| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB100-109SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NBP1-77080SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NBP2-13173SS | |||
| Azide and BSA Free | NBP2-80855 | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NBP1-85816-25ul | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB110-40766SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB100-177SS | |||
| Azide and BSA Free | NBP2-80923 | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NBP1-71663SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| Azide and BSA Free | NB600-1008SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB600-1475SS | |||
| Azide and BSA Free | NBP2-80640 | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NBP1-32731SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB600-336SS | |||
![Western Blot: 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>Western Blot: 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>Western Blot: 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>Western Blot: 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: NLRP3/NALP3 Antibody - BSA Free [NBP1-77080] - HMGB1 promoted the activation of canonical NLRP3 inflammasome in retinal IR injury. The intravitreal injection of HMGB1 inhibitor, GA, significantly suppressed mRNA (B) and protein (D) production of NLRP3. Data are shown as mean +/- SD. **P < 0.01 vs sham group. Image collected and cropped by CiteAb from the following publication (//www.jneuroinflammation.com/content/12/1/137) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/NLRP3-NALP3-Antibody---BSA-Free-Western-Blot-NBP1-77080-img0011.jpg "Western Blot: NLRP3/NALP3 Antibody - BSA Free [NBP1-77080] - HMGB1 promoted the activation of canonical NLRP3 inflammasome in retinal IR injury. The intravitreal injection of HMGB1 inhibitor, GA, significantly suppressed mRNA (B) and protein (D) production of NLRP3. Data are shown as mean +/- SD. **P < 0.01 vs sham group. Image collected and cropped by CiteAb from the following publication (//www.jneuroinflammation.com/content/12/1/137) licensed under a CC-BY license.")
![Immunocytochemistry/Immunofluorescence: NLRP3/NALP3 Antibody - BSA Free [NBP1-77080] - Staining of NALP3 in K562 cells with NALP3 antibody at 2 ug/mL.](http://images.novusbio.com/fullsize/NLRP3-NALP3-Antibody---BSA-Free-Immunocytochemistry-Immunofluorescence-NBP1-77080-img0010.jpg)
![Immunohistochemistry-Paraffin: NLRP3/NALP3 Antibody - BSA Free [NBP1-77080] - Analysis of NALP3 in mouse lung tissue using anti-NALP3 antibody. Image from verified customer review.](http://images.novusbio.com/fullsize/NLRP3-NALP3-Antibody---BSA-Free-Immunohistochemistry-Paraffin-NBP1-77080-img0003.jpg)
![Western Blot: NLRP3/NALP3 Antibody - BSA Free [NBP1-77080] - Analysis of NALP3 in K562 cell lysate with NALP3 antibody at 1 ug/mL (A) in the absence and (B) in the presence of blocking peptide.](http://images.novusbio.com/fullsize/NLRP3-NALP3-Antibody---BSA-Free-Western-Blot-NBP1-77080-img0009.jpg)
![<b>Biological Strategies Validation. </b>Immunocytochemistry/Immunofluorescence: NLRP3/NALP3 Antibody - BSA Free [NBP1-77080] - hADSC-Evs suppressed NLRP3 inflammasome activation in ocular surface of experimental mice under desiccating stress. Representative image of immunofluorescent staining of NLRP3 related genes in corneal and conjunctival epithelia of desiccating mice or treated with hADSC-EVs (*conjunctiva; open triangle cornea). Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32884023/) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/NLRP3-NALP3 Antibody - BSA Free-Immunocytochemistry-Immunofluorescence-NBP1-77080-img0012.jpg)
![Immunocytochemistry/ Immunofluorescence: NLRP3/NALP3 Antibody - BSA Free [NBP1-77080] - hADSC-Evs suppressed NLRP3 inflammasome activation in ocular surface of experimental mice under desiccating stress. (A) Representative image of immunofluorescent staining of NLRP3 related genes in corneal & conjunctival epithelia of desiccating mice or treated with hADSC-EVs (*conjunctiva; open triangle cornea). (B,C) qRT-PCR showed the mRNA levels of NLRP3 related genes in conjunctiva & cornea (four corneas/conjunctivas were mixed as a sample). Data was shown as mean ± SEM. *p < 0.05. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32884023), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nbp1-77080_rabbit-polyclonal-nlrp3-nalp3-antibody-31020241535675.jpg)
![Western Blot: NLRP3/NALP3 Antibody - BSA Free [NBP1-77080] - HMGB1 promoted the activation of canonical NLRP3 inflammasome in retinal IR injury. The intravitreal injection of exogenous rHMGB1 significantly promoted the mRNA & protein production of NLRP3 (a, c) & ASC (e, g) & activation of caspase-1 (i). Thus, the intravitreal injection of HMGB1 inhibitor, GA, significantly suppressed the production of NLRP3 (b, d) & ASC (f, h) & activation of caspase-1 (j). Data are shown as mean ± SD. *P < 0.05, **P < 0.01 vs sham group Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26224068), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nbp1-77080_rabbit-polyclonal-nlrp3-nalp3-antibody-310202415345338.jpg)
![Western Blot: NLRP3/NALP3 Antibody - BSA Free [NBP1-77080] - Co-immunoprecipitation assay: Figure showing interaction of NLRP3, NLRC4 & NAIP with ASC during CFT073 infection in THP-1m. Cytoplasmic extracts of THP-1m infected with or without CFT073, 6 h post stimulation were subjected to IP & WB by various antibodies (ASC, NLRP3, NLRC4, & NAIP) as described in material & methods. Cytoplasmic extract used as input was subjected to check NLRP3, ASC, NLRC4 & NAIP expression as shown in figure. ASC antibody was used to co-immunoprecipitate the complex from cytoplasmic extracts & then immunoblotted to detect NLRP3, NLRC4 & NAIP. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31551961), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nbp1-77080_rabbit-polyclonal-nlrp3-nalp3-antibody-310202415371971.jpg)
![Western Blot: NLRP3/NALP3 Antibody - BSA Free [NBP1-77080] - HMGB1 regulated the activation of NLRP3, rather than the activation of caspase-8, via NF-kappa B pathway. a, b NF-kappa B was activated in ischemic retina at the early stage after reperfusion. c, d Intraocular injection rHMGB1 or GA could promote or suppress the production of phosphor-NF-kappa B p65. e, f Intravitreal injection of NF-kappa B p65 inhibitor, JSH-23, significantly reduced the activation of NLRP3 & decreased the processing of IL-1 beta , g rather than caspase-8. However, intravitreal injection of caspase-8 inhibitor, Z-IETD-fmk, decreased the production of phosphor-NF-kappa B p65, obviously (h). Data are shown as mean ± SD. *P < 0.05, **P < 0.01 vs sham group Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26224068), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nbp1-77080_rabbit-polyclonal-nlrp3-nalp3-antibody-310202415291993.jpg)
![Western Blot: MMP-9 Antibody (4A3) [NBP2-13173] - Analysis of activated MMP9 expression in MMP9 proenzyme incubated with trypsin for various times.](http://images.novusbio.com/fullsize/MMP-9-Antibody-4A3-Western-Blot-NBP2-13173-img0002.jpg "Western Blot: MMP-9 Antibody (4A3) [NBP2-13173] - Analysis of activated MMP9 expression in MMP9 proenzyme incubated with trypsin for various times.")
![Immunohistochemistry: MMP-9 Antibody (4A3) [NBP2-13173] - MMP-9 (green) was detected in murine brain (cortex) using MMP-9-DyLight 488 (4A3) with a concentration of 1:20 in PBS for 2 hours. MMP9-Signals are overlaped with the corresponding phase contrast image. Image from verified customer review. Image using the FITC format of this antibody.](http://images.novusbio.com/fullsize/MMP-9-Antibody-4A3-Immunohistochemistry-NBP2-13173-img0006.jpg)
![Western Blot: MMP-9 Antibody (4A3) [NBP2-13173] - Identification of gelatinases by Western blot analysis. A pool of sera from 10 patients with inactive RR-MS was used. For 2-DZ, pooled sera were concentrated 10-fold and 40 ug of total proteins were applied (left panels). For Western blot analysis pooled sera were concentrated 40-fold and 160 ug of total proteins were subjected to 2-DE (right panels). 2-DE gels were cut and the corresponding nitrocellulose membranes were treated with anti-NGAL Ab (A'), anti-MMP-2 Ab (B') and Anti-MMP-9 (4A3) Ab, recognizing the 65 kD and the 82 kD activated forms (C'); Gel C show the region with isoelectric point between pH 4-5.5 and molecular mass between 85 and 55 kD, analysed by Western blot in C', respectively. Image collected and cropped by CiteAb from the following publication (null), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/MMP-9-Antibody-4A3-Western-Blot-NBP2-13173-img0011.jpg)
![Western Blot: MMP-9 Antibody (4A3) [NBP2-13173] - 1-DZ analysis and identification of gelatinases by Western blot. 1.5 ul of serum from healthy control (HC) or from a patient with inactive RR-MS were loaded on a 7.5% polyacrylamide gel copolymerized with 0.1% (w/v) gelatin (1-DZ). For Western blot analysis, 2 ul of fivefold concentrated (Vivaspin 500, MWCO 50,000; GE Healthcare) serum samples (the same as in 1-DZ) were separated on a 7.5% polyacrylamide gel without gelatin (1-DE), transferred on nitrocellulose membranes and incubated with the following primary antibodies: Anti-NGAL Antibody (5G5) at concentration of 2.0 ug/ml; Anti-MMP-9 (Ab-8) Mouse mAb (IA5) at concentration of 2.66 ug/ml; Anti-MMP-2 (Ab-4) Mouse mAb (75-7F7) at concentration of 1.0 ug/ml and Anti-MMP-9 Ab (4A3) at concentration of 2.0 ug/ml. Image collected and cropped by CiteAb from the following publication (null), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/MMP-9-Antibody-4A3-Western-Blot-NBP2-13173-img0012.jpg)
![Immunohistochemistry-Paraffin: MMP-9 Antibody (4A3) [NBP2-13173] - Analysis of a FFPE tissue section of human esophageal cancer using MMP9 antibody (clone 4A3) at 1:200. The staining was developed with HRP-labelled secondary antibody and DAB reagent followed by hematoxylin counterstaining. This antibody generated a specific extracellular and cytoplasmic staining primarily in the cancer cells while the signal was pretty weak in the tumor stroma.](http://images.novusbio.com/fullsize/MMP-9-Antibody-4A3-Immunohistochemistry-Paraffin-NBP2-13173-img0003.jpg)
![Immunohistochemistry-Paraffin: MMP-9 Antibody (4A3) [NBP2-13173] - Analysis of a FFPE section of human esophageal cancer using MMP9 antibody (clone 4A3) at 1:200. The staining was developed with HRP-labelled secondary antibody and DAB reagent followed by hematoxylin counterstaining. This antibody clone generated an extracellular and cytoplasmic staining mainly in the cancer cells while the signal was very weak in the stromal cells of the tumor.](http://images.novusbio.com/fullsize/MMP-9-Antibody-4A3-Immunohistochemistry-Paraffin-NBP2-13173-img0004.jpg)
![Western Blot: MMP-9 Antibody (4A3) [NBP2-13173] - 2-DZ analysis & identification of MMP-9 by Western blot. Left panels (A & B): 2-D zymography (2-DZ) of serum samples from healthy control (A) & from an inactive RR-MS patient not subjected to therapy (same patient as in Fig. 2; B). For 2-DZ, aliquots of 35 μl of serum were resuspended in the rehydration solution & subjected to isoelectrofocusing (IEF; 1st dimension) on IPG Dry-Strips of 13 cm in a linear pH gradient of 4–7. After IEF, IPG strips were equilibrated & then applied for the 2nd dimension in a 8.5% (w/v) polyacrylamide gel copolymerized with 0.1% (w/v) gelatin. The isoforms & charge variants of MMP-2 & MMP-9 appear as clear spots of digestion on the dark background of the gel. Right panels (A' & B') represent Western blot analysis of the same sera shown in A & B. Aliquots of 35 μl of serum samples (instead of the usual 20 μl) were subjected to 2D electrophoresis (2-DE) by using 8.5% (w/v) polyacrylamide gels without gelatin. After transfer of the proteins, the nitrocellulose membranes were incubated with an anti MMP-9 (Ab-8) Mouse mAb (IA5) at concentration of 2.66 μg/ml. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/24616914), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nbp2-13173_mouse-monoclonal-mmp-9-antibody-4a3-31020241612243.jpg)
![Western Blot: MMP-9 Antibody (4A3) [NBP2-13173] - 2-DZ analysis & identification of MMP-9 by Western blot. Left panels (A & B): 2-D zymography (2-DZ) of serum samples from healthy control (A) & from an inactive RR-MS patient not subjected to therapy (same patient as in Fig. 2; B). For 2-DZ, aliquots of 35 μl of serum were resuspended in the rehydration solution & subjected to isoelectrofocusing (IEF; 1st dimension) on IPG Dry-Strips of 13 cm in a linear pH gradient of 4–7. After IEF, IPG strips were equilibrated & then applied for the 2nd dimension in a 8.5% (w/v) polyacrylamide gel copolymerized with 0.1% (w/v) gelatin. The isoforms & charge variants of MMP-2 & MMP-9 appear as clear spots of digestion on the dark background of the gel. Right panels (A' & B') represent Western blot analysis of the same sera shown in A & B. Aliquots of 35 μl of serum samples (instead of the usual 20 μl) were subjected to 2D electrophoresis (2-DE) by using 8.5% (w/v) polyacrylamide gels without gelatin. After transfer of the proteins, the nitrocellulose membranes were incubated with an anti MMP-9 (Ab-8) Mouse mAb (IA5) at concentration of 2.66 μg/ml. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/24616914), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nbp2-13173_mouse-monoclonal-mmp-9-antibody-4a3-310202416114778.jpg)
![Western Blot: HIF-1 alpha Antibody Pack [NB100-900WB] - HIF-1 alpha induction by CoCl2 on Caki-1 cell lysate. HIF-1 alpha antibody (H1alpha67) [NB100-105]. Western blot image submitted by a verified customer review.](http://images.novusbio.com/fullsize/HIF-1-alpha-Antibody-Pack-Western-Blot-NB100-900WB-img0019.jpg "<b>Biological Strategies Validation. </b>Western Blot: HIF-1 alpha Antibody Pack [NB100-900WB] - HIF-1 alpha induction by CoCl2 on Caki-1 cell lysate. HIF-1 alpha antibody (H1alpha67) [NB100-105]. Western blot image submitted by a verified customer review.")
![<b>Biological Strategies Validation. </b>Simple Western: HIF-1 alpha Antibody Pack [NB100-900WB] - Simple Western lane view shows a specific band for HIF-1 alpha in 0.5 mg/mL of hypoxic HeLa lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system. HIF-1 alpha Antibody [NB100-449].](http://images.novusbio.com/fullsize/HIF-1-alpha-Antibody-Pack-Simple-Western-NB100-900WB-img0018.jpg)
![Simple Western: HIF-1 alpha Antibody Pack [NB100-900WB] - Image shows a specific band for HIF-1 alpha in 0.2 mg/mL of Hypoxic HeLa lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system.](http://images.novusbio.com/fullsize/HIF-1-alpha-Antibody-Pack-Simple-Western-NB100-900WB-img0022.jpg)
![<b>Genetic Strategies Validation. </b>Western Blot: HIF-1 alpha Antibody Pack [NB100-900WB] - Naive CD4 T cells from WT, VHL-deficient (Vhl KO), or HIF-1 alpha-deficient (HIF-1 alpha KO) mice were differentiated under IL-22-skewing conditions for a total of 60 h. Some cells remained at normoxia for the duration of the culture (N); others were at normoxia for 35 h and then hypoxia (1% O2) for 24 h (H). At 60 h, nuclear extracts were harvested, and HIF-1 alpha and Lamin B1 levels were analyzed by Western blot. Image from verified customer review. HIF-1 alpha Antibody (H1alpha67) [NB100-105]](http://images.novusbio.com/fullsize/HIF-1-alpha-Antibody-Pack-Knockout-Validated-NB100-900WB-img0020.jpg)
![<b>Biological Strategies Validation. </b>Western Blot: HIF-1 alpha Antibody Pack [NB100-900WB] - Normoxic pre-treatment sensitizes glioma cells to radiation after graded chronic hypoxic (GCH) exposure. The results of anchorage-independent colony forming assays are shown for U87, U87-luc, GL261 glioma cells and 0308 GSCs after 5 Gy radiation exposure under varying O2 conditions. For easier comparisons among cell types, raw values are expressed as a % of the cell type's negative (non-irradiated) control and the means & SEMs are plotted. Also shown are Western blots of nuclear HIF-1alpha at the time of irradiation. Corresponding Western blots of lamin A/C are shown as a loading control. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0111199) licensed under a CC-BY license. HIF-1 alpha Antibody [NB100-479]](http://images.novusbio.com/fullsize/HIF-1-alpha-Antibody-Pack-Western-Blot-NB100-900WB-img0015.jpg)
![<b>Genetic Strategies Validation. </b>Western Blot: HIF-1 alpha Antibody Pack [NB100-900WB] - Morphological alterations induced by DMOG are HIF-1alpha dependent. glEND.2 cells were stably transfected with shGFP, shHIF-1alpha or shHIF-2alpha. The clones were cultured under normoxic (N) or hypoxic (H, 1% O2) conditions, or treated with DMOG for 6 h. 30 ug protein of cellular protein were loaded for the detection of HIF-1alpha, and nuclear extracts (20 ug protein) were used for the detection of HIF-2alpha. Image collected and cropped by CiteAb from the following publication (//biosignaling.biomedcentral.com/articles/10.1186/1478-811X-11-80) licensed under a CC-BY license. HIF-1 alpha Antibody [NB100-449]](http://images.novusbio.com/fullsize/HIF-1-alpha-Antibody-Pack-Knockdown-Validated-NB100-900WB-img0017.jpg)
![Western Blot: HIF-1 alpha Antibody Pack [NB100-900WB] - Analysis of HIF-1 alpha in overexpression and endogenous HIF-1 alpha & HIF-2 alpha using anti-HIF-1 alpha antibody NB100-134. The data showed that HIF-1 alpha antibody did not react to HIF-2 alpha overexpression. Wester blot image submitted by a verified customer review.](http://images.novusbio.com/fullsize/HIF-1-alpha-Antibody-Pack-Western-Blot-NB100-900WB-img0021.jpg)
![<b>Biological Strategies Validation. </b>Western Blot: HIF-1 alpha Antibody Pack [NB100-900WB] - HIF-1 alpha induction on Caki-1 cell lysate using CoCl2. Western blot image submitted by a verified customer review. HIF-1 alpha Antibody [NB100-449]](http://images.novusbio.com/fullsize/HIF-1-alpha-Antibody-Pack-Western-Blot-NB100-900WB-img0016.jpg)
![Western Blot: HIF-1 alpha Antibody Pack [NB100-900WB] - Detection of HIF-1 alpha (125-130 kDa) from human placental villous explant total protein. HIF-1 alpha Antibody (HA111) [NB100-296]](http://images.novusbio.com/fullsize/HIF-1-alpha-Antibody-Pack-Western-Blot-NB100-900WB-img0023.jpg)
![<b>Biological Strategies Validation. </b>Immunocytochemistry/Immunofluorescence: ATF3 Antibody [NBP1-85816] - ATF3 antibody in indirect immunofluorescence staining of human tumor cells using a green-fluorescent secondary antibody showing nuclear localization. Nuclei stained with DAPI (blue). Image from verified customer review.](http://images.novusbio.com/fullsize/ATF3-Antibody-Immunocytochemistry-Immunofluorescence-NBP1-85816-img0028.jpg)
![Immunocytochemistry/Immunofluorescence: ATF3 Antibody [NBP1-85816] - Staining of human cell line A-431 shows localization to nucleus and nucleoli. Antibody staining is shown in green.](http://images.novusbio.com/fullsize/ATF3-Antibody-Immunocytochemistry-Immunofluorescence-NBP1-85816-img0012.jpg)
![Immunohistochemistry-Paraffin: ATF3 Antibody [NBP1-85816] - Staining of human fallopian tube shows moderate to strong nuclear positivity in a subset of glandular cells.](http://images.novusbio.com/fullsize/ATF3-Antibody-Immunohistochemistry-Paraffin-NBP1-85816-img0015.jpg)
![Immunohistochemistry-Paraffin: ATF3 Antibody [NBP1-85816] - Staining of human placenta shows strong nuclear positivity in trophoblastic cells.](http://images.novusbio.com/fullsize/ATF3-Antibody-Immunohistochemistry-Paraffin-NBP1-85816-img0016.jpg)
![Immunohistochemistry-Paraffin: ATF3 Antibody [NBP1-85816] - Staining of human urinary bladder shows moderate to strong nuclear positivity in epithelial cells.](http://images.novusbio.com/fullsize/ATF3-Antibody-Immunohistochemistry-Paraffin-NBP1-85816-img0018.jpg)
![Immunohistochemistry-Frozen: ATF3 Antibody [NBP1-85816] - Image was captured under an epi-fluorescent microscope. Alexa 488 conjugated rabbit antibody was used for the secondary antibody. Immunofluorescent signal was localized in the nucleus. Image submitted by a verified customer review.](http://images.novusbio.com/fullsize/ATF3-Antibody-Immunohistochemistry-Frozen-NBP1-85816-img0023.jpg)
![Western Blot: ATF3 Antibody [NBP1-85816] - Usp9X inhibition causes Noxa increase & ER stress in MPNST cell lines. Ultrastructural analysis shows features of paraptosis. (a,b) ST88-14 cells were transfected for 24 h with either non-targeting (NT)-siRNA or Usp9X-siRNA (a) or treated with WP1130 at the concentration of 1.25 & 2.5 µM (b). Whole cell extracts were collected prior to Western blot analysis for ATF3, Noxa & beta -actin. Numbers shows protein quantification analyzed through ImageJ. N = 3. (c–e) Ultrastructural appearance of untreated control cells using TEM. (f–h) After treatment with WP1130 at the concentration of 2.5 µM (f,g,h) T265-2c cells showed extensive cytosolic vacuolization (f, red arrows) & swelling of ER (g, red arrowheads) & mitochondria (h, red arrows). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30478285), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nbp1-85816_rabbit-polyclonal-atf3-antibody-310202415171333.jpg)
![Immunocytochemistry/ Immunofluorescence: ATF3 Antibody [NBP1-85816] - Axotomy-induced recombination in peripherally-projecting neurons. A, Validation of an ATF3-specific antibody. The Novus antibody (NBP1-85816) produces a positive signal in nuclei of axotomized sensory neurons in ATF3+/+ mice, but not ATF3cre/cre mice. Note that the Santa Cruz antibody (C-19) labels neuronal nuclei in in the latter (inset), indicating non-specific staining. B, C, Axotomy induced reporter expression in sensory (DRG), sympathetic (stellate ganglion, SG), & motoneurons 4 d after injury. D, Reporter expression in sensory axons & motoneurons one week after injury. E, Preventing CreERT2 translocation from cytoplasm to nucleus with ICI 182780 reduces recombination in ATF3+ cells (by ∼50%). F, Recombination efficiency 16 d after injury was calculated by expressing the proportion of tracer-filled somata (labeled at the time of injury) that were also reporter (tdtomato)-positive. G, Recombination efficiencies at 4 & 16 d after injury (n = 3 for each time point) for DRG & motoneurons. Images in panels A, B, E were taken from whole mounts, those in C, D, F from cryosections. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30993183), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nbp1-85816_rabbit-polyclonal-atf3-antibody-31020241613641.jpg)
![Immunohistochemistry: ATF3 Antibody [NBP1-85816] - Nociceptor deletion of Tsc2 preferentially upregulates cJun & Atf3 expression in IB4-positive neurons. A, Immunohistochemistry of L4 DRG contralateral & ipsilateral to a sciatic nerve transection (SN injury) at 3 d post-injury stained for cJun, Isl1 (all neurons), & IB4. Arrows point to cJun-positive, IB4-negative neurons, & arrowheads point to cJun, IB4 double-positive neurons in uninjured Tsc2 cKO DRG. Scale bars: 50 μm. B, Quantification of percentage of cJun-positive neurons from A. C, Immunohistochemistry of L4 DRG for Atf3, Isl1 (all neurons) & IB4. Arrows point to Atf3-positive, IB4-negative neurons & arrowheads point to Atf3, IB4 double-positive neurons in uninjured Tsc2 cKO DRG. Scale bars: 50 μm. D, Quantification of percentage of Atf3-positive neurons from C. E, Western blotting of uninjured control & Tsc2 cKO L4/L5 DRG from mice receiving daily vehicle or rapamycin treatment for 3 d. F, Quantification of protein expression from E. Log2 fold change relative to uninjured control from the same biological replicate. N.S., not significant, *p < 0.05, **p < 0.01, ***p < 0.001, ****p < 0.0001. Extended Data Figure 5-1 shows data values of mean & SEM, number of replicates, statistical tests, & values for all comparisons. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31182472), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nbp1-85816_rabbit-polyclonal-atf3-antibody-31020241613637.jpg)
![Western Blot: ATF3 Antibody [NBP1-85816] - Nociceptor deletion of Tsc2 preferentially upregulates cJun & Atf3 expression in IB4-positive neurons. A, Immunohistochemistry of L4 DRG contralateral & ipsilateral to a sciatic nerve transection (SN injury) at 3 d post-injury stained for cJun, Isl1 (all neurons), & IB4. Arrows point to cJun-positive, IB4-negative neurons, & arrowheads point to cJun, IB4 double-positive neurons in uninjured Tsc2 cKO DRG. Scale bars: 50 μm. B, Quantification of percentage of cJun-positive neurons from A. C, Immunohistochemistry of L4 DRG for Atf3, Isl1 (all neurons) & IB4. Arrows point to Atf3-positive, IB4-negative neurons & arrowheads point to Atf3, IB4 double-positive neurons in uninjured Tsc2 cKO DRG. Scale bars: 50 μm. D, Quantification of percentage of Atf3-positive neurons from C. E, Western blotting of uninjured control & Tsc2 cKO L4/L5 DRG from mice receiving daily vehicle or rapamycin treatment for 3 d. F, Quantification of protein expression from E. Log2 fold change relative to uninjured control from the same biological replicate. N.S., not significant, *p < 0.05, **p < 0.01, ***p < 0.001, ****p < 0.0001. Extended Data Figure 5-1 shows data values of mean & SEM, number of replicates, statistical tests, & values for all comparisons. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31182472), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nbp1-85816_rabbit-polyclonal-atf3-antibody-31020241612236.jpg)
![Immunocytochemistry/ Immunofluorescence: ATF3 Antibody [NBP1-85816] - Axotomy does not induce ATF3 in Schwann cells. A, Cryosections from injured DRG (inset) & distal sciatic nerve from the same mouse processed for ATF3 immunohistochemistry (Novus NBP1-85816). B, Punctate staining in the nerve proved to be non-specific fluorescence of leukocytes (note non-nuclear signal in the absence of primary antibody). C, In intact sciatic nerves, cells morphologically identical to Remak cells had at some point undergone recombination. D, Following injury, their numbers increased. E, This was attributable to their proliferation in the injured nerve (as opposed to ATF3 induction & subsequent recombination). C′, D′, Magnification of areas outlined in C & D demonstrate the spindle shaped morphology characteristic of Remak cells. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30993183), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nbp1-85816_rabbit-polyclonal-atf3-antibody-310202416121992.jpg)
![Western Blot: CD11b/c Antibody - BSA Free [NB110-40766] - Analysis of CD11b/c in Raw 264.7 whole cell lysate.](http://images.novusbio.com/fullsize/CD11b-c-Antibody---BSA-Free-Western-Blot-NB110-40766-img0002.jpg "Western Blot: CD11b/c Antibody - BSA Free [NB110-40766] - Analysis of CD11b/c in Raw 264.7 whole cell lysate.")
![Immunocytochemistry/Immunofluorescence: CD11b/c Antibody - BSA Free [NB110-40766] - CD11 antibody was tested in Raw264.7 cells with FITC (green). Nuclei were counterstained with DAPI (blue).](http://images.novusbio.com/fullsize/CD11b-c-Antibody---BSA-Free-Immunocytochemistry-Immunofluorescence-NB110-40766-img0006.jpg)
![Immunohistochemistry-Frozen: CD11b/c Antibody - BSA Free [NB110-40766] - 10 um Cryosection of murine acute brain slices stained with CD11b/c antibody (1:300 = 3.3 ug/ml) and Alexa Fluor 555 donkey anti rabbit IgG. Antibody shows specific staining, but the background is quite heavy. Image from verified customer review.](http://images.novusbio.com/fullsize/CD11b-c-Antibody---BSA-Free-Immunohistochemistry-Frozen-NB110-40766-img0009.jpg)
![Flow Cytometry: CD11b/c Antibody - BSA Free [NB110-40766] - A surface stain was performed on RAW 264.7 with NB110-40766 and a matched isotype control. 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/CD11b-c-Antibody---BSA-Free-Flow-Cytometry-NB110-40766-img0008.jpg)
![<b>Biological Strategies Validation. </b>Western Blot: CD11b/c Antibody - BSA Free [NB110-40766] - Effects of oltipraz on the expression of CD11b/c, phosphoinositide 3-kinase (PI3K), phosphorylated protein kinase B (p-Akt), and phosphorylated inhibitor of kB alpha (p-IkB alpha) in the spinal cord of the CCI-injured mice. The relative protein levels of (A) CD11b/c and (B) PI3K on the ipsilateral side of the spinal cord in the CCI-injured mice treated with oltipraz (OLT) or vehicle are represented. (C) Representative examples of blots for CD11b/c (160 kDa), PI3K (130 kDa), and GAPDH (37 kDa). Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31234342/) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/CD11b-c Antibody - BSA Free-Western Blot-NB110-40766-img0011.jpg)
![Immunocytochemistry/Immunofluorescence: CD11b/c Antibody - BSA Free [NB110-40766] - Phase contrast microscopy images of HFA and brain tumor cells and immunofluorescence images of cultured primary brain tumor cells, AA and HFA. HFA were derived from three different fetal brains. HFA from an 18-week- old fetus (passaged once) - GFAP (DAKO) merged with DAPI and CD68 (zoomed: 2.1x magnification); GFAP (green and red) was used as an astrocyte marker and CD68 (red) and CD11b (green) were used as markers for microglia. Nuclei indicated by DAPI (blue) in all images. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0112945), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/CD11b-c-Antibody---BSA-Free-Immunocytochemistry-Immunofluorescence-NB110-40766-img0010.jpg)
![Immunohistochemistry: CD11b/c Antibody - BSA Free [NB110-40766] - Staining of human bone marrow, myeloid precursors.](http://images.novusbio.com/fullsize/CD11b-c-Antibody---BSA-Free-Immunohistochemistry-NB110-40766-img0007.jpg)
![Western Blot: CD11b/c Antibody - BSA Free [NB110-40766] - Effects of oltipraz on the expression of CD11b/c, phosphoinositide 3-kinase (PI3K), phosphorylated protein kinase B (p-Akt), & phosphorylated inhibitor of kappa B alpha (p-IkB alpha ) in the spinal cord of the CCI-injured mice. The relative protein levels of (A) CD11b/c, (B) PI3K, (D) p-Akt, & (E) p-IKB alpha on the ipsilateral side of the spinal cord in the CCI-injured mice treated with oltipraz (OLT) or vehicle are represented. The sham-operated mice (SHAM) treated with vehicle were used as controls. (C) Representative examples of blots for CD11b/c (160 kDa), PI3K (130 kDa), & GAPDH (37 kDa), & (F) for p-Akt (60 kDa), Akt (60 kDa), p-IKB alpha (40 kDa) & IKB alpha (40 kDa). CD11b/c & PI3K are expressed relative to GAPDH levels whereas phosphorylated proteins are expressed relative to their corresponding total proteins. In all panels, * denotes significant differences vs. sham-operated mice treated with vehicle (p < 0.05; one-way ANOVA followed by the SNK test). Results are presented as the mean ± SEM; n = 5 samples per experimental group. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31234342), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-40766_rabbit-polyclonal-cd11b-c-antibody-310202416235533.jpg)
![Western Blot: CD11b/c Antibody - BSA Free [NB110-40766] - Effects of oltipraz on the expression of CD11b/c, PI3K, p-Akt, & p-IkB alpha in the prefrontal cortex of the CCI-injured mice. The relative protein levels of (A) CD11b/c, (B) PI3K, (D) p-Akt, & (E) p-IKB alpha in the prefrontal cortex of the CCI-injured mice treated with oltipraz (OLT) or vehicle. The sham-operated mice (SHAM) treated with vehicle were used as controls. Representative examples of blots for (C) CD11b/c (160 kDa), PI3K (130 kDa) & GAPDH (37 kDa), & for (F) p-Akt (60 kDa), Akt (60 kDa), p-IKB alpha (40 kDa) & IKB alpha (40 kDa). CD11b/c & PI3K are expressed relative to GAPDH levels whereas phosphorylated proteins are expressed relative to their corresponding total proteins. In all panels, * denotes significant differences vs. sham-operated mice treated with vehicle (p < 0.05; one-way ANOVA followed by the SNK test). Results are presented as the mean ± SEM; n = 4-–5 samples per experimental group. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31234342), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-40766_rabbit-polyclonal-cd11b-c-antibody-310202416235518.jpg)
![Western Blot: CD11b/c Antibody - BSA Free [NB110-40766] - Effects of oltipraz on the expression of CD11b/c, PI3K, p-Akt, & p-IkB alpha in the hippocampus of the CCI-injured mice. The relative protein levels of (A) CD11b/c, (B) PI3K, (D) p-Akt, & (E) p-IKB alpha in the hippocampus of the CCI-injured mice treated with oltipraz (OLT) or vehicle. The sham-operated mice (SHAM) treated with vehicle were used as controls. Representative examples of blots for (C) CD11b/c (160 kDa), PI3K (130 kDa), & GAPDH (37 kDa); & (F) for p-Akt (60 kDa), Akt (60 kDa), p-IKB alpha (40 kDa), & IKB alpha (40 kDa). CD11b/c & PI3K are expressed relative to GAPDH levels whereas phosphorylated proteins are expressed relative to their corresponding total proteins. In all panels, * denotes significant differences vs. sham-operated mice treated with vehicle (p < 0.05; one-way ANOVA followed by the SNK test). Results are presented as the mean ± SEM; n = 5 samples per experimental group. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31234342), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-40766_rabbit-polyclonal-cd11b-c-antibody-310202416235538.jpg)
![Immunocytochemistry/ Immunofluorescence: CD11b/c Antibody - BSA Free [NB110-40766] - Phase contrast microscopy images of HFA & brain tumor cells & immunofluorescence images of cultured primary brain tumor cells, AA & HFA.HFA were derived from three different foetal brains. (A) 18-week foetus (10× magnification); (B) 19-week foetus, first week in culture (10× magnification); (C) 19-week foetus, day 5 in culture (20× magnification); (D) Primary GBM after 2 trypsinisations (20x); (E) Recurrent GBM (20x); (F) Secondary GBM after 3 trypsinisations (10x); (G) OII 14 days in culture (10x); (H) AII 13 days in culture (10x); (I) Negative control for NGS merged with DAPI; (J) Negative control for secondary antibodies merged with DAPI; (K) GBM cells derived from one patient – GFAP (DAKO) merged with DAPI & CD68 (zoomed: 2.4× magnification); (L) primary brain tumor cells from one patient (male, 40 years old) (passaged three times) - GFAP (Novocastra) merged with DAPI; (K & L) GFAP (green) was used as a GBM marker & CD68 (red) was used as a marker for microglia. (M) AA from one Female, 61 years old; (passaged twice) - GFAP (Novocastra) merged with DAPI; (N) AA from one male 40 years old; (passaged once) - GFAP (Sigma) merged with DAPI & CD68 (Abcam); (M & N) GFAP (green) was used as an astrocyte marker & CD68 (red) & CD11b (green) were used as markers for microglia; (O) HFA from one 17-week- old foetus (passaged once) - GFAP (Novocastra) merged with DAPI & CD11b (Novus); (P) HFA from an 18-week- old foetus (passaged once) - GFAP (DAKO) merged with DAPI & CD68 (zoomed: 2.1× magnification); (O & P) GFAP (green & red) was used as an astrocyte marker & CD68 (red) & CD11b (green) were used as markers for microglia. Nuclei indicated by DAPI (blue) in all images. Image collected & cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0112945), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-40766_rabbit-polyclonal-cd11b-c-antibody-310202416235543.jpg)
![Western Blot: Rad51C Antibody (2H11/6) - BSA Free [NB100-177] - The expression of DNA damage-responsive proteins was measured by western blot analysis following treatment with olaparib and SAHA alone or in combination. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/25888415/) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/Rad51C-Antibody-2H11-6-BSA-Free-Western-Blot-NB100-177-img0008.jpg "<b>Biological Strategies Validation. </b>Western Blot: Rad51C Antibody (2H11/6) - BSA Free [NB100-177] - The expression of DNA damage-responsive proteins was measured by western blot analysis following treatment with olaparib and SAHA alone or in combination. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/25888415/) licensed under a CC-BY license.")
![<b>Biological Strategies Validation. </b>Flow Cytometry: Rad51C Antibody (2H11/6) [NB100-177] - Intracellular flow cytometric staining of 1 x 10^6 HeLa cells using Rad51C antibody (dark blue). Isotype control shown in orange. An antibody concentration of 1 ug/1x10^6 cells was used.](http://images.novusbio.com/fullsize/Rad51C-Antibody-2H11-6-Flow-Cytometry-NB100-177-img0006.jpg)
![Western Blot: Rad51C Antibody (2H11/6) [NB100-177] - Rad51C detected in HEK293 lysate using NB 100-177. Photo courtesy of B.T. Bennett & K. Knight, University of Massachusetts Medical School.](http://images.novusbio.com/fullsize/Rad51C-Antibody-2H11-6-Western-Blot-NB100-177-img0003.jpg)
![Western Blot: Rad51C Antibody (2H11/6) [NB100-177] - Analysis of RAD51c in 1) Hela WCE 2) HepG2 WCE 3) Cos-7 WCE 4) Hek293 WCE.](http://images.novusbio.com/fullsize/Rad51C-Antibody-2H11-6-Western-Blot-NB100-177-img0001.jpg)
![Simple Western: Rad51C Antibody (2H11/6) [NB100-177] - Lane view shows a specific band for Rad51C in 0.5 mg/ml of HepG2 lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system.](http://images.novusbio.com/fullsize/Rad51C-Antibody-2H11-6-Simple-Western-NB100-177-img0007.jpg)
![Immunocytochemistry/Immunofluorescence: CD31/PECAM-1 Antibody [NBP1-71663] - Staining of mouse glioma tissue using CD31/PECAM-1 Antibody (NBP1-71663) at a dilution of 1:2500. Image provided by Dr. Eric Woolf of Dignity Health.](http://images.novusbio.com/fullsize/CD31-PECAM-1-Antibody-Immunocytochemistry-Immunofluorescence-NBP1-71663-img0009.jpg "Immunocytochemistry/Immunofluorescence: CD31/PECAM-1 Antibody [NBP1-71663] - Staining of mouse glioma tissue using CD31/PECAM-1 Antibody (NBP1-71663) at a dilution of 1:2500. Image provided by Dr. Eric Woolf of Dignity Health.")
![Simple Western: CD31/PECAM-1 Antibody [NBP1-71663] - Image shows a specific band for CD31/PECAM 1 in 0.5 mg/mL of HUVEC lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system.](http://images.novusbio.com/fullsize/CD31-PECAM-1-Antibody-Simple-Western-NBP1-71663-img0010.jpg)
![<b>Biological Strategies Validation. </b>Immunohistochemistry: CD31/PECAM-1 Antibody [NBP1-71663] - 5-HTR1A agonist enhances neovascularization during skin wound healing (excisional punch biopsy model). CD31/PECAM-1 endothelial cell immunohistochemical staining at day 5 (A,B) and day 7 (E,F), image scale bars represented at 50 um. Results were presented as mean +/- SEM (n = 5 images per wound). Two-way ANOVA was performed and significance levels were set at *P < 0.05, **P < 0.01. Image collected and cropped by CiteAb from the following publication (//www.frontiersin.org/article/10.3389/fphar.2018.01406/full), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/CD31-PECAM-1-Antibody-Immunohistochemistry-NBP1-71663-img0012.jpg)
![Western Blot: CD31/PECAM-1 Antibody [NBP1-71663] - Snail and EndMT-related protein expression in lungs in orthotopic murine 4T1 breast cancer model. ag Expression of Snail (see Methods). Levels of CD31/PECAM-1 determined by western blot analysis in pooled (n = 6) samples in control and 4T1 breast cancer-bearing mice from the 1st to 5th week after 4T1 cancer cell inoculation (see Methods). Results presented as fold change vs control sample corresponding to healthy mice. Total protein after transfer was used as loading control Image collected and cropped by Citeab from the following publication (Nitric oxide deficiency and endothelial-mesenchymal transition of pulmonary endothelium in the progression of 4T1 metastatic breast cancer in mice. Breast Cancer Res (2018) licensed under a CC-BY license](http://images.novusbio.com/fullsize/CD31-PECAM-1-Antibody-Western-Blot-NBP1-71663-img0013.jpg)
![Immunocytochemistry/Immunofluorescence: CD31/PECAM-1 Antibody [NBP1-71663] - HUVEC cells were fixed for 10 minutes using 10% formalin and then permeabilized for 5 minutes using 1X TBS + 0.5% Triton X-100. The cells were incubated with CD31/PECAM-1 Antibody at 5 ug/mL overnight at 4C and detected with an anti-rabbit Dylight 488 (Green) at a 1:500 dilution. Alpha tubulin (DM1A) NB100-690 was used as a co-stain at a 1:1000 dilution and detected with an anti-mouse Dylight 550 (Red) at a 1:500 dilution. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 40X objective.](http://images.novusbio.com/fullsize/CD31-PECAM-1-Antibody-Immunocytochemistry-Immunofluorescence-NBP1-71663-img0011.jpg)
![Flow Cytometry: CD31/PECAM-1 Antibody [NBP1-71663] - CD31/PECAM-1 Antibody was tested in WeHi cells with Dylight 488 (green) alongside a matched isotype control (black).](http://images.novusbio.com/fullsize/CD31-PECAM-1-Antibody-Flow-Cytometry-NBP1-71663-img0005.jpg)
![Western Blot: CD31/PECAM-1 Antibody [NBP1-71663] - Detection of CD31 in HUVEC cell lysates.](http://images.novusbio.com/fullsize/CD31-PECAM-1-Antibody-Western-Blot-NBP1-71663-img0008.jpg)
![Immunohistochemistry-Paraffin: LYVE-1 Antibody [NB600-1008] - Positive staining for Lyve-1 on FFPE Mouse Liver, 20x magnification. Antibody diluted 1:800. Image from verified customer review.](http://images.novusbio.com/fullsize/LYVE-1-Antibody-Immunohistochemistry-Paraffin-NB600-1008-img0050.jpg "Immunohistochemistry-Paraffin: LYVE-1 Antibody [NB600-1008] - Positive staining for Lyve-1 on FFPE Mouse Liver, 20x magnification. Antibody diluted 1:800. Image from verified customer review.")
![Immunohistochemistry-Paraffin: LYVE-1 Antibody [NB600-1008] - Mouse kidney stained with LYVE-1 antibody. Image from verified customer review.](http://images.novusbio.com/fullsize/LYVE-1-Antibody-Immunohistochemistry-Paraffin-NB600-1008-img0047.jpg)
![Western Blot: LYVE-1 Antibody [NB600-1008] - Analysis of anti-mouse LYVE-1. Sample was loaded in 15% SDS-polyacrylamide gel under reducing conditions.](http://images.novusbio.com/fullsize/LYVE-1-Antibody-Western-Blot-NB600-1008-img0030.jpg)
![Immunohistochemistry: LYVE-1 Antibody [NB600-1008] - Zeb1-regulation of alkali-induced corneal NV in mice. c1 A representative stereoscopic image of the Zeb1-/+ and d1 Zeb1+/+ corneas and c2-d2 their whole flat-mount corneas immunostained with the endothelium marker CD31 and the lymphatic vessel marker LYVE-1. *p = 0.05; **p = 0.01. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32620870/) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/LYVE-1 Antibody-Immunohistochemistry-NB600-1008-img0057.jpg)
![Immunohistochemistry-Paraffin: LYVE-1 Antibody [NB600-1008] - Mouse liver. Antibody at 1:800. Detection by Polymer-HRP. Image from verified customer review.](http://images.novusbio.com/fullsize/LYVE-1-Antibody-Immunohistochemistry-Paraffin-NB600-1008-img0051.jpg)
![Immunohistochemistry: LYVE-1 Antibody [NB600-1008] - Hypoxia, blood vessel and proliferation staining. IHC staining in the Biopsy 23 and Biopsy 3 respectively for CA-9, EF5, CD31, Ki67 and LYVE1. 15x Magnification. Image collected and cropped by CiteAb from the following publication (//www.mdpi.com/2072-6694/4/3/821), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/LYVE-1-Antibody-Immunohistochemistry-NB600-1008-img0052.jpg)
![Immunohistochemistry: LYVE-1 Antibody [NB600-1008] - Zeb1-regulation of alkali-induced corneal NV in mice.a Reduction of Zeb1 mRNA in the heterozygous Zeb−/+ corneas compared to the homozygous Zeb1+/+ corneas. b Significant NV score & vessel size reduction in the Zeb1−/+ corneas as compared to their Zeb1+/+ siblings. c1 A representative stereoscopic image of the Zeb1−/+ & d1 Zeb1+/+ corneas & c2–d2 their whole flat-mount corneas immunostained with the endothelium marker CD31 & the lymphatic vessel marker LYVE-1. *p ≤ 0.05; **p ≤ 0.01. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32620870), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-1008_rabbit-polyclonal-lyve-1-antibody-31020241535663.jpg)
![Immunohistochemistry: LYVE-1 Antibody [NB600-1008] - Zeb1-regulation of alkali-induced corneal NV in mice.a Reduction of Zeb1 mRNA in the heterozygous Zeb−/+ corneas compared to the homozygous Zeb1+/+ corneas. b Significant NV score & vessel size reduction in the Zeb1−/+ corneas as compared to their Zeb1+/+ siblings. c1 A representative stereoscopic image of the Zeb1−/+ & d1 Zeb1+/+ corneas & c2–d2 their whole flat-mount corneas immunostained with the endothelium marker CD31 & the lymphatic vessel marker LYVE-1. *p ≤ 0.05; **p ≤ 0.01. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32620870), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-1008_rabbit-polyclonal-lyve-1-antibody-310202415175280.jpg)
![Immunocytochemistry/Immunofluorescence: CD31/PECAM-1 Antibody (MEC13.3) [NB600-1475] - Mouse MS1 cells were fixed in 4% paraformaldehyde for 10 minutes and permeabilized in 0.05% Triton X-100 in PBS for 5 minutes. The cells were incubated with CD31/PECAM-1 Antibody [MEC13.3] (NB600-1475) at 1ug/ml overnight at 4C and detected with an anti-rat 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/CD31-PECAM-1-Antibody-MEC13-3-Immunocytochemistry-Immunofluorescence-NB600-1475-img0019.jpg "Immunocytochemistry/Immunofluorescence: CD31/PECAM-1 Antibody (MEC13.3) [NB600-1475] - Mouse MS1 cells were fixed in 4% paraformaldehyde for 10 minutes and permeabilized in 0.05% Triton X-100 in PBS for 5 minutes. The cells were incubated with CD31/PECAM-1 Antibody [MEC13.3] (NB600-1475) at 1ug/ml overnight at 4C and detected with an anti-rat DyLight 488 (Green) at a 1:1000 dilution for 60 minutes. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 100X objective and digitally deconvolved.")
![Immunohistochemistry-Frozen: CD31/PECAM-1 Antibody (MEC13.3) [NB600-1475] - 4T1 tumor sections were stained for CD31 (green) and CD105 (red).](http://images.novusbio.com/fullsize/CD31-PECAM-1-Antibody-MEC13-3-Immunohistochemistry-Frozen-NB600-1475-img0006.jpg)
![Flow (Cell Surface): CD31/PECAM-1 Antibody (MEC13.3) [NB600-1475] - A surface stain was performed on WEHI-3 Cells with CD31/PECAM-1 Antibody (MEC13.3) (NB600-1475, blue) and a matched isotype control (orange). Cells were incubated in an antibody dilution of 2.5 ug/mL for 20 minutes at room temperature, followed by rat F(ab)2 IgG (H+L) APC-conjugated secondary antibody (F0113, R&D Systems).](http://images.novusbio.com/fullsize/CD31-PECAM-1-Antibody-MEC13-3-Flow-Cell-Surface-NB600-1475-img0009.jpg)
![Flow Cytometry: CD31/PECAM-1 Antibody (MEC13.3) [NB600-1475] - C57BL/6 mouse splenocytes stained with purified CD31/PECAM-1 Antibody (MEC13.3), followed by anti-rat IgG FITC](http://images.novusbio.com/fullsize/CD31-PECAM-1-Antibody-MEC13-3-Flow-Cytometry-NB600-1475-img0010.jpg)
![Immunocytochemistry/Immunofluorescence: CD31/PECAM-1 Antibody (MEC13.3) [NB600-1475] - Mouse MS1 cells were fixed in 4% paraformaldehyde for 10 minutes and permeabilized in 0.05% Triton X-100 in PBS for 5 minutes. The cells were incubated with CD31/PECAM-1 Antibody [MEC13.3] conjugated to DyLight 488 (NB600-1475G) at 5 ug/ml for 1 hour at room temperature. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 100X objective and digitally deconvolved.](http://images.novusbio.com/fullsize/CD31-PECAM-1-Antibody-MEC13-3-Immunocytochemistry-Immunofluorescence-NB600-1475-img0017.jpg)
![Immunocytochemistry/Immunofluorescence: CD31/PECAM-1 Antibody (MEC13.3) [NB600-1475] - MS1 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 at 5.0 ug/ml overnight at 4C and detected with an anti-mouse Dylight 488 (Green) at a 1:500 dilution. Actin was detected with Phalloidin 568 (Red) at a 1:200 dilution. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 40X objective.](http://images.novusbio.com/fullsize/CD31-PECAM-1-Antibody-MEC13-3-Immunocytochemistry-Immunofluorescence-NB600-1475-img0007.jpg)
![Immunocytochemistry/Immunofluorescence: CD31/PECAM-1 Antibody (MEC13.3) [NB600-1475] - was tested in Wehi-3 cells with Dylight 488 (green). Nuclei and beta-tubulin were counterstained with DAPI (blue) and Dylight 550 (red).](http://images.novusbio.com/fullsize/CD31-PECAM-1-Antibody-MEC13-3-Immunocytochemistry-Immunofluorescence-NB600-1475-img0011.jpg)
![Immunohistochemistry-Frozen: CD31/PECAM-1 Antibody (MEC13.3) [NB600-1475] - JAK3 colocalized with endothelial cells labeled with CD31. Image collected and cropped by CiteAb from the following publication (//journal.frontiersin.org/article/10.3389/fneur.2017.00363/full), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/CD31-PECAM-1-Antibody-MEC13-3-Immunohistochemistry-Paraffin-NB600-1475-img0015.jpg)
![Flow Cytometry: CD31/PECAM-1 Antibody (MEC13.3) [NB600-1475] - A surface stain was performed on MS1 cells with CD31/PECAM-1 [MEC13.3] Antibody NB600-1475R (blue) and a matched isotype control (orange). Cells were incubated in an antibody dilution of 2.5 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to DyLight 550.](http://images.novusbio.com/fullsize/CD31-PECAM-1-Antibody-MEC13-3-Flow-Cytometry-NB600-1475-img0022.jpg)
![Immunocytochemistry/Immunofluorescence: CD31/PECAM-1 Antibody (MEC13.3) [NB600-1475] - Mouse MS1 cells were fixed in 4% paraformaldehyde for 10 minutes and permeabilized in 0.05% Triton X-100 in PBS for 5 minutes. The cells were incubated with CD31/PECAM-1 Antibody [MEC13.3] conjugated to Alexa Fluor 647 (NB600-1475AF647) at 5 ug/ml for 1 hour at room temperature. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 100X objective and digitally deconvolved.](http://images.novusbio.com/fullsize/CD31-PECAM-1-Antibody-MEC13-3-Immunocytochemistry-Immunofluorescence-NB600-1475-img0016.jpg)
![Immunocytochemistry/Immunofluorescence: CD31/PECAM-1 Antibody (MEC13.3) [NB600-1475] - Mouse MS1 cells were fixed in 4% paraformaldehyde for 10 minutes and permeabilized in 0.05% Triton X-100 in PBS for 5 minutes. The cells were incubated with CD31/PECAM-1 Antibody [MEC13.3] conjugated to DyLight 550 (NB600-1475R) at 5 ug/ml for 1 hour at room temperature. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 100X objective and digitally deconvolved.](http://images.novusbio.com/fullsize/CD31-PECAM-1-Antibody-MEC13-3-Immunocytochemistry-Immunofluorescence-NB600-1475-img0018.jpg)
![Immunohistochemistry-Frozen: CD31/PECAM-1 Antibody (MEC13.3) [NB600-1475] - Staining of mouse CD31 in non-small cell lung cancer tumor sections from a human NSCLC tumor-bearing mouse. This image was submitted via customer Review.](http://images.novusbio.com/fullsize/CD31-PECAM-1-Antibody-MEC13-3-Immunohistochemistry-Frozen-NB600-1475-img0012.jpg)
![Flow (Cell Surface): CD31/PECAM-1 Antibody (MEC13.3) [NB600-1475] - A surface stain was performed on WEHI-3 Cells with CD31 (MEC13.3) antibody NB600-1475 (blue) and a matched isotype control (orange). Cells were incubated in an antibody dilution of 2.5 ug/mL for 20 minutes at room temperature, followed by rat F(ab)2 IgG (H+L) APC-conjugated secondary antibody (F0113, R&D Systems).](http://images.novusbio.com/fullsize/CD31-PECAM-1-Antibody-MEC13-3-Flow-Cell-Surface-NB600-1475-img0013.jpg)
![Flow Cytometry: CD31/PECAM-1 Antibody (MEC13.3) [NB600-1475] - A surface stain was performed on MS-1 cells with CD31/PECAM-1 Antibody (MEC13.3) (NB600-1475AF647, blue) and a matched isotype control (orange). Cells were incubated in an antibody dilution of 5 ug/mL for 20 minutes at room temperature. Both antibodies were conjugated to Alexa Fluor 647.](http://images.novusbio.com/fullsize/CD31-PECAM-1-Antibody-MEC13-3-Flow-Cytometry-NB600-1475-img0014.jpg)
![Flow Cytometry: CD31/PECAM-1 Antibody (MEC13.3) [NB600-1475] - A surface stain was performed on MS1 cells with CD31/PECAM-1 [MEC13.3] Antibody NB600-1475DL594 (blue) and a matched isotype control (orange). Cells were incubated in an antibody dilution of 2.5 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to DyLight 594.](http://images.novusbio.com/fullsize/CD31-PECAM-1-Antibody-MEC13-3-Flow-Cytometry-NB600-1475-img0020.jpg)
![Flow Cytometry: CD31/PECAM-1 Antibody (MEC13.3) [NB600-1475] - A surface stain was performed on MS1 cells with CD31/PECAM-1 [MEC13.3] Antibody NB600-1475G (blue) and a matched isotype control (orange). Cells were incubated in an antibody dilution of 5 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to DyLight 488.](http://images.novusbio.com/fullsize/CD31-PECAM-1-Antibody-MEC13-3-Flow-Cytometry-NB600-1475-img0021.jpg)
![Immunocytochemistry/ Immunofluorescence: CD31/PECAM-1 Antibody (MEC13.3) - BSA Free [NB600-1475] - (A) Representative Western blots depicting phosphorylated JAK3 (pJAK3), total JAK3, & corresponding beta -actin levels in the ipsilateral (CXI) versus the contralateral (CXC) cortex at 24 h in sham & mice subjected to permanent middle cerebral artery occlusion (pMCAO). (B,C) Quantified pJAK3 & JAK3 values normalized to beta -actin in the cortex of sham & mice subjected to stroke. Both pJAK3 & JAK3 are significantly increased in the ipsilateral cortex of stroked animals (*P < 0.05 & **P < 0.01 with respect to sham ipsilateral/contralateral & stroke contralateral; sham, n = 5; stroke, n = 13). Data were analyzed using a two-way ANOVA (ipsilateral/contralateral or sham/stroke) with Bonferroni post-test. (D) Diagram showing peri-infarct brain region from which images were taken (n = 3). Scale bar is 10 µm, & magnification is 60×. (E) JAK3 colocalized with microglia/macrophages labeled with Iba-1. (F) JAK3 colocalized with neurons labeled with NeuN. (G) JAK3 colocalized with endothelial cells labeled with CD31. (H) JAK3 is not colocalized with astrocytes labeled with GFAP. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28790974), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-1475_rat-monoclonal-cd31-pecam-1-antibody-mec13-3-310202416171428.jpg)
![Western Blot: Arginase 1/ARG1/liver Arginase Antibody [NBP1-32731] - Non-transfected (-) and transfected (+) HepG2 whole cell extracts (30 ug) were separated by 10% SDS-PAGE, and the membrane was blotted with Arginase 1 antibody.](http://images.novusbio.com/fullsize/Arginase-1-ARG1-liver-Arginase-Antibody-Western-Blot-NBP1-32731-img0022.jpg "<b>Genetic Strategies Validation. </b>Western Blot: Arginase 1/ARG1/liver Arginase Antibody [NBP1-32731] - Non-transfected (-) and transfected (+) HepG2 whole cell extracts (30 ug) were separated by 10% SDS-PAGE, and the membrane was blotted with Arginase 1 antibody.")
![<b>Genetic Strategies Validation. </b>Immunohistochemistry: Arginase 1/ARG1/liver Arginase Antibody [NBP1-32731] - TRP53-regulated EndMT modulates the M1 and M2 populations of increased TAMs after radiotherapy. Immunofluorescence detection of F4/80, CD31, and Arg1, in KP tumours from WT and EC-p53KO mice, with or without irradiation (23 days after irradiation). Image collected and cropped by Citeab from the following publication (Tumour-vasculature development via endothelial-to-mesenchymal transition after radiotherapy controls CD44v6+ cancer cell and macrophage polarization. Nat Commun (2018) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/Arginase-1-ARG1-liver-Arginase-Antibody-Immunohistochemistry-NBP1-32731-img0033.jpg)
![Simple Western: Arginase 1/ARG1/liver Arginase Antibody [NBP1-32731] - Simple Western lane view shows a specific band for ARG1 in human and mouse Liver lysate using ARG1 antibody (NBP1-32731) at 25 ug/ml. This experiment was performed under reducing conditions using the 12-230 kDa separation system.](http://images.novusbio.com/fullsize/Arginase-1-ARG1-liver-Arginase-Antibody-Simple-Western-NBP1-32731-img0029.jpg)
![Flow Cytometry: Arginase 1/ARG1/liver Arginase Antibody [NBP1-32731] - Effects of berberine on the M2 population of macrophages. Representative dot plot of M2 subpopulations in control group and the rats injected with ISO 3 and 7 days later. M2 cells were labelled with F4/80 and Arg1. Image collected and cropped by Citeab from the following publication (Protective role of berberine in isoprenaline-induced cardiac fibrosis in rats. BMC Cardiovasc Disord (2019) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/Arginase-1-ARG1-liver-Arginase-Antibody-Flow-Cytometry-NBP1-32731-img0032.jpg)
![Western Blot: Arginase 1/ARG1/liver Arginase Antibody [NBP1-32731] - Arginase 1 antibody detects Arginase 1 protein. Various whole cell extracts (30ug) were separated by 12% SDS-PAGE, and the membrane was blotted with Arginase 1 antibody diluted at 1:1000.](http://images.novusbio.com/fullsize/Arginase-1-ARG1-liver-Arginase-Antibody-Western-Blot-NBP1-32731-img0014.jpg)
![Immunoprecipitation: Arginase 1/ARG1/liver Arginase Antibody [NBP1-32731] - Analysis was performed using Arginase 1 antibody EasyBlot anti-Rabbit IgG was used as a secondary reagent. Arginase 1 protein from HepG2 whole cell extracts using 5 ug of Arginase 1 antibody.](http://images.novusbio.com/fullsize/Arginase-1-ARG1-liver-Arginase-Antibody-Immunoprecipitation-NBP1-32731-img0015.jpg)
![Western Blot: Arginase 1/ARG1/liver Arginase Antibody [NBP1-32731] - Rat tissue extract (50 ug) was separated by 12% SDS-PAGE, and the membrane was blotted with Arginase 1 antibody diluted at 1:10000.](http://images.novusbio.com/fullsize/Arginase-1-ARG1-liver-Arginase-Antibody-Western-Blot-NBP1-32731-img0020.jpg)
![Immunocytochemistry/Immunofluorescence: Arginase 1/ARG1/liver Arginase Antibody [NBP1-32731] - An intracellular stain was performed on HepG2 cells with Arginase 1/ARG1/liver Arginase Antibody NBP1-32731AF647 (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 2.5 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to Alexa Fluor 647.](http://images.novusbio.com/fullsize/Arginase-1-ARG1-liver-Arginase-Antibody-Immunocytochemistry-Immunofluorescence-NBP1-32731-img0034.jpg)
![Western Blot: Arginase 1/ARG1/liver Arginase Antibody [NBP1-32731] - Mouse tissue extract (50 ug) was separated by 12% SDS-PAGE, and the membrane was blotted with Arginase 1 antibody diluted at 1:10000.](http://images.novusbio.com/fullsize/Arginase-1-ARG1-liver-Arginase-Antibody-Western-Blot-NBP1-32731-img0018.jpg)
![Immunocytochemistry/Immunofluorescence: Arginase 1/ARG1/liver Arginase Antibody [NBP1-32731] - Paraformaldehyde-fixed HeLa.](http://images.novusbio.com/fullsize/Arginase-1-ARG1-liver-Arginase-Antibody-Immunocytochemistry-Immunofluorescence-NBP1-32731-img0009.jpg)
![Immunocytochemistry/Immunofluorescence: Arginase 1/ARG1/liver Arginase Antibody [NBP1-32731] - HepG2 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-ARG1 at 10 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/Arginase-1-ARG1-liver-Arginase-Antibody-Immunocytochemistry-Immunofluorescence-NBP1-32731-img0027.jpg)
![Immunohistochemistry-Paraffin: Arginase 1/ARG1/liver Arginase Antibody [NBP1-32731] - Cal27 xenograft, using arginase I antibody at 1:500 dilution.](http://images.novusbio.com/fullsize/Arginase-1-ARG1-liver-Arginase-Antibody-Immunohistochemistry-Paraffin-NBP1-32731-img0010.jpg)
![Immunohistochemistry-Paraffin: Arginase 1/ARG1/liver Arginase Antibody [NBP1-32731] - Tissue section of the mouse liver using 1:200 dilution of ARG1 antibody (NBP1-32731). The signal was developed using HRP-DAB method which followed counterstaining of the cells with hematoxylin.](http://images.novusbio.com/fullsize/Arginase-1-ARG1-liver-Arginase-Antibody-Immunohistochemistry-Paraffin-NBP1-32731-img0026.jpg)
![Immunohistochemistry-Paraffin: Arginase 1/ARG1/liver Arginase Antibody [NBP1-32731] - Hepatocellular carcinoma stained with Arginase1 1:100, pH9 antigen retrieval. Image from verified customer review.](http://images.novusbio.com/fullsize/Arginase-1-ARG1-liver-Arginase-Antibody-Immunohistochemistry-Paraffin-NBP1-32731-img0028.jpg)
![Flow Cytometry: Arginase 1/ARG1/liver Arginase Antibody [NBP1-32731] - An intracellular stain was performed on HepG2 with NBP1-32731 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 5 ug/mL for 30 minutes at room temperature, followed by Rabbit IgG (H+L) Cross-Adsorbed Secondary Antibody.](http://images.novusbio.com/fullsize/Arginase-1-ARG1-liver-Arginase-Antibody-Flow-Cytometry-NBP1-32731-img0025.jpg)
![Flow Cytometry: Arginase 1/ARG1/liver Arginase Antibody [NBP1-32731] - An intracellular stain was performed on RH30 cells with Arginase 1 Antibody NBP1-32731 (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 5.0 ug/mL for 30 minutes at room temperature, followed by Rabbit IgG (H+L) Cross-Adsorbed Secondary Antibody.](http://images.novusbio.com/fullsize/Arginase-1-ARG1-liver-Arginase-Antibody-Flow-Cytometry-NBP1-32731-img0030.jpg)
![Western Blot: Arginase 1/ARG1/liver Arginase Antibody [NBP1-32731] - Western blot analysis and gel protein densitometry were used for quantification of MARCH1 (NBP1-59758) and Arginase 1 (NBP1-32731) proteins on transduced macrophage D: The gel image indicates the blot results 48 and 72 hr after transduction, compared with the non-transduced cells. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35656075/) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/nbp1-32731_rabbit-polyclonal-arginase-1-arg1-liver-arginase-antibody-862023835350.jpg)
![Immunocytochemistry/ Immunofluorescence: Arginase 1/ARG1/liver Arginase Antibody - BSA Free [NBP1-32731] - Validation of the LCM/MS data from cellular protrusions using microscopy. Immunofluorescence (IF) of proteins identified by LCM/MS (A–D) “expected” or (E–H) “not expected” to be within protrusions based on their known functions/localizations. (A) Cd47 & (B) Anxa2 are found in both hCAD/dCAD protrusions. (C) Tenm2 is found within hCAD protrusions & (D) Cobl in GCs. Interestingly, (E) Grk5 was observed in hCAD protrusions; (F) Hist1h3b protein in hCAD protrusions & GCs (G) Hspa1b in dCAD protrusions & TNTs & (H) Arg1 in dCAD protrusions, GCs, & TNTs. White arrows/arrowheads show punctates within dCAD/hCAD protrusions & GCs or within TNTs, respectively. Scale bars = 10 μm. IF of all 8 proteins corroborate the LCM/MS protein identification for each subtypes of protrusions. (I) 1198 unique proteins were identified by LCM/MS to be in protrusions & 169 were found to be exclusive to protrusions. 904 of the 1198 proteins found in protrusions & 87 out of 169 exclusive proteins had images in the HPA Subcell database. IF images for the proteins identified by LCM/MS in protrusions, present in the HPA Subcell database, were observed & catalogued as being observed or not in protrusions (Figure S2). On average 4.7% of proteins are found in protrusions in the HPA database, 13.6% are found in our LCM isolated protrusions & 23% were found in the “exclusive” LCM protrusions. The fold enrichment increases by 2.9% or 4.8% when we looked at proteins identified by LCM/MS in protrusions or exclusive to protrusions, respectively. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30866487), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nbp1-32731_rabbit-polyclonal-arginase-1-arg1-liver-arginase-antibody-310202416165649.jpg)
![Immunocytochemistry/Immunofluorescence: c-Myc Antibody [NB600-336] - Staining of K-562, U266, Daudi and normal T cells with c-Myc antibody. ICC/IF image submitted by a verified customer review.](http://images.novusbio.com/fullsize/c-Myc-Antibody-Immunocytochemistry-Immunofluorescence-NB600-336-img0010.jpg "Immunocytochemistry/Immunofluorescence: c-Myc Antibody [NB600-336] - Staining of K-562, U266, Daudi and normal T cells with c-Myc antibody. ICC/IF image submitted by a verified customer review.")
![Western Blot: c-Myc Antibody [NB600-336] - Detection of c-Myc in HtrA2-Myc Transfectant lysates .](http://images.novusbio.com/fullsize/c-Myc-Antibody-Western-Blot-NB600-336-img0012.jpg)
![Western Blot: c-Myc Antibody [NB600-336] - Analysis of c-Myc on Jurkat whole cell extract using NB600-336.](http://images.novusbio.com/fullsize/c-Myc-Antibody-Western-Blot-NB600-336-img0004.jpg)
![Western Blot: c-Myc Antibody [NB600-336] - Lane 1: control HEK293 cell lysate. Lane 2: CMYC over-expression in HEK293 cell lysate. WB image submitted by a verified customer review.](http://images.novusbio.com/fullsize/c-Myc-Antibody-Western-Blot-NB600-336-img0014.jpg)
![Immunohistochemistry: c-Myc Antibody [NB600-336] - Analysis of c-Myc in mouse prostate using DAB with hematoxylin counterstain.](http://images.novusbio.com/fullsize/c-Myc-Antibody-Immunohistochemistry-NB600-336-img0002.jpg)
![Western Blot: c-Myc Antibody [NB600-336] - c-Myc in MOLT-4 cells. WB image submitted by a verified customer review.](http://images.novusbio.com/fullsize/c-Myc-Antibody-Western-Blot-NB600-336-img0006.jpg)
![Western Blot: c-Myc Antibody [NB600-336] - Analysis of whole cell lysate (WCL) of Jurkat cells using anti-cMyc antibody (NB600-336) at 1:1000 dilution. HRP conjugated goat anti-rabbit IgG (H+L) cross adsorbed secondary antibody was used with ECL substrate for the detection of c-Myc antibody bound to the blotted protein. This c-Myc antibody detected the c-Myc specific band at its expected position (48-50kDa). The signal below 10 kDa in this blot is potentially the degraded protein and we have not characterized this band.](http://images.novusbio.com/fullsize/c-Myc-Antibody-Western-Blot-NB600-336-img0013.jpg)
![Western Blot: c-Myc Antibody [NB600-336] - Analysis using the HRP conjugate of NB600-336. Detection of c-Myc in NIH/3T3 cell lysates (30ug and 45ug per lane) using anti-c-Myc antibody. WB image submitted by a verified customer review.](http://images.novusbio.com/fullsize/c-Myc-Antibody-Western-Blot-NB600-336-img0009.jpg)
![Immunocytochemistry/Immunofluorescence: c-Myc Antibody [NB600-336] - Detection of c-myc Tagged Plakoglobin by Immunofluorescence. Samples: Human microvascular endothelial cells expressing c-myc tagged plakoglobin following transient transfection.](http://images.novusbio.com/fullsize/c-Myc-Antibody-Immunocytochemistry-Immunofluorescence-NB600-336-img0005.jpg)
![Simple Western: c-Myc Antibody [NB600-336] - Lane view shows a specific band for c-Myc in 0.05 mg/ml of Jurkat lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system.](http://images.novusbio.com/fullsize/c-Myc-Antibody-Simple-Western-NB600-336-img0007.jpg)