitometry quantification of MTH1 & EBNA1 expression in BJAB-tTAE1 cells. The mean intensity of the MTH1 & EBNA1 specific bands relative to GAPDH in three independent experiments is shown in the figure. c Regression analysis of the relationship between expression levels of MTH1 & EBNA1. The data from three independent experiments were used for the plot. d Representative western blots illustrating the expression of MTH1, MUTYH, & OGG1 in BJAB-tTAE1 cells cultured for two weeks in the presence or absence of doxycycline. e Fold change is the ratio between the intensity of the specific band in cells cultured without or with doxycycline. The mean ± SD of four independent experiments is shown. f qPCR analysis of the levels of MTH1, OGG1, & MUTYH transcripts in BJAB-tTAE1 cells cultured for 2 weeks in the presence or absence of doxycycline. The mean ± SE of the fold change in six independent experiments each performed in triplicate is shown Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31511648), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-106_rabbit-polyclonal-ogg1-antibody-3102024155529.jpg)
![Western Blot: OGG1 Antibody - BSA Free [NB100-106] - The antioxidant pathways are activated during EBV infection & are required for growth transformation. Freshly isolated B-lymphocytes infected with the transforming B95-8 strain of EBV were cultured for up to 2 weeks in the presence or absence of MTH1 inhibitors. Protein expression was monitored by western blots, cell proliferation & activation of the DDR were assessed by 3H-Thy incorporation & staining for gamma H2AX, respectively. a representative western blots illustrating the parallel increase of MTH1 & EBNA1 expression following EBV infection & mean ± SE of the intensity of the MTH1 specific band in five independent experiments. b Representative western blots illustrating the expression of MTH1, MUTYH & OGG1 in ex vivo untreated B-cell & freshly EBV infected & SAC induced B blasts cultured for comparable times & showing similar levels of cell proliferation. c Quantification of the specific bands. Relative expression is the ration between the intensity in the treated cells versus freshly harvested cells. The mean ± SE of three to four independent experiments is shown. d Inhibition of MTH1 prevents the establishment of EBV transformed lymphoblastoid cell lines. 3H-Thy incorporation was measured after culture of freshly EBV infected B-lymphocytes in the presence of the indicated amounts of MTH1 inhibitors. Depending on the condition of the cultures harvesting was done after ten to fifteen days. e Inhibition of MTH1 strongly enhances the induction of DNA damage in freshly EBV infected cells. DNA damage was detected by gamma H2AX staining. f Mean ± SE of the % gamma H2AX positive cells in three independent experiments. *P < 0.05; **P < 0.01 Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31511648), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-106_rabbit-polyclonal-ogg1-antibody-310202415523940.jpg)
![Immunohistochemistry: OGG1 Antibody - BSA Free [NB100-106] - Comparison of the expression of OGG1 (A) & PARP-1 (B) protein in normal colon tissue, polyp & cancer tissue of adenoma (AD, n = 68) & carcinoma (CRC, n = 103) patients.Immunohistochemical detection in paraffin embedded sections stained with hematoxylin & eosin. Center mark in the box indicates the medians of the samples. The length of each box (IQR, interquartile range) represents the range within which the central 50% of the values fell, with the vertical edges placed at the first & third quartiles. Whiskers show variability outside the upper & lower quartiles. P was obtained with the Mann-Whitney test. Representative examples of the levels of PARP-1 protein in tissues of CRC patients determined by Western analysis. The analysis was performed on tumor & normal tissues of 41 CRC patients (C). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/25526641), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-106_rabbit-polyclonal-ogg1-antibody-3102024165727.jpg)
![Western Blot: OGG1 Antibody - BSA Free [NB100-106] - HDAC1 modulates OGG1 activity.a, b Representative images & quantification of OGG1 acetylation assessed by WB analysis using anti-acetylated lysine (Ac-Lysine, 4G12). Recombinant OGG1 (100 ng) first acetylated by p300 (25 ng), & incubated w/ titrated amount of HDAC1 (25 & 50 ng). a, b Four replicates from four independent experiments. c Reaction scheme of OGG1 cleavage assay. 5′IRDye800CW-labeled oligonucleotides (33 nt) contain an 8-oxoG base at position 17 & complementary unlabeled strand used as OGG1 substrate. Recombinant OGG1 proteins incubated w/ OGG1 substrate & resolved by 20% denaturing urea PAGE. d, e Representative images & quantification of OGG1 cleavage activity on reaction samples shown in Fig. 3a. d, e Seven replicates from four independent experiments. Nuclear extracts from HEK cells overexpressing OGG1 used as a positive control. f Co-immunoprecipitation of OGG1 w/ HDAC1 in cortical nuclear extracts from 2-month-old wild-type mice (n = 2) from one experiment. The asterisks indicate nonspecific cross-reaction w/ IgG heavy & light chains. g, h Representative images & quantification of acetylation status of endogenous OGG1 in hippocampal lysates of 13M control (n = 4) & Hdac1 cKO (n = 4) animals. g, h Two independent experiments. i Representative images of OGG1 cleavage assay using hippocampal nuclear extracts of 13M control & Hdac1 cKO mice. j Quantification of cleaved 17-nt products after OGG1 cleavage assay using hippocampal nuclear extracts of 13M control (n = 6) & Hdac1 cKO (n = 4) animals. i, j Two independent experiments. All values are shown as mean ± SEM. Statistical analysis: b, e one-way ANOVA w/ Tukey’s post hoc test; h, j two-tailed Student’s t test. Source data are provided as a Source Data file. Image collected & cropped by CiteAb from following publication (//pubmed.ncbi.nlm.nih.gov/32424276), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-106_rabbit-polyclonal-ogg1-antibody-31020241682186.jpg)
![Western Blot: APE Antibody (13B8E5C2) - BSA Free [NB100-116] - APE Antibody (13B8E5C2) [NB100-116] - Whole cell protein from human HeLa, A431, mouse Neuro2A and rat PC12 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-APE-1 in block buffer and detected with an anti-mouse HRP secondary antibody using chemiluminescence.](http://images.novusbio.com/fullsize/APE-Antibody-13B8E5C2-Western-Blot-NB100-116-img0014.jpg "Western Blot: APE Antibody (13B8E5C2) - BSA Free [NB100-116] - APE Antibody (13B8E5C2) [NB100-116] - Whole cell protein from human HeLa, A431, mouse Neuro2A and rat PC12 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-APE-1 in block buffer and detected with an anti-mouse HRP secondary antibody using chemiluminescence.")
![<b>Genetic Strategies Validation. </b>Knockdown Validated: APE Antibody (13B8E5C2) - BSA Free [NB100-116] - APE Antibody (13B8E5C2) [NB100-116] - Repression of p21 by APE1 in p53-null cells and effect of ectopic p53 in this repression. Representative Western analysis of p53, APE1, p21 and alpha-Tubulin levels in the same HCT116p53null cells. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0068467) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/APE-Antibody-13B8E5C2-Knockdown-Validated-NB100-116-img0016.jpg)
![Immunocytochemistry/Immunofluorescence: APE Antibody (13B8E5C2) - BSA Free [NB100-116] - APE Antibody (13B8E5C2) [NB100-116] - HeLa cells stained NB100-116 (Green) detected with DyLight Fluor 488 conjugated anti-rabbit IgG secondary antibody. Nuclei are counterstained with Hoechst 33258 (Blue).](http://images.novusbio.com/fullsize/APE-Antibody-13B8E5C2-Immunocytochemistry-Immunofluorescence-NB100-116-img0010.jpg)
![Immunohistochemistry: APE Antibody (13B8E5C2) - BSA Free [NB100-116] - APE Antibody (13B8E5C2) [NB100-116] - Immunohistochemical staining of APE1. A. Nuclear staining in the luminal epithelium of normal breast ducts and lobules. B. Low, and C. high nuclear APE1 expression in invasive breast cancer. (magnification x400). Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0099528) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/APE-Antibody-13B8E5C2-Immunohistochemistry-NB100-116-img0017.jpg)
![<b>Biological Strategies Validation. </b>Chromatin Immunoprecipitation (ChIP): APE Antibody (13B8E5C2) - BSA Free [NB100-116] - APE Antibody (13B8E5C2) [NB100-116] - Association of p53 and APE1 on p53-binding sites in p21 promoter. Re-ChIP analysis (first IP with alpha-APE1 and the second IP with alpha-p53 antibody) showing simultaneous recruitment of APE1 and p53 in control vs. EPE treated cells; *: p value <0.05 (n=2) calculated based on APE1/p53 enriched DNA from control vs. etoposide treated cells. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0068467) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/APE-Antibody-13B8E5C2-Chromatin-Immunoprecipitation-ChIP-NB100-116-img0015.jpg)
![Simple Western: APE Antibody (13B8E5C2) - BSA Free [NB100-116] - APE Antibody (13B8E5C2) [NB100-116] - Image shows a specific band for APE1 in 0.1 mg/mL of HeLa lysate. This experiment was performed under reducing conditions using the 12-230kDa separation system. * Non-specific interaction with the 230 kDa Simple Western standard may be seen with this antibody.](http://images.novusbio.com/fullsize/APE-Antibody-13B8E5C2-Simple-Western-NB100-116-img0012.jpg)
![Immunocytochemistry/Immunofluorescence: APE Antibody (13B8E5C2) - BSA Free [NB100-116] - APE Antibody (13B8E5C2) [NB100-116] - HeLa cells were fixed for 10 minutes using 10% formalin and then permeabilized for 5 minutes using 1X PBS + 0.05% Triton X-100. The cells were incubated with anti-APE (13B8E5C2) at 5 ug/mL overnight at 4C and detected with an anti-mouse 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/APE-Antibody-13B8E5C2-Immunocytochemistry-Immunofluorescence-NB100-116-img0013.jpg)
![Western Blot: APE Antibody (13B8E5C2) - BSA Free [NB100-116] - APE Antibody (13B8E5C2) [NB100-116] - Ovarian Cancer cell lines.](http://images.novusbio.com/fullsize/APE-Antibody-13B8E5C2-Western-Blot-NB100-116-img0008.jpg)
![Immunocytochemistry/Immunofluorescence: APE Antibody (13B8E5C2) - BSA Free [NB100-116] - APE Antibody (13B8E5C2) [NB100-116] - Immunocytochemical detection of APE-ref-1 in breast cancer cell line MDA MB 231.](http://images.novusbio.com/fullsize/APE-Antibody-13B8E5C2-Immunocytochemistry-Immunofluorescence-NB100-116-img0009.jpg)
![Immunohistochemistry-Paraffin: APE Antibody (13B8E5C2) - BSA Free [NB100-116] - APE Antibody (13B8E5C2) [NB100-116] - APE1 antibody was tested in human breast cancer xenograft using DAB with hematoxylin counterstain.](http://images.novusbio.com/fullsize/APE-Antibody-13B8E5C2-Immunohistochemistry-Paraffin-NB100-116-img0001.jpg)
![Chromatin Immunoprecipitation: APE Antibody (13B8E5C2) - BSA Free [NB100-116] - Association of APE1 & AP4 in p21 proximal promoter region.(A & B) ChIP Real Time PCR analysis showing relative enrichment of (A) APE1 & (B) AP4 in p21 proximal promoter containing AP4-responsive E-Box elements in HCT116p53null cells. (C) Re-ChIP (first IP with alpha -APE1 & the second IP with alpha -AP4 antibody) analysis showing simultaneous recruitment of APE1 & AP4 in this promoter region. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/23874636), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-116_mouse-monoclonal-ape-antibody-13b8e5c2-310202415394546.jpg)
![Western Blot: APE Antibody (13B8E5C2) - BSA Free [NB100-116] - Effect of APE1 on p21 activation in p53 WT cells.(A) Western analysis for APE1 level in WT APE1 & N delta 42 APE1 overexpressing cells. (B) Real Time RT-PCR analysis showing relative quantitation of p21 transcript level in etoposide-treated WT APE1-overexpressing HCT116WT cells & N delta 42 APE1 overexpressing cells; *: p value <0.05 (n = 2) calculated from control (empty vector transfection) vs. WT APE1 overexpression, WT APE1 overexpression along with etoposide treatment or N delta 42 overexpression. (C) Luciferase activity in cells co-transfected with empty or WT APE1-expression vector & p21 promoter-luciferase construct; *: p value <0.05 (n = 2) calculated from control (empty vector transfection) vs. APE1 overexpression. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/23874636), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-116_mouse-monoclonal-ape-antibody-13b8e5c2-310202415371965.jpg)
![Western Blot: APE Antibody (13B8E5C2) - BSA Free [NB100-116] - Analysis of single strand break repair in MCF-7 monolayer & mammosphere cell populations. (a) Cells were exposed to 4 Gy 60Co gamma -radiation & the relative degree of single-strand breakage (SSB) was determined by alkaline single-cell gel electrophoresis (comet assay) 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 SSB repair in response to 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 SSB repair proteins. alpha -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/nb100-116_mouse-monoclonal-ape-antibody-13b8e5c2-310202415525298.jpg)
![Western Blot: APE Antibody (13B8E5C2) - BSA Free [NB100-116] - Intracellular APE1/Ref-1 was targeted to the plasma membrane in response to acetylation. (A & B) Whole cell lysates were immunoprecipitated using an anti-acetyl lysine antibody, followed by immunoblotting with the polyclonal anti-APE1/Ref-1 antibody. The blots were stripped & re-probed with anti-beta -actin & APE1/Ref-1 antibody to ensure equal protein loading. Similar results were obtained from replicate experiments. Column, mean (n = 3); bars, SE. *, p < 0.05, significantly different compared with control or between group by one-way ANOVA followed by Bonferroni’s multiple comparison test. (C,D) Membrane fractions or whole cell lysates were prepared from the TSA-treated cells. Immunoblotting for APE1/Ref-1 was performed using the polyclonal anti-APE1/Ref-1 antibody. Blots were stripped & re-probed with anti-N-cadherin & anti-beta -actin antibodies to control for differences in protein loading. Fold changes in the levels of APE1/Ref-1 in the plasma membrane fraction relative to the control are shown. †, indicates molecular marker (N-cadherin) of left image. Column mean (n = 3); bars, SE.*, p < 0.05 indicates a significantly different result compared with control or between groups by one-way ANOVA followed by Bonferroni’s multiple comparison test. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31261750), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-116_mouse-monoclonal-ape-antibody-13b8e5c2-310202415541999.jpg)
![Immunocytochemistry/ Immunofluorescence: APE Antibody (13B8E5C2) - BSA Free [NB100-116] - AcAPE1 is exclusively associated w/ chromatin & remains bound to condensed chromosomes. (A & B) Asynchronous normal lung fibroblast IMR90 cells & lung adenocarcinoma A549 cells immunostained w/ anti-APE1 & anti-AcAPE1 Abs, counterstained w/ DAPI, & visualized by confocal microscopy & 3D SIM. (C) Colocalization of AcAPE1 w/ histone H3 or active enhancer-specific histone marker acetylated H3K27 (H3K27Ac). (D) BJ-hTERT cells serum starved for 72 h & then fixed at different time points. Cells immunostained w/ anti-APE1 & anti-AcAPE1 Abs & counterstained w/ anti-TO-PRO-3 iodide Ab. (E) Mitotic A549 cells immunostained w/ anti-APE1 & anti-AcAPE1 & visualized by 3D SIM. (F) BJ-hTERT cells either serum starved for 72 h (G0/G1 phase), treated w/ nocodazole (mitotic cells) or aphidicolin (G1/S phase synchronized cells), or untreated, & whole-cell extracts isolated using 150 mM or 300 mM salt-containing lysis buffer. Western blot analysis for anti-APE1 & anti-AcAPE1 levels performed. Anti-HSC70 used as loading control. (G) A proximal ligation assay performed w/ mouse anti-APE1 & rabbit anti-APE1 (mAPE1 & Rabbit-APE1), mouse anti-mouse APE1 & rabbit anti-AcAPE1 (mAPE1 & rAcAPE1), & rabbit anti-AcAPE1 & mouse anti-histone H3 (mHistone H3 & rAcAPE1) to confirm the chromatin association of AcAPE1. Mouse IgG (mIgG) & rabbit anti-AcAPE1 used as a control. At least 50 cells counted for PLA foci. (H) Colocalization of p300 & AcAPE1 on chromatin (DAPI). (I) HCT116 cells transfected w/ E1A & mutant E1A, & at 48 h after transfection, IF performed. Cells immunostained w/ anti-p300 & anti-APE1 or anti-AcAPE1 & counterstained w/ DAPI. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27994014), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-116_mouse-monoclonal-ape-antibody-13b8e5c2-310202415533841.jpg)
![Western Blot: APE Antibody (13B8E5C2) - BSA Free [NB100-116] - XPF is epistatic to APE in the gemcitabine resistance. The expression of XPF and/or APE was suppressed by siRNAs in HeLa cells & the cellular sensitivity to gemcitabine was examined. XPF- or APE-suppressed HeLa cells (closed square & closed triangle, respectively) showed sensitivity to gemcitabine. Cosuppression of XPF & APE (closed circle with dashed line) resulted in the sensitivity to gemcitabine similar to the sensitivity induced by the suppression of XPF or APE individually. A control siRNA (siControl) was used as a control (open diamond). Three independent experiments were performed & averages of surviving fraction are plotted. The error bars show standard deviations. The differences in the gemcitabine sensitivity between the control cells & the cells treated with siXPF, siAPE, or siXPF+siAPE are statistically significant at 10 nM & 50 nM with p<0.05. The western blots showed a significant suppression of XPF (more than 95%) & ~75% reduction in the expression of APE with the siRNA treatment. The cosuppression experiments with two siRNAs, siXPF & siAPE, resulted in similar levels of suppression of each protein induced by individual siRNA (more than 95% reduction in XPF & ~85% reduction in APE). Tubulin was used as a protein loading control. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30941207), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-116_mouse-monoclonal-ape-antibody-13b8e5c2-310202415523918.jpg)
![Immunocytochemistry/ Immunofluorescence: APE Antibody (13B8E5C2) - BSA Free [NB100-116] - Plasma membrane associated APE1/Ref-1 is bound to ABCA1 in response to acetylation. Cells transiently expressing wild type APE1/Ref-1-FLAG or mutant APE1/Ref-1(K6/7R)-FLAG were treated with 1 µM TSA for 1 h. (A) Whole cell lysates were immunoprecipitated using the monoclonal anti-ABCA1 antibody, followed by immunoblot with the anti-FLAG antibody. (B) For reverse immunoprecipitation, cell lysates were immunoprecipitated with anti-APE1/Ref-1 antibody followed by immunoblot analysis with the polyclonal anti-ABCA1 antibody. Blots were stripped & re-probed with anti-ABCA1 or FLAG antibodies to ensure equal protein loading & no contamination of cellular proteins. Similar results were observed in replicate experiments. Columns, mean (n = 2-3); bars, SE. *, p < 0.05 indicates a significantly different result from control cells according to unpaired t-tests. (C) The binding between APE1/Ref-1 & ABCA1 in the plasma membrane was visualized using with a Duolink II PLA system with primary polyclonal anti-APE1/Ref-1 & monoclonal anti-ABCA1 antibodies (PLA†). The PLA-specific fluorescence which represents the APE1/Ref-1-ABCA1 signal, & the DAPI nuclear staining are in red & blue, respectively. The experiment was repeated multiple times with similar results; the data shown here are from a representative experiment. Optical slices were examined using a 40× oil immersion objective with a 2× zoom factor. Scale bar, 20 µm (×80). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31261750), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-116_mouse-monoclonal-ape-antibody-13b8e5c2-31020241555225.jpg)
![Immunocytochemistry/ Immunofluorescence: APE Antibody (13B8E5C2) - BSA Free [NB100-116] - APE1 acetylation enhances its stability on chromatin & its interaction with downstream BER proteins. (A) Colocalization of ligase III & AcAPE1 in A549 cells. Cells were immunostained with anti-ligase III & anti-AcAPE1 Abs. (B) WT or K5R mutant APE1-overexpressing HEK293T cells were treated with TSA-nicotinamide (NAM) for 6 h or not treated, & the nuclear extract was immunoprecipitated using anti-FLAG Ab & immunoblotted with anti-XRCC1 & anti-FLAG Abs. (C) A549 cells were fixed with paraformaldehyde before (top) or after treatment with Triton X-100 (0.5%) (middle) or Triton X-100 plus salt (100 mM KCl) (bottom) & immunostained with anti-APE1 or anti-AcAPE1 Abs & counterstained with DAPI. (D) Acetylation of APE1 induces a conformational change in APE1. The distinct intrinsic fluorescence emission spectra of APE1 & AcAPE1 at 280 nm are shown. A.U., absorbance units. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27994014), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-116_mouse-monoclonal-ape-antibody-13b8e5c2-3102024165741.jpg)
![Immunocytochemistry/ Immunofluorescence: APE Antibody (13B8E5C2) - BSA Free [NB100-116] - AcAPE1 is exclusively associated w/ chromatin & remains bound to condensed chromosomes. (A & B) Asynchronous normal lung fibroblast IMR90 cells & lung adenocarcinoma A549 cells immunostained w/ anti-APE1 & anti-AcAPE1 Abs, counterstained w/ DAPI, & visualized by confocal microscopy & 3D SIM. (C) Colocalization of AcAPE1 w/ histone H3 or active enhancer-specific histone marker acetylated H3K27 (H3K27Ac). (D) BJ-hTERT cells serum starved for 72 h & then fixed at different time points. Cells immunostained w/ anti-APE1 & anti-AcAPE1 Abs & counterstained w/ anti-TO-PRO-3 iodide Ab. (E) Mitotic A549 cells immunostained w/ anti-APE1 & anti-AcAPE1 & visualized by 3D SIM. (F) BJ-hTERT cells either serum starved for 72 h (G0/G1 phase), treated w/ nocodazole (mitotic cells) or aphidicolin (G1/S phase synchronized cells), or untreated, & whole-cell extracts isolated using 150 mM or 300 mM salt-containing lysis buffer. Western blot analysis for anti-APE1 & anti-AcAPE1 levels performed. Anti-HSC70 used as loading control. (G) A proximal ligation assay performed w/ mouse anti-APE1 & rabbit anti-APE1 (mAPE1 & Rabbit-APE1), mouse anti-mouse APE1 & rabbit anti-AcAPE1 (mAPE1 & rAcAPE1), & rabbit anti-AcAPE1 & mouse anti-histone H3 (mHistone H3 & rAcAPE1) to confirm the chromatin association of AcAPE1. Mouse IgG (mIgG) & rabbit anti-AcAPE1 used as a control. At least 50 cells counted for PLA foci. (H) Colocalization of p300 & AcAPE1 on chromatin (DAPI). (I) HCT116 cells transfected w/ E1A & mutant E1A, & at 48 h after transfection, IF performed. Cells immunostained w/ anti-p300 & anti-APE1 or anti-AcAPE1 & counterstained w/ DAPI. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27994014), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-116_mouse-monoclonal-ape-antibody-13b8e5c2-31020241682167.jpg)
![Immunocytochemistry/ Immunofluorescence: APE Antibody (13B8E5C2) - BSA Free [NB100-116] - APE1 is acetylated after binding to AP sites in the chromatin. (A) BJ-hTERT cells were treated with MX (50 mM) for the indicated times. IF was performed using anti-APE1 & anti-AcAPE1, & counterstaining with DAPI was used. (B) HCT116 cells were treated with various doses of MX for 30 min, IF was performed using anti-APE1 & anti-AcAPE1, & counterstaining with DAPI was used. (C) HCT116 cells were treated with 50 mM MX for 30 min, IF was performed using anti-OGG1, & counterstaining with DAPI was used. (D) BJ-hTERT cells pretreated with 50 mM MX for 30 min or not pretreated were exposed to MMS (2 mM) for 1 h. IF was performed using anti-APE1 & anti-AcAPE1, & counterstaining with DAPI was used. Confocal microscopy was used to visualize the AcAPE1 levels in control cells & cells treated with MMS or MX, or both. (E) ChIP with anti-OGG1 antibody followed by Western blotting (ChIP-on-Western) was performed to examine the association of AcAPE1 & ligase III on chromatin after induction of DNA damage with GO. (F) The association of AcAPE1 with the endogenous p21 promoter in control or MMS- or MX-treated cells was examined by promoter-directed ChIP using anti-AcAPE1. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27994014), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-116_mouse-monoclonal-ape-antibody-13b8e5c2-31020241612630.jpg)
![Immunocytochemistry/ Immunofluorescence: APE Antibody (13B8E5C2) - BSA Free [NB100-116] - APE1 is acetylated after binding to AP sites in the chromatin. (A) BJ-hTERT cells were treated with MX (50 mM) for the indicated times. IF was performed using anti-APE1 & anti-AcAPE1, & counterstaining with DAPI was used. (B) HCT116 cells were treated with various doses of MX for 30 min, IF was performed using anti-APE1 & anti-AcAPE1, & counterstaining with DAPI was used. (C) HCT116 cells were treated with 50 mM MX for 30 min, IF was performed using anti-OGG1, & counterstaining with DAPI was used. (D) BJ-hTERT cells pretreated with 50 mM MX for 30 min or not pretreated were exposed to MMS (2 mM) for 1 h. IF was performed using anti-APE1 & anti-AcAPE1, & counterstaining with DAPI was used. Confocal microscopy was used to visualize the AcAPE1 levels in control cells & cells treated with MMS or MX, or both. (E) ChIP with anti-OGG1 antibody followed by Western blotting (ChIP-on-Western) was performed to examine the association of AcAPE1 & ligase III on chromatin after induction of DNA damage with GO. (F) The association of AcAPE1 with the endogenous p21 promoter in control or MMS- or MX-treated cells was examined by promoter-directed ChIP using anti-AcAPE1. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27994014), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-116_mouse-monoclonal-ape-antibody-13b8e5c2-310202415532029.jpg)
![Immunocytochemistry/ Immunofluorescence: APE Antibody (13B8E5C2) - BSA Free [NB100-116] - AcAPE1 is exclusively associated w/ chromatin & remains bound to condensed chromosomes. (A & B) Asynchronous normal lung fibroblast IMR90 cells & lung adenocarcinoma A549 cells immunostained w/ anti-APE1 & anti-AcAPE1 Abs, counterstained w/ DAPI, & visualized by confocal microscopy & 3D SIM. (C) Colocalization of AcAPE1 w/ histone H3 or active enhancer-specific histone marker acetylated H3K27 (H3K27Ac). (D) BJ-hTERT cells serum starved for 72 h & then fixed at different time points. Cells immunostained w/ anti-APE1 & anti-AcAPE1 Abs & counterstained w/ anti-TO-PRO-3 iodide Ab. (E) Mitotic A549 cells immunostained w/ anti-APE1 & anti-AcAPE1 & visualized by 3D SIM. (F) BJ-hTERT cells either serum starved for 72 h (G0/G1 phase), treated w/ nocodazole (mitotic cells) or aphidicolin (G1/S phase synchronized cells), or untreated, & whole-cell extracts isolated using 150 mM or 300 mM salt-containing lysis buffer. Western blot analysis for anti-APE1 & anti-AcAPE1 levels performed. Anti-HSC70 used as loading control. (G) A proximal ligation assay performed w/ mouse anti-APE1 & rabbit anti-APE1 (mAPE1 & Rabbit-APE1), mouse anti-mouse APE1 & rabbit anti-AcAPE1 (mAPE1 & rAcAPE1), & rabbit anti-AcAPE1 & mouse anti-histone H3 (mHistone H3 & rAcAPE1) to confirm the chromatin association of AcAPE1. Mouse IgG (mIgG) & rabbit anti-AcAPE1 used as a control. At least 50 cells counted for PLA foci. (H) Colocalization of p300 & AcAPE1 on chromatin (DAPI). (I) HCT116 cells transfected w/ E1A & mutant E1A, & at 48 h after transfection, IF performed. Cells immunostained w/ anti-p300 & anti-APE1 or anti-AcAPE1 & counterstained w/ DAPI. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27994014), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-116_mouse-monoclonal-ape-antibody-13b8e5c2-31020241612615.jpg)
![Immunocytochemistry/ Immunofluorescence: APE Antibody (13B8E5C2) - BSA Free [NB100-116] - AcAPE1 is exclusively associated w/ chromatin & remains bound to condensed chromosomes. (A & B) Asynchronous normal lung fibroblast IMR90 cells & lung adenocarcinoma A549 cells immunostained w/ anti-APE1 & anti-AcAPE1 Abs, counterstained w/ DAPI, & visualized by confocal microscopy & 3D SIM. (C) Colocalization of AcAPE1 w/ histone H3 or active enhancer-specific histone marker acetylated H3K27 (H3K27Ac). (D) BJ-hTERT cells serum starved for 72 h & then fixed at different time points. Cells immunostained w/ anti-APE1 & anti-AcAPE1 Abs & counterstained w/ anti-TO-PRO-3 iodide Ab. (E) Mitotic A549 cells immunostained w/ anti-APE1 & anti-AcAPE1 & visualized by 3D SIM. (F) BJ-hTERT cells either serum starved for 72 h (G0/G1 phase), treated w/ nocodazole (mitotic cells) or aphidicolin (G1/S phase synchronized cells), or untreated, & whole-cell extracts isolated using 150 mM or 300 mM salt-containing lysis buffer. Western blot analysis for anti-APE1 & anti-AcAPE1 levels performed. Anti-HSC70 used as loading control. (G) A proximal ligation assay performed w/ mouse anti-APE1 & rabbit anti-APE1 (mAPE1 & Rabbit-APE1), mouse anti-mouse APE1 & rabbit anti-AcAPE1 (mAPE1 & rAcAPE1), & rabbit anti-AcAPE1 & mouse anti-histone H3 (mHistone H3 & rAcAPE1) to confirm the chromatin association of AcAPE1. Mouse IgG (mIgG) & rabbit anti-AcAPE1 used as a control. At least 50 cells counted for PLA foci. (H) Colocalization of p300 & AcAPE1 on chromatin (DAPI). (I) HCT116 cells transfected w/ E1A & mutant E1A, & at 48 h after transfection, IF performed. Cells immunostained w/ anti-p300 & anti-APE1 or anti-AcAPE1 & counterstained w/ DAPI. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27994014), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-116_mouse-monoclonal-ape-antibody-13b8e5c2-310202415541968.jpg)
![Western Blot: APE Antibody (13B8E5C2) - BSA Free [NB100-116] - Repression of p21 by APE1 in p53-null cells & effect of ectopic p53 in this repression.(A & B) Real Time RT-PCR analysis showing relative quantitation of p21 transcript level in (A) HCT116p53null cells with WT & N delta 42 APE1 overexpression; *: p value (n = 4) calculated from control (empty vector transfection) vs. WT or N delta 42 APE1 overexpression, & (B) control (control siRNA) vs. APE1-depleted HCT116p53null cells; *: p value <0.05 (n = 4) calculated from control vs. APE1-depleted cells. (C) Effect of ectopic p53 expression on p21 transcript level in control vs. APE1-depleted HCT116p53null cells. First, cells were transfected with control siRNA or APE1 siRNA, the next day both the cell types were again transfected with empty vector or p53 expression vector & after 48 hrs the cells were harvested; signal from empty vector transfection in both control & APE1-depleted cells were set as reference samples; *: p value <0.05 (n = 3) calculated based on the effect of ectopic p53 expression over empty vector transfection in control vs. APE1-depleted cells. (D) Effect of APE1 depletion in control (empty vector transfected) vs. ectopic p53-expressing HCT116p53null cells; the same experiment was performed as in C but analyzed differently; signal from control siRNA-transfected cells in both empty vector transfected & ectopic p53 expressing cases were set as reference samples; *: p value <0.05 (n = 3) calculated based on the effect of APE1-depletion in empty vector transfected vs. ectopic p53 expressing cells. (E) Representative Western analysis of p53, APE1, p21 & alpha -Tubulin levels in the same HCT116p53null cells as in B–D. (F & G) Real Time RT-PCR analysis of p21 level in Saos2 cells as in C & D. *: p value <0.05 (n = 2). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/23874636), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-116_mouse-monoclonal-ape-antibody-13b8e5c2-3102024168212.jpg)
![Immunocytochemistry/ Immunofluorescence: APE Antibody (13B8E5C2) - BSA Free [NB100-116] - APE1 is acetylated after binding to AP sites in the chromatin. (A) BJ-hTERT cells were treated with MX (50 mM) for the indicated times. IF was performed using anti-APE1 & anti-AcAPE1, & counterstaining with DAPI was used. (B) HCT116 cells were treated with various doses of MX for 30 min, IF was performed using anti-APE1 & anti-AcAPE1, & counterstaining with DAPI was used. (C) HCT116 cells were treated with 50 mM MX for 30 min, IF was performed using anti-OGG1, & counterstaining with DAPI was used. (D) BJ-hTERT cells pretreated with 50 mM MX for 30 min or not pretreated were exposed to MMS (2 mM) for 1 h. IF was performed using anti-APE1 & anti-AcAPE1, & counterstaining with DAPI was used. Confocal microscopy was used to visualize the AcAPE1 levels in control cells & cells treated with MMS or MX, or both. (E) ChIP with anti-OGG1 antibody followed by Western blotting (ChIP-on-Western) was performed to examine the association of AcAPE1 & ligase III on chromatin after induction of DNA damage with GO. (F) The association of AcAPE1 with the endogenous p21 promoter in control or MMS- or MX-treated cells was examined by promoter-directed ChIP using anti-AcAPE1. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27994014), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-116_mouse-monoclonal-ape-antibody-13b8e5c2-31020241682160.jpg)
![Western Blot: APE Antibody (13B8E5C2) - BSA Free [NB100-116] - Intracellular APE1/Ref-1 was targeted to the plasma membrane in response to acetylation. (A & B) Whole cell lysates were immunoprecipitated using an anti-acetyl lysine antibody, followed by immunoblotting with the polyclonal anti-APE1/Ref-1 antibody. The blots were stripped & re-probed with anti-beta -actin & APE1/Ref-1 antibody to ensure equal protein loading. Similar results were obtained from replicate experiments. Column, mean (n = 3); bars, SE. *, p < 0.05, significantly different compared with control or between group by one-way ANOVA followed by Bonferroni’s multiple comparison test. (C,D) Membrane fractions or whole cell lysates were prepared from the TSA-treated cells. Immunoblotting for APE1/Ref-1 was performed using the polyclonal anti-APE1/Ref-1 antibody. Blots were stripped & re-probed with anti-N-cadherin & anti-beta -actin antibodies to control for differences in protein loading. Fold changes in the levels of APE1/Ref-1 in the plasma membrane fraction relative to the control are shown. †, indicates molecular marker (N-cadherin) of left image. Column mean (n = 3); bars, SE.*, p < 0.05 indicates a significantly different result compared with control or between groups by one-way ANOVA followed by Bonferroni’s multiple comparison test. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31261750), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-116_mouse-monoclonal-ape-antibody-13b8e5c2-31020241683933.jpg)
![Immunocytochemistry/ Immunofluorescence: APE Antibody (13B8E5C2) - BSA Free [NB100-116] - AcAPE1 is exclusively associated w/ chromatin & remains bound to condensed chromosomes. (A & B) Asynchronous normal lung fibroblast IMR90 cells & lung adenocarcinoma A549 cells immunostained w/ anti-APE1 & anti-AcAPE1 Abs, counterstained w/ DAPI, & visualized by confocal microscopy & 3D SIM. (C) Colocalization of AcAPE1 w/ histone H3 or active enhancer-specific histone marker acetylated H3K27 (H3K27Ac). (D) BJ-hTERT cells serum starved for 72 h & then fixed at different time points. Cells immunostained w/ anti-APE1 & anti-AcAPE1 Abs & counterstained w/ anti-TO-PRO-3 iodide Ab. (E) Mitotic A549 cells immunostained w/ anti-APE1 & anti-AcAPE1 & visualized by 3D SIM. (F) BJ-hTERT cells either serum starved for 72 h (G0/G1 phase), treated w/ nocodazole (mitotic cells) or aphidicolin (G1/S phase synchronized cells), or untreated, & whole-cell extracts isolated using 150 mM or 300 mM salt-containing lysis buffer. Western blot analysis for anti-APE1 & anti-AcAPE1 levels performed. Anti-HSC70 used as loading control. (G) A proximal ligation assay performed w/ mouse anti-APE1 & rabbit anti-APE1 (mAPE1 & Rabbit-APE1), mouse anti-mouse APE1 & rabbit anti-AcAPE1 (mAPE1 & rAcAPE1), & rabbit anti-AcAPE1 & mouse anti-histone H3 (mHistone H3 & rAcAPE1) to confirm the chromatin association of AcAPE1. Mouse IgG (mIgG) & rabbit anti-AcAPE1 used as a control. At least 50 cells counted for PLA foci. (H) Colocalization of p300 & AcAPE1 on chromatin (DAPI). (I) HCT116 cells transfected w/ E1A & mutant E1A, & at 48 h after transfection, IF performed. Cells immunostained w/ anti-p300 & anti-APE1 or anti-AcAPE1 & counterstained w/ DAPI. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27994014), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-116_mouse-monoclonal-ape-antibody-13b8e5c2-310202415535126.jpg)
![Chromatin Immunoprecipitation: APE Antibody (13B8E5C2) - BSA Free [NB100-116] - Association of p53 & APE1 on p53-binding sites in p21 promoter.(A) p21 promoter structure showing p53 & AP4 binding sites. (B) ChIP Real Time PCR analysis showing relative enrichment (2− delta CT) of APE1-immunoprecipitated DNA over that from control IgG in p21 promoter regions containing p53 binding sites 1 & 2 in HCT116WT cells. (C) Re-ChIP analysis (first IP with alpha -APE1 & the second IP with alpha -p53 antibody) showing simultaneous recruitment of APE1 & p53 in control vs. etoposide treated cells; *: p value <0.05 (n = 2) calculated based on APE1/p53 enriched DNA from control vs. etoposide treated cells. (D) Western analysis of FLAG immunoprecipitate (IP) to detect APE1-associated p53 & FLAG (APE1) from empty vector vs. FLAG-tagged WT APE1 or FLAG-tagged N delta 33 APE1 transfected HCT116WT cells (left panel) & from control vs. etoposide-treated WT APE1-FLAG transfected cells (right panel). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/23874636), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-116_mouse-monoclonal-ape-antibody-13b8e5c2-31020241683929.jpg)
![Western Blot: APE Antibody (13B8E5C2) - BSA Free [NB100-116] - Gemcitabine-induced recruitment of XPF to chromatin depends on APE. HCT116, APE-suppressed HCT116 (HCT116 shAPE), & XPF-deficient HCT116 (HCT116 g4-10) cells were treated with 1 μM of gemcitabine & chromatin fractions were isolated in the indicated time. The presence of XPF & APE was detected by western blots. The asterisk (∗) shows a cross-reacted protein with the anti-XPF antibody. Histone H2AX was used as a loading control. Gemcitabine-induced recruitment of XPF to chromatin (lanes 1-3) was compromised in HCT116 shAPE cell line (lanes 4-5). The chromatin-bound APE is not changed by the gemcitabine treatment (lanes 4-6, Supplementary Figure 5). A signal of XPF (and APE) was normalized with a signal of H2AX in each chromatin fraction using ImageJ software. Then a ratio of chromatin-bound XPF with gemcitabine to XPF in control was determined & depicted as bar graphs. Three independent experiments were performed & averages of the ratio at indicated time points were plotted. The error bars show standard deviations. Only the difference in the chromatin-bound XPF between chromatin from control experiments & chromatin that was incubated one hour with 1 μM gemcitabine is statistically significant in HCT116 (p<0.05). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30941207), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-116_mouse-monoclonal-ape-antibody-13b8e5c2-310202415541910.jpg)
![Simple Western: APE Antibody [NB100-101] - Lane view shows a specific band for APE1 in 0.1 mg/ml of HeLa lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system.](http://images.novusbio.com/fullsize/APE-Antibody-Simple-Western-NB100-101-img0011.jpg "Simple Western: APE Antibody [NB100-101] - Lane view shows a specific band for APE1 in 0.1 mg/ml of HeLa lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system.")
![Western Blot: APE Antibody [NB100-101] - Analysis of APE1 in cell lysates: 1. HeLa, 2. Ntera2, 3. A431, 4. HepG2, 5. MCF7, 6. NIH 3T3, 7. PC12, and 8. Cos 7.](http://images.novusbio.com/fullsize/APE-Antibody-Western-Blot-NB100-101-img0002.jpg)
![Immunohistochemistry: APE Antibody [NB100-101] - Immunohistochemical staining of APE-ref-1 in prostate cancer.](http://images.novusbio.com/fullsize/APE-Antibody-Immunohistochemistry-NB100-101-img0006.jpg)
![Western Blot: APE Antibody [NB100-101] - RKO cells were subjected to scrambled siRNA (Mock) or siRNA against TDP1 (TDP1KD) and cell lysates analyzed by immunoblotting (left). Control RKO (RKOSc siRNA) and RKO cells in which TDP1 levels were depleted (RKOTDP1 siRNA) were examined for their survival following exposure to the indicated doses of MMS, as described earlier in the text (right). Increasing the load of unrepaired methylated purines by exploiting the limited availability of TDP1 alone or in combination with canonical BER factors such as APE1 provides a new synthetic lethal setting to improve the clinical outcome of temozolomide-based cancer therapy. Image collected and cropped by CiteAb from the following publication (academic.oup.com/nar/article/42/5/3089/1051107), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/APE-Antibody-Western-Blot-NB100-101-img0012.jpg)
![Immunocytochemistry/Immunofluorescence: APE Antibody [NB100-101] - IF on HeLa cells. Image from verified customer review.](http://images.novusbio.com/fullsize/APE-Antibody-Immunocytochemistry-Immunofluorescence-NB100-101-img0009.jpg)
![Western Blot: APE Antibody [NB100-101] - SH-SY5Y (nuclear extract) tested at 1:1000 dilution. Image provided by verified customer review.](http://images.novusbio.com/fullsize/APE-Antibody-Western-Blot-NB100-101-img0008.jpg)
![Flow Cytometry: APE Antibody [NB100-101] - Spectral properties of Alexa Fluor(R) 488: an excitation maximum of 490 nm and an emission maximum of 525 nm. Use the Novus Spectra Viewer to identify the optimal laser(s) and filters for Alexa Fluor(R) 488 and to determine its compatibility with other fluorophores when designing a multicolor experiment. //www.novusbio.com/spectraviewer](http://images.novusbio.com/fullsize/APE-Antibody-Flow-Cytometry-NB100-101-img0013.jpg)
![Western Blot: APE Antibody [NB100-101] - Analysis of APE in human melanoma cell lysate using anti-APE antibody. Image from verified customer review.](http://images.novusbio.com/fullsize/APE-Antibody-Western-Blot-NB100-101-img0010.jpg)
![Immunocytochemistry/Immunofluorescence: APE Antibody [NB100-101] - Detection of APE1 (Green) in HepG2 cells using NB100-101. Nuclei (Blue) are counterstained with Hoechst 33258.](http://images.novusbio.com/fullsize/APE-Antibody-Immunocytochemistry-Immunofluorescence-NB100-101-img0007.jpg)
![Western Blot: APE Antibody - BSA Free [NB100-101] - Defective p53 activity leads to failure of the BER coordination system. (A) High-throughput microscopy analysis of TIG-1 cells transfected with plasmids expressing wild-type or mutant p53. Boxplots showing the distribution of APE1 staining intensity (in arbitrary units) in p53 low versus p53 overexpressing cells. Each p53 mutant is reported on top of the relevant plot. The dashed line highlights the median APE1 intensity in p53 low cells (N > 5000). NS: not statistically significant at P 8000). (D) Representative high-throughput immuno-fluorescence pictures showing TIG-1 cells stained for APE1 (right panel) & p53 (middle panel) after transfection with a p53 expressing plasmid. Cells that downregulating APE1 in response to p53 overexpression are marked by a contour line. Image collected & cropped by CiteAb from the following publication (//academic.oup.com/nar/article-lookup/doi/10.1093/nar/gkw015), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-101_rabbit-polyclonal-ape-antibody-310202415483627.jpg)
![Western Blot: APE Antibody - BSA Free [NB100-101] - Excessive AP-endonuclease activity in cells with p53 impairment leads to accumulation of genomic instability. (A) Representative western blotting analysis on WI38 (SV40) cells shows rescue of gamma H2AX staining upon co-depletion of XRCC1 & APE1. (B) Neutral Comet assay on WI38 (SV40) fibroblasts shows accumulation of DSBs upon XRCC1-depletion & rescue after co-depletion of XRCC1 & APE1. Results are expressed as mean ± SD of three independent experiments. (C) Representative western blotting analysis on WI38 (SV40) cells shows rescue of gamma H2AX staining after depletion of XRCC1 in presence of APE1 inhibitor III (APE1i III, 5 μM for 24 h), or AR03 (2.5 μM for 24 h). Actin was used as loading control in all western blotting experiments. Image collected & cropped by CiteAb from the following publication (//academic.oup.com/nar/article-lookup/doi/10.1093/nar/gkw015), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-101_rabbit-polyclonal-ape-antibody-31020241548519.jpg)
![Simple Western: PCNA Antibody (PC10) [NB500-106] - Image shows a specific band for PCNA in 0.5 mg/mL of HeLa lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system.](http://images.novusbio.com/fullsize/PCNA-Antibody-PC10-Simple-Western-NB500-106-img0008.jpg "Simple Western: PCNA Antibody (PC10) [NB500-106] - Image shows a specific band for PCNA in 0.5 mg/mL of HeLa lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system.")
![Immunocytochemistry/Immunofluorescence: PCNA Antibody (PC10) [NB500-106] - NIH3T3 cells were fixed and permeabilized for 10 minutes using -20C MeOH. The cells were incubated with anti-PCNA Antibody (PC10) NB500-106 at 1 ug/ml overnight at 4C and detected with an anti-mouse 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/PCNA-Antibody-PC10-Immunocytochemistry-Immunofluorescence-NB500-106-img0015.jpg)
![Immunohistochemistry-Paraffin: PCNA Antibody (PC10) [NB500-106] - Analysis of paraffin-embedded human colon carcinoma, showing nuclear localization.](http://images.novusbio.com/fullsize/PCNA-Antibody-PC10-Immunohistochemistry-Paraffin-NB500-106-img0007.jpg)
![Western Blot: PCNA Antibody (PC10) [NB500-106] - Analysis of human (HeLa lysate), murine (SV-T2 lysate), bovine (BAEC lysate), and porcine (PAE lysate) cell extracts.](http://images.novusbio.com/fullsize/PCNA-Antibody-PC10-Western-Blot-NB500-106-img0006.jpg)
![Western Blot: PCNA Antibody (PC10) [NB500-106] - Western blot of PCNA levels across different stages of the cell cycle. U-2 OS cells were synchronised at G1/S with 2 mM thymidine an released for 10 hours for G2/M or re-arrested in G2 for extended duration with 10uM RO-3306. Antibody at 1:2000. WB image submitted by a verified customer review.](http://images.novusbio.com/fullsize/PCNA-Antibody-PC10-Western-Blot-NB500-106-img0014.jpg)
![Immunohistochemistry-Frozen: PCNA Antibody (PC10) [NB500-106] - Paraformaldehyde fixed frozen section of brain from murine embryo using PCNA antibody clone PC10 (green), an IB4 antibody (red) and DAPI. Image provided by Dr. Siegenthaler via product review.](http://images.novusbio.com/fullsize/PCNA-Antibody-PC10-Immunohistochemistry-Frozen-NB500-106-img0009.jpg)
![Immunocytochemistry/Immunofluorescence: PCNA Antibody (PC10) [NB500-106] - PC12 cells were fixed and permeabilized for 10 minutes using -20C MeOH. The cells were incubated with anti-PCNA Antibody (PC10) NB500-106 at 1 ug/ml overnight at 4C and detected with an anti-mouse 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/PCNA-Antibody-PC10-Immunocytochemistry-Immunofluorescence-NB500-106-img0016.jpg)
![Immunocytochemistry/Immunofluorescence: PCNA Antibody (PC10) [NB500-106] - HeLa cells were fixed and permeabilized for 10 minutes using cold (-20C) MeOH. The cells were incubated with anti-PCNA [PC10] at 5 ug/mL overnight at 4C and detected with an anti-mouse IgG 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/PCNA-Antibody-PC10-Immunocytochemistry-Immunofluorescence-NB500-106-img0010.jpg)
![Immunohistochemistry: PCNA Antibody (PC10) [NB500-106] - Development of the germinal zones in the tree shrew neocortex. Immunofluorescence for PCNA (yellow) and DAPI staining (blue) on 30 um-cryosections of E32-P1 tree shrew neocortex. The top margin of the image corresponds to the transition zone SVZ/intermediate zone. Scale bars, 50 um. VZ, ventricular zone; SVZ, subventricular zone; iSVZ, inner SVZ; oSVZ, outer SVZ. Image collected and cropped by CiteAb from the following publication (//journal.frontiersin.org/article/10.3389/fnana.2018.00029/full), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/PCNA-Antibody-PC10-Immunohistochemistry-NB500-106-img0013.jpg)
![Flow Cytometry: PCNA Antibody (PC10) [NB500-106] - An intracellular stain was performed on HepG2 cells with PCNA Antibody (PC10) NB500-106G (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 10 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to DyLight 488.](http://images.novusbio.com/fullsize/PCNA-Antibody-PC10-Flow-Cytometry-NB500-106-img0012.jpg)
![Western Blot: PCNA Antibody (PC10) [NB500-106] - HeLa cell nuclear extract was resolved by electrophoresis, transferred to nitrocellulose and probed with monoclonal anti-PCNA antibody. Proteins were visualized using a goat anti-mouse secondary conjugated to HRP and a chemiluminescence detection system.](http://images.novusbio.com/fullsize/PCNA-Antibody-PC10-Western-Blot-NB500-106-img0005.jpg)
![Western Blot: PCNA Antibody (PC10) [NB500-106] - Whole cell protein from human HeLa, A431, mouse Neuro2A and rat PC12 cells was separated on a 4-20% gel by SDS-PAGE, transferred to 0.2 um PVDF membrane and blocked in 5% non-fat milk in TBST. The membrane was probed with 1.0 ug/mL anti-Histone h3 in block buffer and detected with an anti-mouse HRP secondary antibody using chemiluminescence.](http://images.novusbio.com/fullsize/PCNA-Antibody-PC10-Western-Blot-NB500-106-img0011.jpg)
![Immunohistochemistry: PCNA Antibody (PC10) [NB500-106] - Analysis of PCNA in mouse cornea. Image courtesy of product review by Bo-Yie Chen.](http://images.novusbio.com/fullsize/PCNA-Antibody-PC10-Immunohistochemistry-NB500-106-img0001.jpg)
![Chromatin Immunoprecipitation: PCNA Antibody (PC10) [NB500-106] - Events taking place during a transient telomere dysfunction. All strains were cdc13–1, incubated for 160 min at 36°C to induce telomere uncapping, followed by 90 min at 23°C to allow telomere re-capping. Nocodazole & BrdU were added to the cultures at time 0. (A) Dynamics of ssDNA loss in sub-telomeres. (B) BrdU incorporation in sub-telomeres, minus incorporation at ‘CEN’ (e.g. a centromere-proximal locus, in this case ERG26). (C–F) Dynamics of the protein association with sub-telomeres, measured for Rap1 & major DNA synthesis factors (indicated above each graph). ChIP (%) was calculated as the fraction of immunoprecipitated sub-telomeric DNA, minus the fraction precipitated at ‘CEN’ (G) Dynamics of ssDNA loss at YER188W. (H) BrdU incorporation at YER188W, minus incorporation at ‘CEN’. (I–L) The protein association with YER188W was analyzed as in C–F. (M) ssDNA at ‘CEN’. (N) BrdU incorporation at ‘CEN’. (O–R) Association of proteins with ‘CEN’. (S) Growth of serial dilution of wild-type (first row) & cdc13–1 cells with or without additional mutations (indicated on the left of each row) at temperatures indicated above each plate. The plate shown on the right was cycled three times between 4 h at 36°C (to accumulate ssDNA) & 4 h at 21°C (to re-synthesize DNA), followed by incubation at 21°C for another two days. Image collected & cropped by CiteAb from the following publication (//academic.oup.com/nar/article-lookup/doi/10.1093/nar/gkw071), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb500-106_mouse-monoclonal-pcna-antibody-pc10-310202416154647.jpg)
![Immunocytochemistry/ Immunofluorescence: PCNA Antibody (PC10) [NB500-106] - Development of the germinal zones in the tree shrew neocortex. (A–D) Immunofluorescence for PCNA (yellow) & DAPI staining (blue) on 30 μm-cryosections of E32–P1 tree shrew neocortex. The top margin of the image corresponds to the transition zone SVZ/intermediate zone. Scale bars, 50 μm. VZ, ventricular zone; SVZ, subventricular zone; iSVZ, inner SVZ; oSVZ, outer SVZ. (E) Quantification of the VZ thickness of the E32–P1 tree shrew neocortex. (F) Quantification of the SVZ thickness of the E32–P1 tree shrew neocortex. (G) Quantification of the VZ & SVZ thickness of the E32–P1 tree shrew neocortex, expressed as percentage of the sum of VZ & SVZ. (H) Quantification of the iSVZ & oSVZ thickness of the E37 tree shrew neocortex, expressed as percentage of the sum of iSVZ & oSVZ. (E–H) Data represent mean ± SD & were obtained from two consecutive sections of two brains each. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29725291), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb500-106_mouse-monoclonal-pcna-antibody-pc10-31020241615468.jpg)
![Knockout Validated: MTH1 Antibody [NB100-109] - Western blot shows lysates of HEK293T human embryonic kidney parental cell line and MTH1 knockout (KO) HEK293T cell line. PVDF membrane was probed with 1:500 of Rabbit Anti-Human MTH1 Polyclonal Antibody (Catalog # NB100-109) followed by HRP-conjugated Anti-Rabbit IgG Secondary Antibody (Catalog #HAF008). Specific band was detected for MTH1 at approximately 18 kDa (as indicated) in the parental HEK293T cell line, but is not detectable in the knockout HEK293T cell line. This experiment was conducted under reducing conditions.](http://images.novusbio.com/fullsize/MTH1-Antibody-Knockout-Validated-NB100-109-img0010.jpg "<b>Genetic Strategies Validation. </b>Knockout Validated: MTH1 Antibody [NB100-109] - Western blot shows lysates of HEK293T human embryonic kidney parental cell line and MTH1 knockout (KO) HEK293T cell line. PVDF membrane was probed with 1:500 of Rabbit Anti-Human MTH1 Polyclonal Antibody (Catalog # NB100-109) followed by HRP-conjugated Anti-Rabbit IgG Secondary Antibody (Catalog #HAF008). Specific band was detected for MTH1 at approximately 18 kDa (as indicated) in the parental HEK293T cell line, but is not detectable in the knockout HEK293T cell line. This experiment was conducted under reducing conditions.")
![<b>Genetic Strategies Validation. </b>Simple Western: MTH1 Antibody [NB100-109] - Simple Western lane view shows a specific band for MTH1 in 0.5 mg/ml of A431 lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system.](http://images.novusbio.com/fullsize/MTH1-Antibody-Simple-Western-NB100-109-img0007.jpg)
![Western Blot: MTH1 Antibody [NB100-109] - The cells from esophageal cancer cell lines: KYSE-450, EC109 and EC9706 (d, e), liver cancer cell lines: SMMC-7721, HepG2 and ZIP177 (f, g), gastric cancer cell lines: MGC-803, HGC-27, SGC-7901 and MKN45 (h, i), as well as the corresponding normal cell lines: Het-1A (d, e), L02 (f, g) and GES-1 (h, i) were cultured and lysed. The MTH1 protein levels were determined by Western Blot. GAPDH was used as a loading control. At least three independent experiments were performed for each group. j The cells indicated above were lysed and the total mRNA was extracted. The mRNA level of MTH1 was determined by RT-PCR. GAPDH was used as a control. At least three independent experiments were performed for each group. Image collected and cropped by Citeab from the following publication (Potent and specific MTH1 inhibitors targeting gastric cancer. Cell Death Dis (2019)) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/MTH1-Antibody-Western-Blot-NB100-109-img0018.jpg)
![<b>Biological Strategies Validation. </b>Western Blot: MTH1 Antibody [NB100-109] - The antioxidant pathways are activated during EBV infection and are required for growth transformation. Freshly isolated B-lymphocytes infected with the transforming B95-8 strain of EBV were cultured for up to 2 weeks in the presence or absence of MTH1 inhibitors. Protein expression was monitored by western blots, cell proliferation and activation of the DDR were assessed by 3H-Thy incorporation and staining for I3H2AX, respectively. Representative western blots illustrating the expression of MTH1, MUTYH and OGG1 in ex vivo untreated B-cell and freshly EBV infected and SAC induced B blasts cultured for comparable times and showing similar levels of cell proliferation. Image collected and cropped by Citeab from the following publication (The Epstein-Barr virus nuclear antigen-1 upregulates the cellular antioxidant defense to enable B-cell growth transformation and immortalization. Oncogene (2020)) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/MTH1-Antibody-Western-Blot-NB100-109-img0011.jpg)
![Immunocytochemistry/Immunofluorescence: MTH1 Antibody [NB100-109] - HeLa cells were fixed for 10 minutes using 10% formalin and then permeabilized for 5 minutes using 1X PBS + 0.05% Triton-X100. The cells were incubated with anti-MTH1 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/MTH1-Antibody-Immunocytochemistry-Immunofluorescence-NB100-109-img0009.jpg)
![Western Blot: MTH1 Antibody [NB100-109] - EBNA1 promotes the upregulation of oxidative DNA damage repair pathways in EBV converted cell lines and EBV positive BLs. Densitometry quantification of the specific bands. The intensity of the specific band in EBV positive cells relative the EBV-negative parental is shown. Image collected and cropped by Citeab from the following publication (The Epstein-Barr virus nuclear antigen-1 upregulates the cellular antioxidant defense to enable B-cell growth transformation and immortalization. Oncogene (2020)) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/MTH1-Antibody-Western-Blot-NB100-109-img0012.jpg)
![Western Blot: MTH1 Antibody [NB100-109] - MTH1 antibody was tested in the labeled lanes.](http://images.novusbio.com/fullsize/MTH1-Antibody-Western-Blot-NB100-109-img0004.jpg)
![Western Blot: MTH1 Antibody [NB100-109] - Analysis of MTH1 in 1. Ntera2, 2. MCF7 cell lysate, 3. A431 cell lysate and 4. COS7 cell lysate.](http://images.novusbio.com/fullsize/MTH1-Antibody-Western-Blot-NB100-109-img0001.jpg)
![Immunocytochemistry/Immunofluorescence: MTH1 Antibody [NB100-109] - A431 cells were fixed for 10 minutes using 10% formalin and then permeabilized for 5 minutes using 1X TBS + 0.5% Triton-X100. The cells were incubated with anti-MTH1 (NB100-109) at a 1:200 dilution overnight at 4C and detected with an anti-rabbit Dylight 488 (Green) at a 1:500 dilution. Alpha tubulin was used as a co-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/MTH1-Antibody-Immunocytochemistry-Immunofluorescence-NB100-109-img0008.jpg)
![<b>Genetic Strategies Validation. </b>Knockdown Validated: MTH1 Antibody [NB100-109] - MTH1 suppression reduces the two gastric cancer cell survival. MGC-803, HGC-27 and GES-1 cells were treated by MTH1 specific siRNA 1 and #2 for 72h. Non-targeting siRNA(NT) treatment was used as control. Western Blot analysis of the protein levels of MTH1, MUTYH, OGG1, p21, ATMpS1981 and p53pS15, after the cells were treated with siRNA#2. Densitometry shows relative protein expression normalized by GAPDH. Image collected and cropped by Citeab from the following publication (Potent and specific MTH1 inhibitors targeting gastric cancer. Cell Death Dis (2019)) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/MTH1-Antibody-Knockdown-Validated-NB100-109-img0013.jpg)
![<b>Genetic Strategies Validation. </b>Knockdown Validated: MTH1 Antibody [NB100-109] - Simultaneous suppression of MTH1 and MYH was efficiently achieved using a two-vector system. Steps of cell line establishment are illustrated here. Top 15% of cells expressing GFP and RFP670 were sorted to improve the knockdown efficiency. Expression levels of MYH and MTH1 were analyzed after 96h of treatment with shRNA set2. Data were double normalized with GAPDH and NT-shRNA control samples and expressed as percentage. Image collected and cropped by Citeab from the following publication (hMYH and hMTH1 cooperate for survival in mismatch repair defective T-cell acute lymphoblastic leukemia. Oncogenesis (2016)) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/MTH1-Antibody-Knockdown-Validated-NB100-109-img0017.jpg)
![Western Blot: MTH1 Antibody - BSA Free [NB100-109] - Compound MI-743 causes intracellular 8-oxo-dG accumulation & DNA damage.a MGC-803, HGC-27 & GES-1 cells were treated with DMSO or 5 µM MI-743 for 48 h. Intracellular 8-oxo-dG was stained with Cy3-conjugated avidin. DNA was counterstained with 4,6-diamidino-2-phenylindole (DAPI). Images were acquired at ×100 magnification by a Nikon Eclipse TE 2000-S fluorescence microscope. At least three independent experiments were performed for each group. b MGC-803, HGC-27 & GES-1 cells were treated with DMSO or 10 µM MI-743 for 48 h & run in alkaline comet assay. Pictures were originally captured at ×40 magnification. H2O2 was used as positive control. c Tail moment was calculated by CometScore software. Three individual experiments were performed for each group. d–f Western blot analysis of the protein levels of MTH1, MUTYH, OGG1, p21, ATMpS1981 & p53pS15 in MGC-803, HGC-27 & GES-1 cells, treated with increasing concentrations of MI-743 (0, 1, 2, 4, 8 & 12 µM). g, h Densitometry shows relative protein expression normalized for GAPDH. Data are representative of three independent experiments. i–k Western Blot analysis of the protein levels of MTH1, MUTYH, OGG1, p21, ATMpS1981 & p53pS15 of protein lysates, isolated from MGC-803, HGC-27 & GES-1 cells, which were treated with 12 µM MI-743 for 0, 12, 24, 36 & 48 h. l, m Densitometry shows relative protein expression normalized for GAPDH. Data are presented as means ± SD. Three individual experiments were performed for each group. *P < 0.05, **P < 0.01, ***P < 0.001 as compared with the controls Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31164636), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-109_rabbit-polyclonal-mth1-antibody-310202415532071.jpg)
![Western Blot: MTH1 Antibody - BSA Free [NB100-109] - Compound MI-743 causes intracellular 8-oxo-dG accumulation & DNA damage.a MGC-803, HGC-27 & GES-1 cells were treated with DMSO or 5 µM MI-743 for 48 h. Intracellular 8-oxo-dG was stained with Cy3-conjugated avidin. DNA was counterstained with 4,6-diamidino-2-phenylindole (DAPI). Images were acquired at ×100 magnification by a Nikon Eclipse TE 2000-S fluorescence microscope. At least three independent experiments were performed for each group. b MGC-803, HGC-27 & GES-1 cells were treated with DMSO or 10 µM MI-743 for 48 h & run in alkaline comet assay. Pictures were originally captured at ×40 magnification. H2O2 was used as positive control. c Tail moment was calculated by CometScore software. Three individual experiments were performed for each group. d–f Western blot analysis of the protein levels of MTH1, MUTYH, OGG1, p21, ATMpS1981 & p53pS15 in MGC-803, HGC-27 & GES-1 cells, treated with increasing concentrations of MI-743 (0, 1, 2, 4, 8 & 12 µM). g, h Densitometry shows relative protein expression normalized for GAPDH. Data are representative of three independent experiments. i–k Western Blot analysis of the protein levels of MTH1, MUTYH, OGG1, p21, ATMpS1981 & p53pS15 of protein lysates, isolated from MGC-803, HGC-27 & GES-1 cells, which were treated with 12 µM MI-743 for 0, 12, 24, 36 & 48 h. l, m Densitometry shows relative protein expression normalized for GAPDH. Data are presented as means ± SD. Three individual experiments were performed for each group. *P < 0.05, **P < 0.01, ***P < 0.001 as compared with the controls Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31164636), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-109_rabbit-polyclonal-mth1-antibody-310202415525293.jpg)
![Western Blot: MTH1 Antibody - BSA Free [NB100-109] - Characteristic expression of MTH1 in human gastric cancer tissues & ten digestive tract cancer cell lines.a The total RNA from fresh human gastric cancer tissues was isolated by RNApure Tissue&Cell Kit. The mRNA level of MTH1 in human gastric cancer (Increased, n = 21, Decreased, n = 6 & Unchanged, n = 8) & adjacent normal tissues (Con, n = 35) was determined by RT-PCR. The protein levels of MTH1 in human gastric (GC) & adjacent normal (GN) tissue sections were determined by immuohistochemistry (IHC) staining. The integral optical densities (IOD) were analyzed by Image-Pro Plus 6.0 software. b Representative IHC pictures of GC & GN. Scale bars, 50 μm. c IODs of GC & GN. n = 10 for each group. The cells from esophageal cancer cell lines: KYSE-450, EC109 & EC9706 (d, e), liver cancer cell lines: SMMC-7721, HepG2 & ZIP177 (f, g), gastric cancer cell lines: MGC-803, HGC-27, SGC-7901 & MKN45 (h, i), as well as the corresponding normal cell lines: Het-1A (d, e), L02 (f, g) & GES-1 (h, i) were cultured & lysed. The MTH1 protein levels were determined by Western Blot. GAPDH was used as a loading control. At least three independent experiments were performed for each group. j The cells indicated above were lysed & the total mRNA was extracted. The mRNA level of MTH1 was determined by RT-PCR. GAPDH was used as a control. At least three independent experiments were performed for each group. Data are presented as means ± SD. The symbol *, ** or *** stands for P < 0.05, P < 0.01 or P < 0.001 compared with the controls or normal cell groups Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31164636), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-109_rabbit-polyclonal-mth1-antibody-310202415533819.jpg)
![Western Blot: MTH1 Antibody - BSA Free [NB100-109] - Compound MI-743 causes intracellular 8-oxo-dG accumulation & DNA damage.a MGC-803, HGC-27 & GES-1 cells were treated with DMSO or 5 µM MI-743 for 48 h. Intracellular 8-oxo-dG was stained with Cy3-conjugated avidin. DNA was counterstained with 4,6-diamidino-2-phenylindole (DAPI). Images were acquired at ×100 magnification by a Nikon Eclipse TE 2000-S fluorescence microscope. At least three independent experiments were performed for each group. b MGC-803, HGC-27 & GES-1 cells were treated with DMSO or 10 µM MI-743 for 48 h & run in alkaline comet assay. Pictures were originally captured at ×40 magnification. H2O2 was used as positive control. c Tail moment was calculated by CometScore software. Three individual experiments were performed for each group. d–f Western blot analysis of the protein levels of MTH1, MUTYH, OGG1, p21, ATMpS1981 & p53pS15 in MGC-803, HGC-27 & GES-1 cells, treated with increasing concentrations of MI-743 (0, 1, 2, 4, 8 & 12 µM). g, h Densitometry shows relative protein expression normalized for GAPDH. Data are representative of three independent experiments. i–k Western Blot analysis of the protein levels of MTH1, MUTYH, OGG1, p21, ATMpS1981 & p53pS15 of protein lysates, isolated from MGC-803, HGC-27 & GES-1 cells, which were treated with 12 µM MI-743 for 0, 12, 24, 36 & 48 h. l, m Densitometry shows relative protein expression normalized for GAPDH. Data are presented as means ± SD. Three individual experiments were performed for each group. *P < 0.05, **P < 0.01, ***P < 0.001 as compared with the controls Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31164636), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-109_rabbit-polyclonal-mth1-antibody-310202415541950.jpg)
![Western Blot: MTH1 Antibody - BSA Free [NB100-109] - Characteristic expression of MTH1 in human gastric cancer tissues & ten digestive tract cancer cell lines.a The total RNA from fresh human gastric cancer tissues was isolated by RNApure Tissue&Cell Kit. The mRNA level of MTH1 in human gastric cancer (Increased, n = 21, Decreased, n = 6 & Unchanged, n = 8) & adjacent normal tissues (Con, n = 35) was determined by RT-PCR. The protein levels of MTH1 in human gastric (GC) & adjacent normal (GN) tissue sections were determined by immuohistochemistry (IHC) staining. The integral optical densities (IOD) were analyzed by Image-Pro Plus 6.0 software. b Representative IHC pictures of GC & GN. Scale bars, 50 μm. c IODs of GC & GN. n = 10 for each group. The cells from esophageal cancer cell lines: KYSE-450, EC109 & EC9706 (d, e), liver cancer cell lines: SMMC-7721, HepG2 & ZIP177 (f, g), gastric cancer cell lines: MGC-803, HGC-27, SGC-7901 & MKN45 (h, i), as well as the corresponding normal cell lines: Het-1A (d, e), L02 (f, g) & GES-1 (h, i) were cultured & lysed. The MTH1 protein levels were determined by Western Blot. GAPDH was used as a loading control. At least three independent experiments were performed for each group. j The cells indicated above were lysed & the total mRNA was extracted. The mRNA level of MTH1 was determined by RT-PCR. GAPDH was used as a control. At least three independent experiments were performed for each group. Data are presented as means ± SD. The symbol *, ** or *** stands for P < 0.05, P < 0.01 or P < 0.001 compared with the controls or normal cell groups Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31164636), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-109_rabbit-polyclonal-mth1-antibody-310202415532076.jpg)
![Western Blot: MTH1 Antibody - BSA Free [NB100-109] - The antioxidant pathways are activated during EBV infection & are required for growth transformation. Freshly isolated B-lymphocytes infected with the transforming B95-8 strain of EBV were cultured for up to 2 weeks in the presence or absence of MTH1 inhibitors. Protein expression was monitored by western blots, cell proliferation & activation of the DDR were assessed by 3H-Thy incorporation & staining for gamma H2AX, respectively. a representative western blots illustrating the parallel increase of MTH1 & EBNA1 expression following EBV infection & mean ± SE of the intensity of the MTH1 specific band in five independent experiments. b Representative western blots illustrating the expression of MTH1, MUTYH & OGG1 in ex vivo untreated B-cell & freshly EBV infected & SAC induced B blasts cultured for comparable times & showing similar levels of cell proliferation. c Quantification of the specific bands. Relative expression is the ration between the intensity in the treated cells versus freshly harvested cells. The mean ± SE of three to four independent experiments is shown. d Inhibition of MTH1 prevents the establishment of EBV transformed lymphoblastoid cell lines. 3H-Thy incorporation was measured after culture of freshly EBV infected B-lymphocytes in the presence of the indicated amounts of MTH1 inhibitors. Depending on the condition of the cultures harvesting was done after ten to fifteen days. e Inhibition of MTH1 strongly enhances the induction of DNA damage in freshly EBV infected cells. DNA damage was detected by gamma H2AX staining. f Mean ± SE of the % gamma H2AX positive cells in three independent experiments. *P < 0.05; **P < 0.01 Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31511648), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-109_rabbit-polyclonal-mth1-antibody-31020241612671.jpg)
![Western Blot: MTH1 Antibody - BSA Free [NB100-109] - EBNA1 expression is associated with upregulation of MTH1 & oxidative damage repair pathways. The expression of MTH1, OGG1, & MUTYH was investigated by western blots & qPCR in BJAB-tTAE1 cells upon addition & withdrawal of doxycycline. a Representative western blots illustrating the correlation between the reversible down- & upregulation of MTH1 & EBNA1 in BJAB-tTAE1 cells upon addition & withdrawal of doxycycline. GAPDH was used as loading control. b Densitometry quantification of MTH1 & EBNA1 expression in BJAB-tTAE1 cells. The mean intensity of the MTH1 & EBNA1 specific bands relative to GAPDH in three independent experiments is shown in the figure. c Regression analysis of the relationship between expression levels of MTH1 & EBNA1. The data from three independent experiments were used for the plot. d Representative western blots illustrating the expression of MTH1, MUTYH, & OGG1 in BJAB-tTAE1 cells cultured for two weeks in the presence or absence of doxycycline. e Fold change is the ratio between the intensity of the specific band in cells cultured without or with doxycycline. The mean ± SD of four independent experiments is shown. f qPCR analysis of the levels of MTH1, OGG1, & MUTYH transcripts in BJAB-tTAE1 cells cultured for 2 weeks in the presence or absence of doxycycline. The mean ± SE of the fold change in six independent experiments each performed in triplicate is shown Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31511648), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-109_rabbit-polyclonal-mth1-antibody-310202415535142.jpg)
![Western Blot: MTH1 Antibody - BSA Free [NB100-109] - MTH1 suppression reduces the two gastric cancer cell survival.MGC-803, HGC-27 & GES-1 cells were treated by MTH1 specific siRNA#1 & #2 for 72 h. Non-targeting siRNA(NT) treatment was used as control. a Levels of MTH1 protein then were determined by western blot. b The colony formations were recorded after the cells were treated with MTH1 siRNA#1 & #2 for 7 days. c Western Blot analysis of the protein levels of MTH1, MUTYH, OGG1, p21, ATMpS1981 & p53pS15, after the cells were treated with siRNA#2. f–h Densitometry shows relative protein expression normalized by GAPDH. d The Alkaline comets assay was performed after the cells were transfected with MTH1 siRNA#2 for 72 h. Pictures were originally captured at ×40 magnification by fluorescence microscope. Non-targeting siRNA(NT) or H2O2 treatment was used as a negative or a positive control, respectively. e Tail moment was calculated by CometScore software. Three individual experiments were performed for each group. i Relative cell viability was determined by MTT assay, after the cells were treated with MTH1 siRNA#1 & #2 with or without MI-743 combined with 100uM H2O2. Data are presented as means ± SD. Three individual experiments were performed for each group. The symbols * & #, ** & ## or ***and ### stand for P < 0.05, P < 0.01 or P < 0.001 compared with the controls Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31164636), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-109_rabbit-polyclonal-mth1-antibody-31020241682184.jpg)
![Western Blot: MTH1 Antibody - BSA Free [NB100-109] - Characteristic expression of MTH1 in human gastric cancer tissues & ten digestive tract cancer cell lines.a The total RNA from fresh human gastric cancer tissues was isolated by RNApure Tissue&Cell Kit. The mRNA level of MTH1 in human gastric cancer (Increased, n = 21, Decreased, n = 6 & Unchanged, n = 8) & adjacent normal tissues (Con, n = 35) was determined by RT-PCR. The protein levels of MTH1 in human gastric (GC) & adjacent normal (GN) tissue sections were determined by immuohistochemistry (IHC) staining. The integral optical densities (IOD) were analyzed by Image-Pro Plus 6.0 software. b Representative IHC pictures of GC & GN. Scale bars, 50 μm. c IODs of GC & GN. n = 10 for each group. The cells from esophageal cancer cell lines: KYSE-450, EC109 & EC9706 (d, e), liver cancer cell lines: SMMC-7721, HepG2 & ZIP177 (f, g), gastric cancer cell lines: MGC-803, HGC-27, SGC-7901 & MKN45 (h, i), as well as the corresponding normal cell lines: Het-1A (d, e), L02 (f, g) & GES-1 (h, i) were cultured & lysed. The MTH1 protein levels were determined by Western Blot. GAPDH was used as a loading control. At least three independent experiments were performed for each group. j The cells indicated above were lysed & the total mRNA was extracted. The mRNA level of MTH1 was determined by RT-PCR. GAPDH was used as a control. At least three independent experiments were performed for each group. Data are presented as means ± SD. The symbol *, ** or *** stands for P < 0.05, P < 0.01 or P < 0.001 compared with the controls or normal cell groups Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31164636), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-109_rabbit-polyclonal-mth1-antibody-31020241555213.jpg)
![Western Blot: MTH1 Antibody - BSA Free [NB100-109] - Generation of MTH1/HRASV12 BEAS2B cell lines used in this study(A). MTH1 levels are elevated in nonsmall cell lung tumors relative to adjacent normal tissue. Samples are part of a tissue array obtained from US Biomax. Tissue sections were photographed at 200X. MTH1 expression is seen as brown staining. (B). Schematic showing how cell lines for this study were generated. (C). Western blotting confirming high or low levels of HRASV12 expression in MTH1-overexpressing (pBp.MTH1) & control (pBp) BEAS2B cells. Actin is shown as a loading control. Samples were harvested & lysed approximately 19 days following transduction. Quantitation of HRAS fold-changes (pBp values set to 1) among the samples is shown below the immunoblot images. Fold changes were calculated using loading-normalized signal intensities determined from three independently run blots. (D). Western blotting confirming high & low levels of HRASV12 expression in MTH1-suppressed (shMTH1) & control (shGFP) BEAS2B cells. Actin is shown as a loading control. Samples were harvested & lysed approximately 19 days following transduction. Quantitation of HRAS fold-changes (shGFP values set to 1) among the samples is shown below the immunoblot images & was calculated using loading-normalized signal intensities determined from three independently run blots. Image collected & cropped by CiteAb from the following publication (//www.oncotarget.com/lookup/doi/10.18632/oncotarget.3447), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-109_rabbit-polyclonal-mth1-antibody-310202415541967.jpg)
![Western Blot: MTH1 Antibody - BSA Free [NB100-109] - Compound MI-743 causes intracellular 8-oxo-dG accumulation & DNA damage.a MGC-803, HGC-27 & GES-1 cells were treated with DMSO or 5 µM MI-743 for 48 h. Intracellular 8-oxo-dG was stained with Cy3-conjugated avidin. DNA was counterstained with 4,6-diamidino-2-phenylindole (DAPI). Images were acquired at ×100 magnification by a Nikon Eclipse TE 2000-S fluorescence microscope. At least three independent experiments were performed for each group. b MGC-803, HGC-27 & GES-1 cells were treated with DMSO or 10 µM MI-743 for 48 h & run in alkaline comet assay. Pictures were originally captured at ×40 magnification. H2O2 was used as positive control. c Tail moment was calculated by CometScore software. Three individual experiments were performed for each group. d–f Western blot analysis of the protein levels of MTH1, MUTYH, OGG1, p21, ATMpS1981 & p53pS15 in MGC-803, HGC-27 & GES-1 cells, treated with increasing concentrations of MI-743 (0, 1, 2, 4, 8 & 12 µM). g, h Densitometry shows relative protein expression normalized for GAPDH. Data are representative of three independent experiments. i–k Western Blot analysis of the protein levels of MTH1, MUTYH, OGG1, p21, ATMpS1981 & p53pS15 of protein lysates, isolated from MGC-803, HGC-27 & GES-1 cells, which were treated with 12 µM MI-743 for 0, 12, 24, 36 & 48 h. l, m Densitometry shows relative protein expression normalized for GAPDH. Data are presented as means ± SD. Three individual experiments were performed for each group. *P < 0.05, **P < 0.01, ***P < 0.001 as compared with the controls Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31164636), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-109_rabbit-polyclonal-mth1-antibody-31020241612661.jpg)
![Western Blot: MTH1 Antibody - BSA Free [NB100-109] - Characteristic expression of MTH1 in human gastric cancer tissues & ten digestive tract cancer cell lines.a The total RNA from fresh human gastric cancer tissues was isolated by RNApure Tissue&Cell Kit. The mRNA level of MTH1 in human gastric cancer (Increased, n = 21, Decreased, n = 6 & Unchanged, n = 8) & adjacent normal tissues (Con, n = 35) was determined by RT-PCR. The protein levels of MTH1 in human gastric (GC) & adjacent normal (GN) tissue sections were determined by immuohistochemistry (IHC) staining. The integral optical densities (IOD) were analyzed by Image-Pro Plus 6.0 software. b Representative IHC pictures of GC & GN. Scale bars, 50 μm. c IODs of GC & GN. n = 10 for each group. The cells from esophageal cancer cell lines: KYSE-450, EC109 & EC9706 (d, e), liver cancer cell lines: SMMC-7721, HepG2 & ZIP177 (f, g), gastric cancer cell lines: MGC-803, HGC-27, SGC-7901 & MKN45 (h, i), as well as the corresponding normal cell lines: Het-1A (d, e), L02 (f, g) & GES-1 (h, i) were cultured & lysed. The MTH1 protein levels were determined by Western Blot. GAPDH was used as a loading control. At least three independent experiments were performed for each group. j The cells indicated above were lysed & the total mRNA was extracted. The mRNA level of MTH1 was determined by RT-PCR. GAPDH was used as a control. At least three independent experiments were performed for each group. Data are presented as means ± SD. The symbol *, ** or *** stands for P < 0.05, P < 0.01 or P < 0.001 compared with the controls or normal cell groups Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31164636), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-109_rabbit-polyclonal-mth1-antibody-310202415541912.jpg)
![Western Blot: MTH1 Antibody - BSA Free [NB100-109] - Compound MI-743 causes intracellular 8-oxo-dG accumulation & DNA damage.a MGC-803, HGC-27 & GES-1 cells were treated with DMSO or 5 µM MI-743 for 48 h. Intracellular 8-oxo-dG was stained with Cy3-conjugated avidin. DNA was counterstained with 4,6-diamidino-2-phenylindole (DAPI). Images were acquired at ×100 magnification by a Nikon Eclipse TE 2000-S fluorescence microscope. At least three independent experiments were performed for each group. b MGC-803, HGC-27 & GES-1 cells were treated with DMSO or 10 µM MI-743 for 48 h & run in alkaline comet assay. Pictures were originally captured at ×40 magnification. H2O2 was used as positive control. c Tail moment was calculated by CometScore software. Three individual experiments were performed for each group. d–f Western blot analysis of the protein levels of MTH1, MUTYH, OGG1, p21, ATMpS1981 & p53pS15 in MGC-803, HGC-27 & GES-1 cells, treated with increasing concentrations of MI-743 (0, 1, 2, 4, 8 & 12 µM). g, h Densitometry shows relative protein expression normalized for GAPDH. Data are representative of three independent experiments. i–k Western Blot analysis of the protein levels of MTH1, MUTYH, OGG1, p21, ATMpS1981 & p53pS15 of protein lysates, isolated from MGC-803, HGC-27 & GES-1 cells, which were treated with 12 µM MI-743 for 0, 12, 24, 36 & 48 h. l, m Densitometry shows relative protein expression normalized for GAPDH. Data are presented as means ± SD. Three individual experiments were performed for each group. *P < 0.05, **P < 0.01, ***P < 0.001 as compared with the controls Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31164636), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-109_rabbit-polyclonal-mth1-antibody-310202415541993.jpg)
![Western Blot: MTH1 Antibody - BSA Free [NB100-109] - Screening of MTH1 inhibitors in vitro, MD simulations & binding free energy calculation of compound MI-743 & MTH1.a The structures, IC50 values & (b) percentage of MTH1 inhibition rate of the potential inhibitors MI-743, MI-401 & negative compound MI-929. c MGC-803 cells were treated with 50 µM compounds MI-743, MI-401, (S)-crizotinib or MI-929, respectively, collected & heated for 10 min from 43 to 61 °C. The cells were lysed & the protein levels of MTH1, OGG1, MUTYH or MTH2 were determined by western Blot. At least three independent experiments were performed for each group. Data are presented as means ± SD. d Predicted binding mode of compound MI-743 in MTH1 binding pocket (PDB code: 4N1U). Compound MI-743 is shown as green stick. The residues of MTH1 associated with MI-743 are shown in white. Hydrogen bonds are shown in magenta dash lines & the corresponding distances are given in Å. The RMSD value plots of the protein (MTH1) (e) & ligand (MI-743) (f) in the mutation & wild-type complex systems after 30 ns MD simulations. Binding models of compound MI-743 in MTH1 D119A (g), D120A (h), N33A (i) & W117A (j) mutations. k MM/PBSA binding free energy, estimated with the MTH1 wild-type & mutant systems obtained from the last 5 ns stable MD trajectory. l Flow diagram for the principle of detecting MTH1 activity. Since MTH1 can convert dGTP to dGMP & pyrophosphate, & the latter of which can be hydrolyzed to inorganic pyrophosphate by inorganic pyrophosphatase, the formed inorganic pyrophosphate can react with malachite green & ammonium molybdate to produce the green associated complex, the absorbance of which can be measured at 630 nm by PerkinElmer Envision microplate reader, indicating the activity of MTH1 Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31164636), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-109_rabbit-polyclonal-mth1-antibody-3102024155377.jpg)
![Western Blot: DNA Ligase I Antibody (10H5) [NB100-119] - Various whole cell extracts (30 ug) were separated by 5% SDS-PAGE, and the membrane was blotted with DNA ligase I antibody [10H5] diluted at 1:2000. The HRP-conjugated anti-mouse IgG antibody (NBP2-19382) was used to detect the primary antibody.](http://images.novusbio.com/fullsize/DNA-Ligase-I-Antibody-10H5-Western-Blot-NB100-119-img0003.jpg "Western Blot: DNA Ligase I Antibody (10H5) [NB100-119] - Various whole cell extracts (30 ug) were separated by 5% SDS-PAGE, and the membrane was blotted with DNA ligase I antibody [10H5] diluted at 1:2000. The HRP-conjugated anti-mouse IgG antibody (NBP2-19382) was used to detect the primary antibody.")
![Immunocytochemistry/Immunofluorescence: DNA Ligase I Antibody (10H5) [NB100-119] - HeLa cells were fixed in 4% paraformaldehyde at RT for 15 min. Green: DNA ligase I stained by DNA ligase I antibody [10H5] diluted at 1:500. Red: phalloidin, a cytoskeleton marker, diluted at 1:200. Scale bar= 10 um.](http://images.novusbio.com/fullsize/DNA-Ligase-I-Antibody-10H5-Immunocytochemistry-Immunofluorescence-NB100-119-img0004.jpg)
![Immunohistochemistry-Paraffin: DNA Ligase I Antibody (10H5) [NB100-119] - Human breast carcinoma. DNA ligase I stained by DNA ligase I antibody [10H5] diluted at 1:100. Antigen Retrieval: Citrate buffer, pH 6.0, 15 min.](http://images.novusbio.com/fullsize/DNA-Ligase-I-Antibody-10H5-Immunohistochemistry-Paraffin-NB100-119-img0001.jpg)
![Western Blot: FEN-1 Antibody (4E7) [NB100-150] - Whole cell extract (30 ug) was separated by 12% SDS-PAGE, and the membrane was blotted with FEN1 antibody diluted at 1:500.](http://images.novusbio.com/fullsize/FEN-1-Antibody-4E7-Western-Blot-NB100-150-img0006.jpg "Western Blot: FEN-1 Antibody (4E7) [NB100-150] - Whole cell extract (30 ug) was separated by 12% SDS-PAGE, and the membrane was blotted with FEN1 antibody diluted at 1:500.")
![Immunocytochemistry/Immunofluorescence: FEN-1 Antibody (4E7) [NB100-150] - Analysis of paraformaldehyde-fixed MCF7, using antibody at 1:200 dilution.](http://images.novusbio.com/fullsize/FEN-1-Antibody-4E7-Immunocytochemistry-Immunofluorescence-NB100-150-img0004.jpg)
![Western Blot: NTH1 Antibody [NB100-108] - Detection of NTH1 (37 kDa) from Hela & K562 cell extracts using NB100-108 (1:500). WB data courtesy of Mark Kelly, Indiana Univ.](http://images.novusbio.com/fullsize/NTH1-Antibody-Western-Blot-NB100-108-img0005.jpg "Western Blot: NTH1 Antibody [NB100-108] - Detection of NTH1 (37 kDa) from Hela & K562 cell extracts using NB100-108 (1:500). WB data courtesy of Mark Kelly, Indiana Univ.")
![Immunocytochemistry/Immunofluorescence: NTH1 Antibody [NB100-108] - NTH1 antibody was tested in HeLa cells with FITC (green). Nuclei and alpha-tubulin were counterstained with Dapi (blue) and Dylight 550 (red).](http://images.novusbio.com/fullsize/NTH1-Antibody-Immunocytochemistry-Immunofluorescence-NB100-108-img0006.jpg)
![Immunohistochemistry-Paraffin: NTH1 Antibody [NB100-108] - IHC analysis of a formalin fixed paraffin embedded (FFPE) tissue section of human colon adenocarcinoma using NTH1 antibody at 5ug/ml concentration (1:200 dilution). The primary antibody binding to NTH1/ NTHL1 antigen was detected using HRP conjugated anti-rabbit secondary antibody with DAB reagent, and the sections were further counterstained with hematoxylin for labeling cellular nuclei. The NTH1 antibody generated an expected nuclear cytoplasmic staining of NTH1 protein in colon cancer cells as well as the cells of tumor stroma including cancer associated fibroblasts. The nuclear staining of NTH1 was very strong in a sub-set of colon cancer cells.](http://images.novusbio.com/fullsize/NTH1-Antibody-Immunohistochemistry-Paraffin-NB100-108-img0014.jpg)
![Western Blot: NTH1 Antibody [NB100-108] - Analysis of NTH1 expression in 1) HeLa, 2) A-431, 3) MCF7 whole cell lysates.](http://images.novusbio.com/fullsize/NTH1-Antibody-Western-Blot-NB100-108-img0002.jpg)
![Immunohistochemistry-Paraffin: NTH1 Antibody [NB100-108] - IHC analysis of formalin-fixed paraffin-embedded tissue section of human lymph node cancer using 5 ug/ml concentration of NTH1 antibody. The representative image shows strong nuclear and cytoplasmic positivity of NTH1 protein in the lymph node cancer cells.](http://images.novusbio.com/fullsize/NTH1-Antibody-Immunohistochemistry-Paraffin-NB100-108-img0013.jpg)
![Immunohistochemistry-Paraffin: NTH1 Antibody [NB100-108] - IHC analysis of formalin-fixed paraffin-embedded tissue section of human kidney cancer using 5 ug/ml concentration of NTH1 antibody. The renal cancer cells showed nuclear and cytoplasmic positivity for NTH1 protein, whereas, the tumor stroma was largely negative for immunostaining.](http://images.novusbio.com/fullsize/NTH1-Antibody-Immunohistochemistry-Paraffin-NB100-108-img0012.jpg)
![Immunohistochemistry-Paraffin: NTH1 Antibody [NB100-108] - IHC analysis of formalin-fixed paraffin-embedded tissue section of human rectal cancer using 5 ug/ml concentration of NTH1 antibody. The rectal cancer cells as well as the goblet cells in glandular areas showed nuclear-cytoplasmic positivity for NTH1 protein. The cells of tumor stroma did not develop immunostaining for this protein.](http://images.novusbio.com/fullsize/NTH1-Antibody-Immunohistochemistry-Paraffin-NB100-108-img0011.jpg)
![Immunohistochemistry-Paraffin: NTH1 Antibody [NB100-108] - IHC analysis of formalin-fixed paraffin-embedded tissue section of human rectal cancer using 5 ug/ml concentration of NTH1 antibody. This representative image at high resolution depicts nuclear-cytoplasmic positivity for NTH1 protein in rectal cancer cells and the goblet cells. The cells of tumor stroma did not develop any immunostaining for this protein.](http://images.novusbio.com/fullsize/NTH1-Antibody-Immunohistochemistry-Paraffin-NB100-108-img0010.jpg)
![Western Blot: APE Antibody Pack [NB100-909] - Whole cell protein from human HeLa, A431, mouse Neuro2A and rat PC12 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-APE-1 (NB100-116) in block buffer and detected with an anti-mouse HRP secondary antibody using chemiluminescence.](http://images.novusbio.com/fullsize/APE-Antibody-Pack-NB100-909-img0013.jpg "Western Blot: APE Antibody Pack [NB100-909] - Whole cell protein from human HeLa, A431, mouse Neuro2A and rat PC12 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-APE-1 (NB100-116) in block buffer and detected with an anti-mouse HRP secondary antibody using chemiluminescence.")
![Immunocytochemistry/Immunofluorescence: APE Antibody Pack [NB100-909] - HeLa cells stained with anti-APE Antibody (NB100-116, Green) detected with DyLight Fluor 488 conjugated anti-rabbit IgG secondary antibody. Nuclei are counterstained with Hoechst 33258 (Blue).](http://images.novusbio.com/fullsize/APE-Antibody-Pack-Immunocytochemistry-Immunofluorescence-NB100-909-img0014.jpg)
![Immunohistochemistry: APE Antibody Pack [NB100-909] - Immunohistochemical staining of APE1 using NB100-116. A. Nuclear staining in the luminal epithelium of normal breast ducts and lobules. B. Low, and C. high nuclear APE1 expression in invasive breast cancer. (magnification x400). Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0099528) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/APE-Antibody-Pack-Immunohistochemistry-NB100-909-img0015.jpg)
![Western Blot: APE Antibody Pack [NB100-909] - Analysis of APE1 using NB100-101 in cell lysates: 1. HeLa, 2. Ntera2, 3. A431, 4. HepG2, 5. MCF7, 6. NIH 3T3, 7. PC12, and 8. Cos 7.](http://images.novusbio.com/fullsize/APE-Antibody-Pack-NB100-909-img0011.jpg)
![Immunocytochemistry/Immunofluorescence: APE Antibody Pack [NB100-909] - Detection of APE1 using NB100-101 in HeLa cells. Image from verified customer review.](http://images.novusbio.com/fullsize/APE-Antibody-Pack-Immunocytochemistry-Immunofluorescence-NB100-909-img0012.jpg)
![Immunohistochemistry: APE1 Antibody Pack [NB100-909] - Staining of APE-ref-1 in prostate cancer, using NB100-101.](http://images.novusbio.com/fullsize/APE1-Antibody-Pack-Immunohistochemistry-NB100-909-img0005.jpg)
![Simple Western: APE Antibody Pack [NB100-909] - Lane view shows a specific band for APE1 using NB100-101 in 0.1 mg/ml of HeLa lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system.](http://images.novusbio.com/fullsize/APE-Antibody-Pack-Simple-Western-NB100-909-img0010.jpg)
![<b>Genetic Strategies Validation. </b>Knockdown Validated: APE Antibody Pack [NB100-909] - Repression of p21 by APE1 in p53-null cells and effect of ectopic p53 in this repression. Representative Western analysis of p53, APE1 (using NB100-116), p21 and alpha-Tubulin levels in the same HCT116p53null cells. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0068467) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/APE-Antibody-Pack-Knockdown-Validated-NB100-909-img0018.jpg)
![Western Blot: PARP Antibody (194C1439) - Cleaved [NB100-56599] - Analysis of cleaved PARP in staurosporine-treated Jurkat cells at various time points, antibody at 2 ug/mL. The band corresponding to cleaved PARP is only seen in the treated samples. Anti-mouse Ig HRP conjugate was used in this test.](http://images.novusbio.com/fullsize/PARP-Antibody-194C1439-Cleaved-Western-Blot-NB100-56599-img0004.jpg "<b>Biological Strategies Validation. </b>Western Blot: PARP Antibody (194C1439) - Cleaved [NB100-56599] - Analysis of cleaved PARP in staurosporine-treated Jurkat cells at various time points, antibody at 2 ug/mL. The band corresponding to cleaved PARP is only seen in the treated samples. Anti-mouse Ig HRP conjugate was used in this test.")
![<b>Biological Strategies Validation. </b>Immunocytochemistry/Immunofluorescence: PARP Antibody (194C1439) - Cleaved [NB100-56599] - A431 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-PARP Antibody (194C1439) at 5 ug/ml overnight at 4C and detected with an anti-mouse 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/PARP-Antibody-194C1439-Cleaved-Immunocytochemistry-Immunofluorescence-NB100-56599-img0005.jpg)
![Western Blot: PARP Antibody (194C1439) - Cleaved [NB100-56599] - Analysis using 293T lysates expressing PARP. Image from verified customer review.](http://images.novusbio.com/fullsize/PARP-Antibody-194C1439-Cleaved-Western-Blot-NB100-56599-img0003.jpg)
![Western Blot: PARP Antibody [NBP2-13732] - Analysis in RT-4 cells transfected with control siRNA, target specific siRNA probe #1 and #2. Remaining relative intensity is presented. Loading control: Anti-GAPDH.](http://images.novusbio.com/fullsize/PARP-Antibody-Western-Blot-NBP2-13732-img0009.jpg "<b>Genetic Strategies Validation. </b>Western Blot: PARP Antibody [NBP2-13732] - Analysis in RT-4 cells transfected with control siRNA, target specific siRNA probe #1 and #2. Remaining relative intensity is presented. Loading control: Anti-GAPDH.")
![<b>Genetic Strategies Validation. </b>Immunocytochemistry/Immunofluorescence: PARP Antibody [NBP2-13732] - Staining of human cell line HEK 293 shows localization to nucleus. Antibody staining is shown in green.](http://images.novusbio.com/fullsize/PARP-Antibody-Immunocytochemistry-Immunofluorescence-NBP2-13732-img0007.jpg)
![Immunohistochemistry-Paraffin: PARP Antibody [NBP2-13732] - Staining of human testis shows strong nuclear positivity in cells in seminiferous ducts.](http://images.novusbio.com/fullsize/PARP-Antibody-Immunohistochemistry-Paraffin-NBP2-13732-img0014.jpg)
![Immunohistochemistry-Paraffin: PARP Antibody [NBP2-13732] - Staining of human lymph node shows strong nuclear positivity in lymphoid cells.](http://images.novusbio.com/fullsize/PARP-Antibody-Immunohistochemistry-Paraffin-NBP2-13732-img0010.jpg)
![Immunohistochemistry-Paraffin: PARP Antibody [NBP2-13732] - Staining of human pancreas shows strong nuclear positivity.](http://images.novusbio.com/fullsize/PARP-Antibody-Immunohistochemistry-Paraffin-NBP2-13732-img0011.jpg)
![Immunohistochemistry-Paraffin: PARP Antibody [NBP2-13732] - Staining of human parathyroid gland shows strong nuclear positivity in glandular cells.](http://images.novusbio.com/fullsize/PARP-Antibody-Immunohistochemistry-Paraffin-NBP2-13732-img0012.jpg)
![Immunohistochemistry-Paraffin: PARP Antibody [NBP2-13732] - Staining of human placenta shows strong nuclear positivity in trophoblastic cells.](http://images.novusbio.com/fullsize/PARP-Antibody-Immunohistochemistry-Paraffin-NBP2-13732-img0013.jpg)
![Western Blot: MYH Antibody [NB600-1032] - Analysis of MYH in 20 ugs of HeLa cell lysate.](http://images.novusbio.com/fullsize/MYH-Antibody-Western-Blot-NB600-1032-img0002.jpg "Western Blot: MYH Antibody [NB600-1032] - Analysis of MYH in 20 ugs of HeLa cell lysate.")