Western blot, also called an immunoblot, is an analytical assay commonly used to determine the presence of a particular protein and quantify it. The process uses polyacrylamide gel electrophoresis (PAGE) to separate proteins from a heterogenous lysate based on their molecular weight or 3D structure. The separated proteins are then transferred to a PVDF or nitrocellulose membrane, where the protein(s) of interest can be detected using highly specific antibodies. The detection can then be visualized using chromogenic, fluorescent, or chemiluminescent reporters. Since its initial discovery in the late 1970’s, this sensitive visual assay has become an invaluable tool for molecular biology and proteomics researchers.
Novus offers a range of support options for western blot when you buy a product to help you with your western blot experiment including:
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NBP2-24875SS | |||
| Azide and BSA Free | NBP2-33263 | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| Carrier Free | AF-293-SP | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| Carrier Free | AF796-SP | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| Azide and BSA Free | NBP2-24905 | |||
| Azide and BSA Free | NBP2-24905SS | |||
| BSA Free | NBP2-24906SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB110-40763SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| Azide and BSA Free | NBP2-27409 | |||
| BSA Free | NB100-56704SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| Carrier Free | AF3158-SP | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB100-2288SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB300-318SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB100-56116SS | |||
![Flow Cytometry: TLR3 Antibody (40C1285.6) [NBP2-24875] - Expression of TLR3 protein on epithelial cells. HNEC (A), Detroit-562 (B) and FaDu (C) were stained intracellularly with FITC-Abs against TLR3 (open histograms) or appropriate isotype control (shaded histograms) and analyzed by flow cytometry. Representative pictures from one out of three independent experiments are shown. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0098239), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/TLR3-Antibody-40C1285-6-Flow-Cytometry-NBP2-24875-img0014.jpg "Flow Cytometry: TLR3 Antibody (40C1285.6) [NBP2-24875] - Expression of TLR3 protein on epithelial cells. HNEC (A), Detroit-562 (B) and FaDu (C) were stained intracellularly with FITC-Abs against TLR3 (open histograms) or appropriate isotype control (shaded histograms) and analyzed by flow cytometry. Representative pictures from one out of three independent experiments are shown. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0098239), licensed under a CC-BY license.")
![Western Blot: TLR3 Antibody (40C1285.6) [NBP2-24875] - All the cell lines displayed a strong expression of TLR3 protein. Cell lysates were electrophoresed and blotted to PVDF membrane, which was probed with TLR3-specific antibody. To confirm the immunoreactivity of the antibody, different positive controls were included. Beta-actin was served as loading control and was used to normalize expression levels between cells. Data are representative for analysis of >=2 independent experiments. Image collected and cropped by CiteAb from the following publication (//doi.org/10.1371/journal.pone.0060671) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/TLR3-Antibody-40C1285-6-Western-Blot-NBP2-24875-img0015.jpg)
![Immunohistochemistry-Paraffin: TLR3 Antibody (40C1285.6) [NBP2-24875] - Mouse colon using TLR3 antibody (clone 40C1285.6) at 1:500 dilution with HRP-DAB detection and hematoxylin counterstaining. Intense signal was found in subset of cells at the bases of the crypts.](http://images.novusbio.com/fullsize/TLR3-Antibody-40C1285-6-Immunohistochemistry-Paraffin-NBP2-24875-img0006.jpg)
![Flow Cytometry: TLR3 Antibody (40C1285.6) [NBP2-24875] - Expression of TLR3 in Fravel, L363, OPM1, RPMI8226, XG1, and NCI-H929 as determined by flow cytometry. HCMLs were stained using an intracellular staining protocol with TLR3 antibodies followed by relevant secondary fluorescent-conjugated antibodies. Filled histograms (purple) represent the isotype controls and the open histograms (red) indicate TLR3. Data are representative for analysis of >=2 independent experiments. Image collected and cropped by CiteAb from the following publication (//doi.org/10.1371/journal.pone.0060671) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/TLR3-Antibody-40C1285-6-Flow-Cytometry-NBP2-24875-img0016.jpg)
![Western Blot: TLR3 Antibody (40C1285.6) [NBP2-24875] - Analysis of TLR3 in lysates from A) human intestine and F) ovary using TLR3 antibody at 3 ug/ml. Goat anti-mouse HRP conjugate was used as secondary.](http://images.novusbio.com/fullsize/TLR3-Antibody-40C1285-6-Western-Blot-NBP2-24875-img0018.jpg)
![Western Blot: TLR3 Antibody (40C1285.6) [NBP2-24875] - HEK293T cells were transfected with TLR3, TLR3-9-3 and TLR3-3-9. Western blot was performed using anti-TLR3 or anti-HA antibodies. Anti-Beta-actin antibodies were used as a loading control. The representative data from three experiments are shown. Image collected and cropped by CiteAb from the following publication (//doi.org/10.1371/journal.pone.0092391) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/TLR3-Antibody-40C1285-6-Western-Blot-NBP2-24875-img0017.jpg)
![Immunohistochemistry-Paraffin: TLR3 Antibody (40C1285.6) [NBP2-24875] - Tissue section of mouse intestine using TLR3 antibody (clone 40C1285.6) at 1:500 dilution with HRP-DAB detection and hematoxylin counterstaining. The representative image shows a punctate staining of the ER and endosomes in a subset of cells in Peyer's patches (organized lymphoid nodules) in the tested section.](http://images.novusbio.com/fullsize/TLR3-Antibody-40C1285-6-Immunohistochemistry-Paraffin-NBP2-24875-img0007.jpg)
![Immunohistochemistry-Paraffin: TLR3 Antibody (40C1285.6) [NBP2-24875] - Analysis of TLR3 in (A) human gut lumen (longitudinal section, transverse region) using this antibody at 10 ug/ml (Data courtesy Dr. Elizabeth Furrie, University of Dundee) and mouse spleen tissue using isotype control (B) and this antibody (C) at 5 mg/ml.](http://images.novusbio.com/fullsize/TLR3-Antibody-40C1285-6-Immunohistochemistry-Paraffin-NBP2-24875-img0002.jpg)
![Immunohistochemistry: TLR3 Antibody (40C1285.6) - BSA Free [NBP2-24875] - The nasal epithelium expresses TLR3, TLR7, TLR9, RIG-I & MDA-5.Sections of nasal biopsies were incubated with antibodies against TLR3 (A), TLR7 (B), TLR9 (C), RIG-I (D), & MDA-5 (E) & visualized by 3, 3′-diaminobenzidine (brown). In control slides (F), N-series universal negative control reagent was used. All sections were accompanied with a square magnification. All slides were counterstained with haematoxylin (blue). The figure shows one representative biopsy out of four (3 male, 1 female). The arrows indicate positive stained cells. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/24886842), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nbp2-24875_mouse-monoclonal-tlr3-antibody-40c1285-6-310202415384128.jpg)
![Immunohistochemistry: TLR3 Antibody (40C1285.6) - BSA Free [NBP2-24875] - TLRs are expressed & functional in chondrocytes.A RT-PCR for TLR3 & 9 expression in primary human & murine chondrocytes. GAPDH served as loading control. B Confocal microscopy of labelled CpG (green) & poly(I:C) (red) uptake by either primary human chondrocytes (scale bar 20 µm) or murine hip caps (scale bar 50 µm (centre) 20 µm (right)). DAPI (blue) was used as counterstaining for nuclei. C IFN alpha ELISA of murine chondrocytes stimulated with ODN (one-way ANOVA:F (2, 9) = 2.21, p = 0.16, N = 4). D IFN alpha ELISA of primary human chondrocytes stimulated with ODN & poly(I:C) (one-way ANOVA:F (3, 11) = 0.75, p = 0.55, N = 4). E IFN beta ELISA of murine chondrocytes stimulated with poly(I:C) or ODN (one-way ANOVA: F (2, 15) = 59.61, p < 0.0001, N = 6). F IFN beta ELISA of primary human chondrocytes stimulated with poly(I:C) or ODN (one-way ANOVA:F (2, 6) = 95.43, p = <0.0001, N = 3). G Staurosporine was used to induce cell death. The release of RNA from human primary chondrocytes after treatment was measured in the culture supernatant using the RiboGreen assay (RM ANOVA: F (4, 12) = 101.2, p < 0.0001, N = 4). Dunnett’s post-hoc test revealed an increase for 200, 500, & 1000 ng/ml staurosporine treatment compared to the untreated control. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35277480), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nbp2-24875_mouse-monoclonal-tlr3-antibody-40c1285-6-31020241611475.jpg)
![Western Blot: TLR3 Antibody (40C1285.6) - BSA Free [NBP2-24875] - TLR mRNA & protein expression in airlifted immortal human corneal (HCET) & conjunctival epithelial cells (IOBA-NHC). (a) Averaged fold increase of TLR mRNA in IOBA-NHC cells. The increase was statistically significant for each TLR. (b) Averaged fold increase of TLR mRNA in HCET cells. The increase was statistically significant for each TLR. Cells were airlifted for 10 days. TLR mRNA level was determined by qPCR & compared to submerged cells. The experiment was repeated 3 times. Y error bars represent the standard deviation of the averaged results. (c) Micrographs of a representative western blot showing TLR protein expression in IOBA-NHC cells. Lane 1: submerged-cultured; lane 2: 3 days after airlifting culture; lane 3: 7 days after airlifting culture; lane 4: 10 days after airlifting culture. Glyceraldehyde 3-phosphate dehydrogenase (GAPDH) protein was probed as loading control. (d) Averaged TLR protein increase in IOBA-NHC cells 10 days after airlifting culture compared to submerged-cultured cells. X-ray films from 2 independent western blot experiments were scanned in a densitometer, & the results were averaged. The increase was statistically significant for each TLR protein tested. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/24976686), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nbp2-24875_mouse-monoclonal-tlr3-antibody-40c1285-6-310202416113516.jpg)
![Immunohistochemistry: TLR7 Antibody [NBP2-24906] - The expression of TLR-7 in the hippocampal brain region. The immunofluorescence of TLR7 recognized by Alexa 488, green. GFAP recognized by Alexa 594, red. NEUN recognized by Alexa 633, (blue) and merged image in the hippocampal region. NeuN and GFAP were applied to show the distribution of TLR7 within neuronal and supportive tissue populations. Scale bar 80 um. Image collected and cropped by CiteAb from the following publication (//doi.org/10.1371/journal.pone.0222818) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/TLR7-Antibody-Immunohistochemistry-NBP2-24906-img0022.jpg "Immunohistochemistry: TLR7 Antibody [NBP2-24906] - The expression of TLR-7 in the hippocampal brain region. The immunofluorescence of TLR7 recognized by Alexa 488, green. GFAP recognized by Alexa 594, red. NEUN recognized by Alexa 633, (blue) and merged image in the hippocampal region. NeuN and GFAP were applied to show the distribution of TLR7 within neuronal and supportive tissue populations. Scale bar 80 um. Image collected and cropped by CiteAb from the following publication (//doi.org/10.1371/journal.pone.0222818) licensed under a CC-BY license.")
![Flow Cytometry: TLR7 Antibody [NBP2-24906] - An intracellular stain was performed on THP-1 cells with NBP2-24906 (blue) and a matched isotype control NBP2-24891 (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 1 ug/mL for 30 minutes at room temperature, followed by Rabbit IgG (H+L) Cross-Adsorbed Secondary Antibody, Dylight 550 (SA5-10033, Thermo Fisher).](http://images.novusbio.com/fullsize/TLR7-Antibody-Flow-Cytometry-NBP2-24906-img0025.jpg)
![Immunocytochemistry/Immunofluorescence: TLR7 Antibody [NBP2-24906] - Immunolocalization of TLR7 (A) and glial fibrillary acidic protein (GFAP) (B) in murine myenteric plexus. Most of the GFAP positive cells were also positive for TLR7 in the merged image (C, yellow staining). (Courtesy of Barajon I, et al., Journal of Histochemistry and Cytochemistry, 57(11): 1013-;1023, 2009.)](http://images.novusbio.com/fullsize/TLR7-Antibody-Immunocytochemistry-Immunofluorescence-NBP2-24906-img0002.jpg)
![Immunohistochemistry: TLR7 Antibody [NBP2-24906] - Expression of the TLRs 5 and 7 were evaluated in the PDAC tissue by their staining intensity using TLR5 antibody (NBP2-24787) and TLR7 antibody (NBP2-24906). Note negative staining in E and G; positive staining in F and H. For TLR7 immunopositivity was detectable in the cytoplasm with no notable membranous or nuclear positivity. TLR5 showed distinctive nuclear positivity, and detectable positivity in the cytoplasm in some samples. Image collected and cropped by CiteAb from the following publication (//doi.org/10.1371/journal.pone.0219245) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/TLR7-Antibody-Immunohistochemistry-NBP2-24906-img0023.jpg)
![Immunohistochemistry-Frozen: TLR7 Antibody [NBP2-24906] - analysis of frozen mouse ear skin tissue using anti-TLR7 antibody. Image from verified customer review.](http://images.novusbio.com/fullsize/TLR7-Antibody-Immunohistochemistry-Frozen-NBP2-24906-img0006.jpg)
![Immunohistochemistry-Frozen: TLR7 Antibody [NBP2-24906] - analysis of TLR7 in acetone-fixed, frozen mouse ear skin section using anti-TLR7 antibody. Image from verified customer review.](http://images.novusbio.com/fullsize/TLR7-Antibody-Immunohistochemistry-Frozen-NBP2-24906-img0005.jpg)
![Western Blot: TLR7 Antibody [NBP2-24906] - Analysis using the Azide Free version of NBP2-24906. Detection of TLR7 in RAW cell lysate using this antibody.](http://images.novusbio.com/fullsize/TLR7-Antibody-Western-Blot-NBP2-24906-img0018.jpg)
![Immunocytochemistry/Immunofluorescence: TLR7 Antibody [NBP2-24906] - Analysis using the Azide Free version of NBP2-24906. Staining of Raw 246.7 cells with Dylight 488 (green). Nuclei and alpha-tubulin were counterstained with DAPI (blue) and Dylight 550 (red). Image objective 40x. An antibody dilution of 1:10 was used.](http://images.novusbio.com/fullsize/TLR7-Antibody-Immunocytochemistry-Immunofluorescence-NBP2-24906-img0017.jpg)
![Immunohistochemistry-Paraffin: TLR7 Antibody - BSA Free [NBP2-24906] - Analysis of a FFPE tissue section of human skin using 1:200 dilution of TLR7 antibody (NBP2-24906). The staining was developed using HRP labeled anti-rabbit secondary antibody and DAB reagent, and nuclei of cells were counter-stained with hematoxylin.](http://images.novusbio.com/fullsize/TLR7-Antibody---BSA-Free-Immunohistochemistry-Paraffin-NBP2-24906-img0026.jpg)
![Immunohistochemistry-Paraffin: TLR7 Antibody - BSA Free [NBP2-24906] - Analysis of human colon tissue using NBP2-24905 (top) and an isotype control (bottom) at 5 ug/ml.](http://images.novusbio.com/fullsize/nbp2-24906_rabbit-polyclonal-tlr7-antibody-17720241044656.jpg)
![Immunohistochemistry: TLR7 Antibody - BSA Free [NBP2-24906] - Expression of TLR7 in lung tissues of non-smokers, smokers, & COPD patients. Total protein & mRNA were obtained from lung tissues of non-smokers (n = 15), smokers (n = 12), & COPD patients (n = 15). TLR7 protein & mRNA expression were determined by western blot (A) & real time PCR (B) in lung parenchyma. (A) Representative images of western blot for TLR7 & corresponding densitometry expressed as ratio to beta -actin. (B) TLR7 mRNA expression given as the ratio to GAPDH. (C, D, E) Lung sections were immunostained for TLR7 & quantified by means of immunohistochemical score of TLR7 in alveolar macrophages (C) & bronchial epithelial cells (D). (E) Representative immunohistochemistry images are shown. The control IgG isotype showed negative staining. Data are presented as individual values & mean ± standard deviation. Exact P values were obtained using Kruskal-Wallis & Dunn’s post-hoc tests. Image collected & cropped by CiteAb from the following publication (//respiratory-research.biomedcentral.com/articles/10.1186/s12931-015-0179-5), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nbp2-24906_rabbit-polyclonal-tlr7-antibody-310202416121942.jpg)
![Western Blot: TRPA1 Antibody [NB110-40763] - Expression and localization of TRPA1 channels in wild-type (WT) and APP/PS1 Tg mice. Brains were harvested from WT and APP/PS1 Tg mice at 8A months old. Western blot analysis of protein levels of TRPA1 and I+--tubulin. Image collected and cropped by Citeab from the following publication (Role of transient receptor potential ankyrin 1 channels in Alzheimer's disease. J Neuroinflammation (2016)) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/TRPA1-Antibody-Western-Blot-NB110-40763-img0014.jpg "Western Blot: TRPA1 Antibody [NB110-40763] - Expression and localization of TRPA1 channels in wild-type (WT) and APP/PS1 Tg mice. Brains were harvested from WT and APP/PS1 Tg mice at 8A months old. Western blot analysis of protein levels of TRPA1 and I+--tubulin. Image collected and cropped by Citeab from the following publication (Role of transient receptor potential ankyrin 1 channels in Alzheimer's disease. J Neuroinflammation (2016)) licensed under a CC-BY license.")
![Immunohistochemistry: TRPA1 Antibody [NB110-40763] - Staining TRPA1 in mouse intestine.](http://images.novusbio.com/fullsize/TRPA1-Antibody-Immunohistochemistry-NB110-40763-img0008.jpg)
![Immunocytochemistry/Immunofluorescence: TRPA1 Antibody [NB110-40763] - Ai2 elicits TRPA1-dependent Ca2+ influx in astrocytes. Immunostaining of primary astrocytes from WT mice with anti-IgG and anti-TRPA1 antibody, then FITC-conjugated secondary antibody. Image collected and cropped by Citeab from the following publication (Role of transient receptor potential ankyrin 1 channels in Alzheimer's disease. J Neuroinflammation (2016)) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/TRPA1-Antibody-Immunocytochemistry-Immunofluorescence-NB110-40763-img0011.jpg)
![Flow Cytometry: TRPA1 Antibody [NB110-40763] - An intracellular stain was performed on A549 cells with NB110-40763C (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 2.5 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to DyLight 650.](http://images.novusbio.com/fullsize/TRPA1-Antibody-Flow-Cytometry-NB110-40763-img0010.jpg)
![Flow Cytometry: TRPA1 Antibody [NB110-40763] - An intracellular stain was performed on A549 cells with NB110-40763G (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 5 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to DyLight 488](http://images.novusbio.com/fullsize/TRPA1-Antibody-Flow-Cytometry-NB110-40763-img0009.jpg)
![Western Blot: TRPA1 Antibody [NB110-40763] - The essential role of TRPA1 in Ai2-induced calcium influx in HEK293 cells. (a) Western blot analysis of TRPA1 and I+--tubulin protein levels in non-treated, vector-or TRPA1-transfected HEK293 cells. Image collected and cropped by Citeab from the following publication (Role of transient receptor potential ankyrin 1 channels in Alzheimer's disease. J Neuroinflammation (2016)) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/TRPA1-Antibody-Western-Blot-NB110-40763-img0013.jpg)
![Immunocytochemistry/Immunofluorescence: TRPA1 Antibody [NB110-40763] - Analysis of TRPA1 in HEK 293 cells (Flp In Trex system) cells.](http://images.novusbio.com/fullsize/TRPA1-Antibody-Immunocytochemistry-Immunofluorescence-NB110-40763-img0006.jpg)
![Western Blot: TRPA1 Antibody - BSA Free [NB110-40763] - Effects of Lycium barbarum polysaccharides (LBP) & capsaicin (CAP) on colonic (A) Cyclooxygenase-2 (COX-2), (B) Transient receptor potential cation channel V1 (TRPV1), & (C) Transient receptor potential ankyrin 1 (TRPA1) protein expression. (D) Representatives of Western blot for COX-2, TRPV1, TRPA1, & beta -actin. N: control group, U: ulcerative colitis induced group, L: LBP treated group, C: CAP treated group, M: mixed LBP & CAP treated group. Data are presented as mean ± SEM & analyzed by one-way ANOVA & Fisher’s least significant difference test (n = 8). # p < 0.05 compared to the N group. * p < 0.05 compared to the U group. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35269566), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-40763_rabbit-polyclonal-trpa1-antibody-310202415392558.jpg)
![Immunocytochemistry/ Immunofluorescence: TRPA1 Antibody - BSA Free [NB110-40763] - Expression & localization of TRPA1 channels in wild-type (WT) & APP/PS1 Tg mice. (a) Brains were harvested from WT & APP/PS1 Tg mice at 8 months old. Western blot analysis of protein levels of TRPA1 & alpha -tubulin. Data are mean ± SEM from 6 mice in each group. *, P < 0.05 vs. WT mice. (b, c) Immunohistochemistry of specimens of cortex & hippocampus from 8-month-old WT & APP/PS1 Tg mice with the antibodies anti-TRPA1, anti-vWF (endothelial cell marker), anti-NeuN (neuron marker), anti-GFAP (astrocyte marker) & anti-IBA-1 (microglia marker), then FITC- or Texas red-conjugated secondary antibody. Bar = 50 μm. vWF-positive cells denoted endothelial cells, NeuN-positive cells denoted neurons, & GFAP-positive cells denoted astrocytes, as indicated by arrowheads, stars or arrows, respectively Image collected & cropped by CiteAb from the following publication (//jneuroinflammation.biomedcentral.com/articles/10.1186/s12974-016-0557-z), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-40763_rabbit-polyclonal-trpa1-antibody-310202416235534.jpg)
![Immunocytochemistry/ Immunofluorescence: TRPA1 Antibody - BSA Free [NB110-40763] - Evaluation of anti-TRPA1 antibody specificity by western blotting & immunofluorescence. (a) Lysates derived from HEK293T cells transiently transfected with the TRPA1 & GFP expression construct (TRPA1 OE) or TRPM2 & GFP negative control (TRPM2 OE) were probed with the antibodies indicated. Additional untransfected & GFP only controls are presented in the first blot (6G8). Uncropped full length blots are displayed, gaps between the blots are present to indicate the use of a different antibody. Mouse mAbs C-5 & 6G8, & NB110-40763 can detect TRPA1 only in the membrane fraction of lysates at the expected molecular weight (127.5 kDa). Several TRPA1-specific bands are observed above this weight. NB110-40763 also detects several other antigens. Ab58844 & ACC- 037 only appear to detect antigens other than TRPA1 in the conditions used. (b) The performance of the same antibodies was evaluated by immunofluorescence (red) in comparison to the expression of the GFP reporter (green), or control TRPM2 & GFP overexpressing cells as for western blotting. Mouse mAb C-5 again shows high specificity with a strong correlation between the expression of the GFP reporter & antibody staining, & no staining in TRPM2 & GFP overexpressing controls. NB110-40763 also demonstrates some sensitivity but has high background that likely does not correspond to Fc binding of the antibody, as the other two rabbit polyclonal antibodies or isotype control did show different staining patterns. Ab58844 & ACC- 037 only appear to detect antigens other than TRPA1 in the conditions used. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31811235), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-40763_rabbit-polyclonal-trpa1-antibody-31020241623556.jpg)
![Western Blot: TRPA1 Antibody - BSA Free [NB110-40763] - Expression & localization of TRPA1 channels in wild-type (WT) & APP/PS1 Tg mice. (a) Brains were harvested from WT & APP/PS1 Tg mice at 8 months old. Western blot analysis of protein levels of TRPA1 & alpha -tubulin. Data are mean ± SEM from 6 mice in each group. *, P < 0.05 vs. WT mice. (b, c) Immunohistochemistry of specimens of cortex & hippocampus from 8-month-old WT & APP/PS1 Tg mice with the antibodies anti-TRPA1, anti-vWF (endothelial cell marker), anti-NeuN (neuron marker), anti-GFAP (astrocyte marker) & anti-IBA-1 (microglia marker), then FITC- or Texas red-conjugated secondary antibody. Bar = 50 μm. vWF-positive cells denoted endothelial cells, NeuN-positive cells denoted neurons, & GFAP-positive cells denoted astrocytes, as indicated by arrowheads, stars or arrows, respectively Image collected & cropped by CiteAb from the following publication (//jneuroinflammation.biomedcentral.com/articles/10.1186/s12974-016-0557-z), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-40763_rabbit-polyclonal-trpa1-antibody-310202416235536.jpg)
![Western Blot: GAPDH Antibody (6C5) [NB600-502] - MUS81 promotes DNA synthesis during mitosis in BRCA2-deficient cells. Cell extracts were immunoblotted as indicated. SMC1 and GAPDH were used as loading controls. Image collected and cropped by CiteAb from the following publication (//www.nature.com/doifinder/10.1038/ncomms15983), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/GAPDH-Antibody-6C5-Western-Blot-NB600-502-img0007.jpg "Western Blot: GAPDH Antibody (6C5) [NB600-502] - MUS81 promotes DNA synthesis during mitosis in BRCA2-deficient cells. Cell extracts were immunoblotted as indicated. SMC1 and GAPDH were used as loading controls. Image collected and cropped by CiteAb from the following publication (//www.nature.com/doifinder/10.1038/ncomms15983), licensed under a CC-BY license.")
![Western Blot: GAPDH Antibody (6C5) [NB600-502] - Western blot analysis of GAPDH expression in 1) HeLa, 2) NTERA-2, 3) A-431, 4) HepG2, 5) MCF-7, 6) NIH 3T3, 7) PC-12 and 8) COS-7 whole cell lysates. Theoretical molecular weight: 36 kDa.](http://images.novusbio.com/fullsize/GAPDH-Antibody-6C5-Western-Blot-NB600-502-img0001.jpg)
![Western Blot: GAPDH Antibody (6C5) [NB600-502] - Western blot of FGF23 in the kidney. GAPDH antibody (6C5) served as an internal control. Each value represents the mean +/- SEM. Citation: Sugiura H, Matsushita A, Futaya M, Teraoka A, Akiyama K-i, Usui N, et al. (2018) Fibroblast growth factor 23 is upregulated in the kidney in a chronic kidney disease rat model. PLoS ONE 13(3): e0191706. //doi.org/10.1371/journal.pone.0191706](http://images.novusbio.com/fullsize/GAPDH-Antibody-6C5-Western-Blot-NB600-502-img0006.jpg)
![Simple Western: GAPDH Antibody (6C5) [NB600-502] - Simple Western lane view shows a specific band for GAPDH in 0.5 mg/ml of HeLa lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system. Note: band observed higher than predicted 36 kDa molecular weight.](http://images.novusbio.com/fullsize/GAPDH-Antibody-6C5-Simple-Western-NB600-502-img0003.jpg)
![Simple Western: GAPDH Antibody (6C5) [NB600-502] - Anaylsis in rat brain and spinal cord. This image includes the GAPDH at the predicted kDa as well as a glucocorticoid receptor antibody (peak 102). Verified customer review.](http://images.novusbio.com/fullsize/GAPDH-Antibody-6C5-Simple-Western-NB600-502-img0005.jpg)
![Western Blot: GAPDH Antibody (6C5cc) [NB600-502] - Western blot analysis for whole cell & nuclear signal transduction proteins. (A) Phosphorylated FAK (Y397) was significantly decreased at 24 h & significantly increased at 48 h as compared to sham. (B) Nuclear localization of corresponding signal transduction molecules, p38, & p65, were decreased at 24 h & increased at 48 h as compared to sham. *p 0.05.Immortalized Brca1F/C61G MEFs were infected with retroviruses expressing the indicated shRNAs and/or Cre recombinase, followed by selection with puromycin for 72 h. The frequency of end-to-end chromosome-type fusions was analysed as in (A).MEFs of the indicated genotypes were infected with retroviruses expressing TRF2 and/or CtIP shRNAs, followed by selection with puromycin for 72 h. Cell extracts were prepared 48 h later & analysed by Western blotting as indicated. GAPDH was used as a loading control. *non-specific band. Cells treated as in (C) & (E) were arrested in mitosis with colcemid, & mitotic chromosomes isolated 48 h later were fixed & stained with a Cy3-conjugated (CCCTAA)3-PNA probe (D, F). The frequency of end-to-end chromosome-type fusions is represented as a percentage of fusions observed after TRF2 depletion. Error bars represent SD of two independent experiments. P-values were calculated using an unpaired two-tailed t-test. *P ≤ 0.05. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/25582120), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-502_mouse-monoclonal-gapdh-antibody-6c5-310202416154645.jpg)
![Immunohistochemistry-Paraffin: IKK alpha Antibody (14A231) - BSA Free [NB100-56704] - Analysis of human IKK alpha in tumors of the three groups B (C-IKK alpha), E (Control), H (N-IKK alpha). Specific staining of human IKK alpha-using the NB100-56704 antibody. Scale bar: 70um. Image collected and cropped by CiteAb from the following publication (//www.oncotarget.com/article/8792/text/) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/IKK-alpha-Antibody-14A231-BSA-Free-Immunohistochemistry-Paraffin-NB100-56704-img0018.jpg "Immunohistochemistry-Paraffin: IKK alpha Antibody (14A231) - BSA Free [NB100-56704] - Analysis of human IKK alpha in tumors of the three groups B (C-IKK alpha), E (Control), H (N-IKK alpha). Specific staining of human IKK alpha-using the NB100-56704 antibody. Scale bar: 70um. Image collected and cropped by CiteAb from the following publication (//www.oncotarget.com/article/8792/text/) licensed under a CC-BY license.")
![Western Blot: IKK alpha Antibody (14A231) - BSA Free [NB100-56704] - Western blot showing the increased expression of IKK-alpha in transgenic mice. Image collected and cropped by CiteAb from the following publication (oncotarget.com/fulltext/8792), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/IKK-alpha-Antibody-14A231-BSA-Free-Western-Blot-NB100-56704-img0021.jpg)
![Flow Cytometry: IKK alpha Antibody (14A231) - BSA Free [NB100-56704] - An intracellular stain was performed on Hek293 cells with IKK alpha Antibody (14A231) NB100-56704 (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, followed by Mouse IgG (H+L) Cross-Adsorbed Secondary Antibody, Dylight 550 (35503, Thermo Fisher).](http://images.novusbio.com/fullsize/IKK-alpha-Antibody-14A231-BSA-Free-Flow-Cytometry-NB100-56704-img0017.jpg)
![Western Blot: IKK alpha Antibody (14A231) - BSA Free [NB100-56704] - IKK alpha Antibody (14A231) [NB100-56704] - Total protein from various Human, Mouse and Rat cell lines were separated on a 12% gel by SDS-PAGE, transferred to PVDF membrane and blocked in 5% non-fat milk in TBST. The membrane was probed with 1.0 ug/mL anti-IKK-alpha in 1% non-fat milk in TBST and detected with an anti-mouse HRP secondary antibody using chemiluminescence.](http://images.novusbio.com/fullsize/IKK-alpha-Antibody-14A231-BSA-Free-Western-Blot-NB100-56704-img0010.jpg)
![Immunocytochemistry/Immunofluorescence: IKK alpha Antibody (14A231) - BSA Free [NB100-56704] - Antibody was tested in HeLa cells with Dylight 488 (green). Nuclei and alpha-tubulin were counterstained with DAPI (blue) and Dylight 550 (red). An antibody dilution of 1:10 was used. Image objective 40X.](http://images.novusbio.com/fullsize/IKK-alpha-Antibody-14A231-BSA-Free-Immunocytochemistry-Immunofluorescence-NB100-56704-img0008.jpg)
![Immunohistochemistry: IKK alpha Antibody (14A231) - BSA Free [NB100-56704] - B-I. Immunohistochemistry showing the expression of the transgenic protein in N-IKKa and C-IKKa tumors. Staining with NB100-56704 antibody is shown. (B, C) Representative images showing the expression of transgenic IKKa in tumors and adjacent skin of N-IKKa/TgAC mice (B), and C-IKKa/TgAC animals (C). (D, E) Detail showing the nuclear (D) or cytoplasmic (E) localization of the transgenic IKKa in tumors. (F, G) Similar levels of expression of the transgenic IKKa in different N-IKKa tumors. By contrast variable levels of expression of the transgene are observed between different C-IKKa tumors (H, I). t: tumor; s: non-tumoral skin. Scale bar: (B, C) 100um; (D, E) 80 um; (F-I) 200 um. Image collected and cropped by CiteAb from the following publication (//www.oncotarget.com/article/8792/text/) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/IKK-alpha-Antibody-14A231-BSA-Free-Immunohistochemistry-NB100-56704-img0022.jpg)
![Western Blot: IKK alpha Antibody (14A231) - BSA Free [NB100-56704] - IKK alpha Antibody (14A231) [NB100-56704] - Analysis of IKK alpha in Daudi cell lysate using IKK alpha antibody at 1 ug/mL.](http://images.novusbio.com/fullsize/IKK-alpha-Antibody-14A231-BSA-Free-Western-Blot-NB100-56704-img0005.jpg)
![Immunocytochemistry/Immunofluorescence: IKK alpha Antibody (14A231) - BSA Free [NB100-56704] - A431 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-IKK alpha Antibody (14A231) at 2 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/IKK-alpha-Antibody-14A231-BSA-Free-Immunocytochemistry-Immunofluorescence-NB100-56704-img0014.jpg)
![Immunocytochemistry/Immunofluorescence: IKK alpha Antibody (14A231) - BSA Free [NB100-56704] - HeLa cells were fixed for 10 minutes using 10% formalin and then permeabilized for 5 minutes using 1X PBS + 0.05% Triton X-100. The cells were incubated with anti-IKK alpha Antibody (14A231) at 2 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/IKK-alpha-Antibody-14A231-BSA-Free-Immunocytochemistry-Immunofluorescence-NB100-56704-img0015.jpg)
![Immunohistochemistry-Paraffin: IKK alpha Antibody (14A231) - BSA Free [NB100-56704] - Analysis of a FFPE tissue section of human kidney using 1:200 dilution of IKK alpha clone 14A231 antibody. The staining was developed using HRP labeled anti-rabbit secondary antibody and DAB reagent, and nuclei of cells were counter-stained with hematoxylin.](http://images.novusbio.com/fullsize/IKK-alpha-Antibody-14A231-BSA-Free-Immunohistochemistry-Paraffin-NB100-56704-img0016.jpg)
![Immunohistochemistry-Paraffin: IKK alpha Antibody (14A231) - BSA Free [NB100-56704] - Expression of the transgenic IKK alpha protein in skin of C-IKK alpha and N-IKK alpha mice. D-E. Expression of exogenous IKK alpha protein in back skin of 1-month-old mice. Immunostaining with the NB100-56704 anti-IKK alpha antibody is shown. Note the cytoplasmic expression of the transgene in the C-IKK alpha mice (D). By contrast, it is located in the nuclei of cells in the N-IKK alpha mice (E). In both types of transgenic mice the exogenous IKK alpha is expressed in basal keratinocytes (bk), in the outer root sheath of hair follicles (ORS) and in cells surrounding the sebaceous glands (sb). Scale bar: 60um. Image collected and cropped by CiteAb from the following publication (//www.oncotarget.com/article/8792/text/) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/IKK-alpha-Antibody-14A231-BSA-Free-Immunohistochemistry-Paraffin-NB100-56704-img0020.jpg)
![Simple Western: IKK alpha Antibody (14A231) - BSA Free [NB100-56704] - IKK alpha Antibody (14A231) [NB100-56704] - Image shows a specific band for IKK alpha in 0.5 mg/mL of Daudi (left) and U937 (right) lysate. This exeriment was performed under reducing conditions using the 12-230 kDa separation system.](http://images.novusbio.com/fullsize/IKK-alpha-Antibody-14A231-BSA-Free-Simple-Western-NB100-56704-img0009.jpg)
![Western Blot: IKK alpha Antibody (14A231) - BSA Free [NB100-56704] - NEMO-Ub binding is essential for TNF alpha signaling, but not for IL-1 beta signaling.(a) Schematic illustration of NEMO deletions or point mutations. (b,c) Effects of NEMO C-terminal deletion mutants on TNF alpha & IL-1 beta signaling. NEMO−/Y MEFs were reconstituted with mock, NEMO WT or different C-terminal deletion constructs & stimulated with TNF alpha (b) or IL-1 beta (c). Effects on NF-kappa B signaling were investigated by determining I kappa B alpha phosphorylation & degradation in Western Blots as well as NF-kappa B-DNA binding by EMSA. (d,e) Effects of NEMO D311N on TNF alpha & IL-1 beta signaling. NEMO−/Y MEFs were reconstituted with mock, NEMO WT or NEMO D311N point mutant & stimulated with TNF alpha (d) or IL-1 beta (e). Analysis on NF-kappa B signaling were performed as in (b,c). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26740240), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-56704_mouse-monoclonal-ikk-alpha-antibody-14a231-bsa-free-310202415392529.jpg)
![Western Blot: IKK alpha Antibody (14A231) - BSA Free [NB100-56704] - Expression of the transgenic IKK alpha protein in skin of C-IKK alpha & N-IKK alpha miceA. Recombinant DNA constructs employed to generate both transgenic mice lines. For C-IKK alpha mice generation, the nuclear localization signal (NLS) was removed from the sequence of the human IKK alpha cDNA employed. In the construct used for generation of the N-IKK alpha mice an extra NLS signal was added. WT IKK alpha ; wild type IKK alpha . B. Western blot of total protein extracts showing IKK alpha expression in back skin of Control & C-and N-IKK alpha mice. Actin was used as a loading control. C. Representative example of the K5 staining in back skin section of Control mice. D-E. Expression of exogenous IKK alpha protein in back skin of 1-month-old mice. Immunostaining with the NB100-56704 anti-IKK alpha antibody is showed; similar results were obtained with the H00001147-M04 IKK alpha antibody (not shown). Note the cytoplasmic expression of the transgene in the C-IKK alpha mice (D). By contrast, it is located in the nuclei of cells in the N-IKK alpha mice (E). In both types of transgenic mice the exogenous IKK alpha is expressed in basal keratinocytes (bk), in the outer root sheath of hair follicles (ORS) & in cells surrounding the sebaceous glands (sb). F. Back skin section of Control mice. The NB100-56704 antibody used does not recognize the endogenous IKK alpha in immunohistochemical assays. G. Endogenous IKK alpha expression in control mice using the IKK alpha (sc-7182) antibody. Scale bar: (C) 70 μm; (D-G) 60 μm. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27121058), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-56704_mouse-monoclonal-ikk-alpha-antibody-14a231-bsa-free-310202415523920.jpg)
![Immunohistochemistry-Paraffin: IKK alpha Antibody (14A231) - BSA Free [NB100-56704] - Expression of the transgenic IKK alpha protein in skin of C-IKK alpha & N-IKK alpha miceA. Recombinant DNA constructs employed to generate both transgenic mice lines. For C-IKK alpha mice generation, the nuclear localization signal (NLS) was removed from the sequence of the human IKK alpha cDNA employed. In the construct used for generation of the N-IKK alpha mice an extra NLS signal was added. WT IKK alpha ; wild type IKK alpha . B. Western blot of total protein extracts showing IKK alpha expression in back skin of Control & C-and N-IKK alpha mice. Actin was used as a loading control. C. Representative example of the K5 staining in back skin section of Control mice. D-E. Expression of exogenous IKK alpha protein in back skin of 1-month-old mice. Immunostaining with the NB100-56704 anti-IKK alpha antibody is showed; similar results were obtained with the H00001147-M04 IKK alpha antibody (not shown). Note the cytoplasmic expression of the transgene in the C-IKK alpha mice (D). By contrast, it is located in the nuclei of cells in the N-IKK alpha mice (E). In both types of transgenic mice the exogenous IKK alpha is expressed in basal keratinocytes (bk), in the outer root sheath of hair follicles (ORS) & in cells surrounding the sebaceous glands (sb). F. Back skin section of Control mice. The NB100-56704 antibody used does not recognize the endogenous IKK alpha in immunohistochemical assays. G. Endogenous IKK alpha expression in control mice using the IKK alpha (sc-7182) antibody. Scale bar: (C) 70 μm; (D-G) 60 μm. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27121058), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-56704_mouse-monoclonal-ikk-alpha-antibody-14a231-bsa-free-3102024168399.jpg)
![Western Blot: Lightning-Link HRP Antibody Labeling Kit [701-0000]](http://images.novusbio.com/fullsize/Lightning-Link-HRP-Antibody-Labeling-Kit-Western-Blot-701-0000-img0006.jpg "Western Blot: Lightning-Link HRP Antibody Labeling Kit [701-0000]")
![Immunohistochemistry: Lightning-Link HRP Antibody Labeling Kit [701-0000]](http://images.novusbio.com/fullsize/Lightning-Link-HRP-Antibody-Labeling-Kit-Immunohistochemistry-701-0000-img0004.jpg)
![Western Blot: Lightning-Link HRP Antibody Labeling Kit [701-0000]](http://images.novusbio.com/fullsize/Lightning-Link-HRP-Antibody-Labeling-Kit-Western-Blot-701-0000-img0005.jpg)
![Immunohistochemistry: Lightning-Link HRP Antibody Labeling Kit [701-0000] - Brown= CD20 labeled with HRP, Red= CD3 labeled with alkaline phosphatase. Mouse anti-human CD20 was conjugated to HRP using Lightning-Link® kits, and rat anti human CD3 was conjugated to Alkaline Phosphatase using Lightning Link®. Both antibodies were then used simultaneously to stain formalin fixed paraffin fixed embedded sections of human lymph node. CD20 positive cells are visualized with DAB and are stained brown, and CD3 visualized with Fast Red and stained red.](http://images.novusbio.com/fullsize/Lightning-Link-HRP-Antibody-Labeling-Kit-Immunohistochemistry-701-0000-img0002.jpg)
![Western Blot: BMAL1 Antibody [NB100-2288] - Oxidation causes accumulation of BMAL1. Head and neck cancer cells have different expression levels of the core clock protein BMAL1. Image collected and cropped by CiteAb from the following publication (//www.ncbi.nlm.nih.gov/pmc/articles/PMC5173143/) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/BMAL1-Antibody-Western-Blot-NB100-2288-img0021.jpg "Western Blot: BMAL1 Antibody [NB100-2288] - Oxidation causes accumulation of BMAL1. Head and neck cancer cells have different expression levels of the core clock protein BMAL1. Image collected and cropped by CiteAb from the following publication (//www.ncbi.nlm.nih.gov/pmc/articles/PMC5173143/) licensed under a CC-BY license.")
![Immunohistochemistry: BMAL1 Antibody [NB100-2288] - Analysis of BMAL1 in mouse cerebral cortex (left: wt, right: Bmal1 KO) using anti-BMAL1 antibody. Image from verified customer review.](http://images.novusbio.com/fullsize/BMAL1-Antibody-Chromatin-Immunoprecipitation-NB100-2288-img0018.jpg)
![<b>Biological Strategies Validation. </b>Immunohistochemistry: BMAL1 Antibody [NB100-2288] - Inhibition of mTOR signaling with Rapamycin rescues PTEN-driven accumulation of BMAL1A. Tissue samples and graphic show BMAL1 in K14cre PtenF/F mice and control (arrows). Note a significant amount of BMAL1 expression in PTEN mutant mice. K14cre PtenF/F mice and control littermates received Rapamycin or vehicle every other day for 15 days. Rapamycin treatment reduces the expression of nuclear BMAL1 in K14cre PtenF/F mice (arrowhead) (*** p0.05). Scale bars -30um. Image collected and cropped by CiteAb from the following publication (//www.ncbi.nlm.nih.gov/pmc/articles/PMC5173143/) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/BMAL1-Antibody-Immunocytochemistry-Immunofluorescence-NB100-2288-img0024.jpg)
![Western Blot: BMAL1 Antibody [NB100-2288] - Oxidation causes accumulation of BMAL1. Western blot assay demonstrates time-dependent accumulation of BMAL1 upon oxidative stress in HNSCC cells (*p0.05). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27285754), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2288_rabbit-polyclonal-bmal1-antibody-31020241534364.jpg)
![Western Blot: BMAL1 Antibody [NB100-2288] - Small interference RNA targeting Raptor & Rictor disrupts BMAL1 accumulation in HNSCCTargeted disruption of Raptor (A-B) & Rictor (C-D) using siRNA results in a dose-dependent downregulation of BMAL1 in HNSCC cells. E. Disruption of PTEN by protein oxidation causes activation of mTOR signaling, resulting in accumulation of BMAL1. Notably, inhibition of mTOR signaling, particularly mTORC1 & mTORC2, results in restoration of normal BMAL1 levels in the epidermis of mice & head & neck cancer cells. These results demonstrate a novel role for mTOR in regulating nuclear levels of the core clock gene BMAL1. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27285754), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2288_rabbit-polyclonal-bmal1-antibody-310202415171349.jpg)
![Western Blot: BMAL1 Antibody [NB100-2288] - Targeted disruption of PTEN in vitro & in vivo induces activation of pS6 & BMAL1A. & B. Targeted inhibition of PTEN using siRNA results in concentration-dependent inhibition of PTEN protein in HNSCC cells. HNSCC cells show accumulation of BMAL1 & pS6 in response to PTEN inhibition. C. Immunofluorescence assay to detect BMAL1 in PTEN conditional knockout mice (K14cre PtenF/F) & control littermates. Immunofluorescences & graphic show high accumulation of nuclear BMAL1 in K14cre PtenF/F mice compared to control mice (K14cre). Scale bars represent 50 μm. Black & white images depict cells positive for BMAL1 in K14cre PtenF/F mice (arrows) compared to few BMAL-positive cells in control mice (arrowhead). Scale bars represent 10 μm. (**p<0.01). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27285754), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2288_rabbit-polyclonal-bmal1-antibody-310202415304255.jpg)
![Western Blot: BMAL1 Antibody [NB100-2288] - Small interference RNA targeting Raptor & Rictor disrupts BMAL1 accumulation in HNSCCTargeted disruption of Raptor (A-B) & Rictor (C-D) using siRNA results in a dose-dependent downregulation of BMAL1 in HNSCC cells. E. Disruption of PTEN by protein oxidation causes activation of mTOR signaling, resulting in accumulation of BMAL1. Notably, inhibition of mTOR signaling, particularly mTORC1 & mTORC2, results in restoration of normal BMAL1 levels in the epidermis of mice & head & neck cancer cells. These results demonstrate a novel role for mTOR in regulating nuclear levels of the core clock gene BMAL1. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27285754), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2288_rabbit-polyclonal-bmal1-antibody-31020241538245.jpg)
![Western Blot: BMAL1 Antibody [NB100-2288] - Small interference RNA targeting Raptor & Rictor disrupts BMAL1 accumulation in HNSCCTargeted disruption of Raptor (A-B) & Rictor (C-D) using siRNA results in a dose-dependent downregulation of BMAL1 in HNSCC cells. E. Disruption of PTEN by protein oxidation causes activation of mTOR signaling, resulting in accumulation of BMAL1. Notably, inhibition of mTOR signaling, particularly mTORC1 & mTORC2, results in restoration of normal BMAL1 levels in the epidermis of mice & head & neck cancer cells. These results demonstrate a novel role for mTOR in regulating nuclear levels of the core clock gene BMAL1. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27285754), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2288_rabbit-polyclonal-bmal1-antibody-31020241534379.jpg)
![Western Blot: BMAL1 Antibody [NB100-2288] - Small interference RNA targeting Raptor & Rictor disrupts BMAL1 accumulation in HNSCCTargeted disruption of Raptor (A-B) & Rictor (C-D) using siRNA results in a dose-dependent downregulation of BMAL1 in HNSCC cells. E. Disruption of PTEN by protein oxidation causes activation of mTOR signaling, resulting in accumulation of BMAL1. Notably, inhibition of mTOR signaling, particularly mTORC1 & mTORC2, results in restoration of normal BMAL1 levels in the epidermis of mice & head & neck cancer cells. These results demonstrate a novel role for mTOR in regulating nuclear levels of the core clock gene BMAL1. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27285754), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2288_rabbit-polyclonal-bmal1-antibody-31020241534315.jpg)
![Western Blot: BMAL1 Antibody [NB100-2288] - Targeted disruption of PTEN in vitro & in vivo induces activation of pS6 & BMAL1A. & B. Targeted inhibition of PTEN using siRNA results in concentration-dependent inhibition of PTEN protein in HNSCC cells. HNSCC cells show accumulation of BMAL1 & pS6 in response to PTEN inhibition. C. Immunofluorescence assay to detect BMAL1 in PTEN conditional knockout mice (K14cre PtenF/F) & control littermates. Immunofluorescences & graphic show high accumulation of nuclear BMAL1 in K14cre PtenF/F mice compared to control mice (K14cre). Scale bars represent 50 μm. Black & white images depict cells positive for BMAL1 in K14cre PtenF/F mice (arrows) compared to few BMAL-positive cells in control mice (arrowhead). Scale bars represent 10 μm. (**p<0.01). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27285754), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2288_rabbit-polyclonal-bmal1-antibody-31020241535633.jpg)
![Western Blot: BMAL1 Antibody [NB100-2288] - Oxidation causes accumulation of BMAL1A. Head & neck cancer cells have different expression levels of the core clock protein BMAL1. B. Immunofluorescence assay depicts accumulation of ROS (green channel) & BMAL1 (red channel) upon oxidation. C. & D. Western blot assay demonstrates time-dependent accumulation of BMAL1 upon oxidative stress in HNSCC cells (*p<0.05, **p<0.01). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27285754), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2288_rabbit-polyclonal-bmal1-antibody-310202415363747.jpg)
![Immunocytochemistry/ Immunofluorescence: BMAL1 Antibody [NB100-2288] - Targeted disruption of PTEN in vitro & in vivo induces activation of pS6 & BMAL1A. & B. Targeted inhibition of PTEN using siRNA results in concentration-dependent inhibition of PTEN protein in HNSCC cells. HNSCC cells show accumulation of BMAL1 & pS6 in response to PTEN inhibition. C. Immunofluorescence assay to detect BMAL1 in PTEN conditional knockout mice (K14cre PtenF/F) & control littermates. Immunofluorescences & graphic show high accumulation of nuclear BMAL1 in K14cre PtenF/F mice compared to control mice (K14cre). Scale bars represent 50 μm. Black & white images depict cells positive for BMAL1 in K14cre PtenF/F mice (arrows) compared to few BMAL-positive cells in control mice (arrowhead). Scale bars represent 10 μm. (**p<0.01). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27285754), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2288_rabbit-polyclonal-bmal1-antibody-310202415523930.jpg)
![Immunohistochemistry: BMAL1 Antibody [NB100-2288] - Astrocyte Bmal1 regulates genes with conflicting effects on A beta deposition. (A) Topro, GFAP, & BMAL1 staining in CA1 hippocampus of 4-month-old BMAL1 aKO; APP/PS1-21 mice & Cre- controls (scale bar = 100 µm). Arrows indicate astrocyte nuclei quantified as indicated by Topro nuclei surrounded by GFAP positivity. Blue circles indicate nuclei quantified as BMAL1 negative. Quantification of astrocytes counted as BMAL1- or BMAL1+ is shown on the right. n = 5 mice per group, **** = p < 0.0001 by two-way ANOVA with Sidak multiple comparisons test. (B) Heatmap of Fluidigm qPCR analysis of 20 genes involved in the circadian clock, glial activation, & Alzheimer’s Disease in cortex from Aldh1l1-CreERT2; Bmal1fl/fl mice & Cre- controls with or without APP/PS1-21 or APPNL-G-F/wt (n = 6–8 mice per group). Two-way ANOVA analysis: c = significant main effect of Cre genotype, m = main effect of A beta model, c*m = interaction effect of cre & A beta model, - = no significance (all p < 0.05). (C) Individually plotted genes from A. * = p < 0.05, ** = p < 0.005, *** = p < 0.0005 by two-way ANOVA with Sidak multiple comparisons test. Panel B was made using GraphPad Prism version 9.2 (//www.graphpad.com). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35110643), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-2288_rabbit-polyclonal-bmal1-antibody-310202415525251.jpg)
![Dual RNAscope ISH-IHC: xCT Antibody [NB300-318] - Formalin-fixed paraffin-embedded tissue sections of human stomach were probed for xCT mRNA (ACD RNAScope Probe, catalog #422688; Fast Red chromogen, ACD catalog # 322750). Adjacent tissue section was processed for immunohistochemistry using Rabbit Polyclonal (Novus Biologicals catalog # NB300-318) at 0.25ug/mL with 1 hour incubation at room temperature followed by incubation with anti-rabbit IgG VisUCyte HRP Polymer Antibody (Catalog # VC003) and DAB chromogen (yellow-brown). Tissue was counterstained with hematoxylin (blue). Specific staining was localized to glandular cells.](http://images.novusbio.com/fullsize/xCT-Antibody-Dual-RNAscope-ISH-IHC-NB300-318-img0012.jpg "<b>Orthogonal Strategies Validation. </b>Dual RNAscope ISH-IHC: xCT Antibody [NB300-318] - Formalin-fixed paraffin-embedded tissue sections of human stomach were probed for xCT mRNA (ACD RNAScope Probe, catalog #422688; Fast Red chromogen, ACD catalog # 322750). Adjacent tissue section was processed for immunohistochemistry using Rabbit Polyclonal (Novus Biologicals catalog # NB300-318) at 0.25ug/mL with 1 hour incubation at room temperature followed by incubation with anti-rabbit IgG VisUCyte HRP Polymer Antibody (Catalog # VC003) and DAB chromogen (yellow-brown). Tissue was counterstained with hematoxylin (blue). Specific staining was localized to glandular cells.")
![<b>Biological Strategies Validation and Orthogonal Strategies Validation.</b>Simple Western: xCT Antibody [NB300-318] - Simple Western lane view shows a specific band for xCT using NB300-318 at 25 ug/ml in HeLa and HeLa + DEM cell lysates. This experiment was performed under reducing conditions using the 12-230 kDa separation system.](http://images.novusbio.com/fullsize/xCT-Antibody-Simple-Western-NB300-318-img0013.jpg)
![Western Blot: xCT Antibody [NB300-318] - Western blot analysis of protein isolated from subcutaneous tumors derived from in vivo growth of the clones relative to WT-derived tumors revealed that xCT levels remained low, phospho-STAT5 (p-STAT5) levels remained high, and phospho-STAT3 (p-STAT3) levels remained unchanged in the absence of SH-4-54. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0161202), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/xCT-Antibody-Western-Blot-NB300-318-img0015.jpg)
![Immunohistochemistry: xCT Antibody [NB300-318] - xCT staining in the absorptive epithelia of small intestinal villi detected using NB300-318.](http://images.novusbio.com/fullsize/xCT-Antibody-Immunohistochemistry-NB300-318-img0006.jpg)
![Flow Cytometry: xCT Antibody [NB300-318] - An intracellular stain was performed on HeLa cells with NB300-318AF647 (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/xCT-Antibody-Flow-Cytometry-NB300-318-img0009.jpg)
![Immunocytochemistry/Immunofluorescence: xCT Antibody [NB300-318] - xCT antibody was tested in HepG2 cells with DyLight 488 (green). Nuclei and alpha-tubulin were counterstained with DAPI (blue) and DyLight 550 (red).](http://images.novusbio.com/fullsize/xCT-Antibody-Immunocytochemistry-Immunofluorescence-NB300-318-img0005.jpg)
![Flow Cytometry: xCT Antibody [NB300-318] - An intracellular stain was performed on HeLa cells with xCT Antibody NB300-318AF488 (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 5 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to Alexa Fluor 488.](http://images.novusbio.com/fullsize/xCT-Antibody-Flow-Cytometry-NB300-318-img0010.jpg)
![<b>Biological Strategies Validation. </b>Western Blot: xCT Antibody [NB300-318] - Total protein from Human HeLa cells treated with and without 0.1 mM Diethyl Maleate for 24 hours was separated on a 12% gel by SDS-PAGE, transferred to PVDF membrane and blocked in 5% non-fat milk in TBST. The membrane was probed with 2.0 ug/ml anti-xCT in 1% non-fat milk in TBST and detected with an anti-rabbit HRP secondary antibody using chemiluminescence. Note the increase in xCT expression with treatment.](http://images.novusbio.com/fullsize/xCT-Antibody-Western-Blot-NB300-318-img0007.jpg)
![Flow Cytometry: xCT Antibody [NB300-318] - An intracellular stain was performed on HeLa with xCT Antibody NB300-318 and a matched isotype control. Cells were fixed with 4% PFA and then permeablized with 0.1% saponin. Cells were incubated in an antibody dilution of 2.5 ug/mL for 30 minutes at room temperature, followed by Rabbit IgG APC-conjugated Secondary Antibody (F0111, R&D Systems).](http://images.novusbio.com/fullsize/xCT-Antibody-Flow-Cytometry-NB300-318-img0008.jpg)
![Simple Western: xCT Antibody [NB300-318] - Simple Western lane view shows a specific band for xCT using NB300-318 at 25 ug/mL in HepG2 cell lysates and antibody at 25 ug/mL. Electropherogram image of corresponding Simple Western lane view at WES molecular weight of 63 kDa. Image reported by internal validation.](http://images.novusbio.com/fullsize/xCT-Antibody-Simple-Western-NB300-318-img0014.jpg)
![Western Blot: xCT Antibody - BSA Free [NB300-318] - Subcutaneous injection into nude mice revealed that (A) MDA-MB-231 SH-4-54-resistant clone #2 proliferated at a slower rate than its wild-type (WT) counterpart in vivo. (B) qPCR demonstrated that xCT mRNA levels were lower in tumours isolated from animals injected with clone #2 relative to WT cells (2 animals per treatment group). (C) Western blot analysis of protein isolated from subcutaneous tumours derived from in vivo growth of the clones relative to WT-derived tumours revealed that xCT levels remained low, phospho-STAT5 (p-STAT5) levels remained high, & phospho-STAT3 (p-STAT3) levels remained unchanged in the absence of SH-4-54. Image collected & cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0161202), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-318_rabbit-polyclonal-xct-antibody-310202415392520.jpg)
![Western Blot: xCT Antibody - BSA Free [NB300-318] - A link between KSHV latency & the MC1-R signaling axis in skin-derived cell lines. (a) Western blot analysis of phosphorylated NF-kappa B p65, MC1-R, & TRP-1 in total cell lysates extracted from MeWo (a) or Mel1700 (b) cells either uninfected (control) or acutely infected with KSHV for 0.3 h, 1 h, 3 h, or 6 h. GAPDH was used as loading control. (c) ImageJ quantitation of the p65 band intensities in (a) & (b) relative to GAPDH controls. (d) Mel1700 cells were infected in 6-well plates with increasing volumes (mL/well) of concentrated supernatant containing infectious KSHV, & total RNA from infected cells was subjected to RT-PCR using primer sets for host anti-inflammatory MC1R, POMC, & SLC7A11. (e) Equal aliquots from the same RNA used in (d) were subjected to RT-PCR analysis for select viral latency & cell growth control genes (i.e., GPCR, LANA, & v-FLIP). (f) Western blot analysis of the melanoma cell marker, Melan A, & anti-inflammatory genes MC1-R, TRP1, & SLC7A11 in total cell lysates of uninfected (−) or chronically infected (+) long-term cultures of MeWo-KSHV & Mel1700-KSHV cells. GAPDH was used as an internal control for both the RT-PCR (e) & western blot assays. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/24701351), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-318_rabbit-polyclonal-xct-antibody-31020241621818.jpg)
![Western Blot: xCT Antibody - BSA Free [NB300-318] - A link between KSHV latency & the MC1-R signaling axis in skin-derived cell lines. (a) Western blot analysis of phosphorylated NF-kappa B p65, MC1-R, & TRP-1 in total cell lysates extracted from MeWo (a) or Mel1700 (b) cells either uninfected (control) or acutely infected with KSHV for 0.3 h, 1 h, 3 h, or 6 h. GAPDH was used as loading control. (c) ImageJ quantitation of the p65 band intensities in (a) & (b) relative to GAPDH controls. (d) Mel1700 cells were infected in 6-well plates with increasing volumes (mL/well) of concentrated supernatant containing infectious KSHV, & total RNA from infected cells was subjected to RT-PCR using primer sets for host anti-inflammatory MC1R, POMC, & SLC7A11. (e) Equal aliquots from the same RNA used in (d) were subjected to RT-PCR analysis for select viral latency & cell growth control genes (i.e., GPCR, LANA, & v-FLIP). (f) Western blot analysis of the melanoma cell marker, Melan A, & anti-inflammatory genes MC1-R, TRP1, & SLC7A11 in total cell lysates of uninfected (−) or chronically infected (+) long-term cultures of MeWo-KSHV & Mel1700-KSHV cells. GAPDH was used as an internal control for both the RT-PCR (e) & western blot assays. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/24701351), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-318_rabbit-polyclonal-xct-antibody-310202416212337.jpg)
![Immunohistochemistry: Caspase-8 Antibody - (active/cleaved) [NB100-56116] - Autophagy-deficient mice showed increased activity of apoptosis and necroptosis. Reduced pancreatic Atg7 level increased the expression of Caspase-8 in 12-week-old Atg7deltapan mice. Caspase-8 quantitation and representative IF microphotographs of Atg7F/F (n=5) and Atg7deltapan (n=5) pancreatic tissue stained for DAPI (blue) and Caspase-8 (green) ( 1/1000, scale bar=50 um). Image collected and cropped by CiteAb from the following publication (//www.nature.com/doifinder/10.1038/cddis.2017.313), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/Caspase-8-Antibody-active-cleaved-Immunohistochemistry-NB100-56116-img0009.jpg "Immunohistochemistry: Caspase-8 Antibody - (active/cleaved) [NB100-56116] - Autophagy-deficient mice showed increased activity of apoptosis and necroptosis. Reduced pancreatic Atg7 level increased the expression of Caspase-8 in 12-week-old Atg7deltapan mice. Caspase-8 quantitation and representative IF microphotographs of Atg7F/F (n=5) and Atg7deltapan (n=5) pancreatic tissue stained for DAPI (blue) and Caspase-8 (green) ( 1/1000, scale bar=50 um). Image collected and cropped by CiteAb from the following publication (//www.nature.com/doifinder/10.1038/cddis.2017.313), licensed under a CC-BY license.")
![Western Blot: Caspase-8 Antibody - (active/cleaved) [NB100-56116] - Analysis of active/cleaved Caspase 8 in NRK whole cell lysate using anti-active/cleaved Caspase 8 antibody. WB image submitted by a verified customer review.](http://images.novusbio.com/fullsize/Caspase-8-Antibody-active-cleaved-Western-Blot-NB100-56116-img0003.jpg)
![Immunohistochemistry-Paraffin: Caspase-8 Antibody - (active/cleaved) [NB100-56116] - Sections from a brain tumor tissue array stained for Caspase-8 expression using NB100-56116 at 1:2000. A. Anaplastic glioma (Grade III, left) and Gemistocytoma (Grade II, right) cores showing negative and positive staining for Caspase-8, respectively. B. Higher magnification of the Gemistocytoma tumor (from A).](http://images.novusbio.com/fullsize/Caspase-8-Antibody-active-cleaved-Immunohistochemistry-Paraffin-NB100-56116-img0004.jpg)
![Immunohistochemistry-Paraffin: Caspase-8 Antibody - (active/cleaved) [NB100-56116] - Sections from a brain tissue array stained for Caspase-8 expression using NB100-56116 at 1:2000. A. Normal brain stem (1) and cortex (2). B. Higher magnification of cortex (from A). C. Higher magnification of brain stem (from A). D. Normal cerebellum showing caspase-8 staining in the Purkinge cells.](http://images.novusbio.com/fullsize/Caspase-8-Antibody-active-cleaved-Immunohistochemistry-Paraffin-NB100-56116-img0005.jpg)
![Immunohistochemistry: Caspase-8 Antibody [NB100-56116] - Necroptosis marker p-MLKL can be detected in OA cartilage & after TNF/CHX stimulation.Exemplary images of impacted & differently stimulated cartilage explants after immunohistochemical staining of a cleaved CASP8, b RIPK3, & c p-MLKL. In addition, percentage of cleaved CASP8− (d) & p-MLKL− (e) positive cells was quantified (n = 3). Images were acquired using a 20× objective; the bars represent 200 µm Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31527653), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-56116_rabbit-polyclonal-caspase-8-antibody-active-cleaved-imgenex-img-5703-310202415392576.jpg)
![Immunohistochemistry: Caspase-8 Antibody [NB100-56116] - Expression of necroptosis- & apoptosis-related markers is elevated in OA cartilage.Necroptosis- & apoptosis-related markers in highly degenerated cartilage tissue of OA patients (ICRS grade ≥ 3) were determined by a gene expression analysis of apoptosis & necroptosis markers as well as immunohistochemical analysis (IHC) of b cleaved CASP8, c RIPK3, & d p-MLKL. Macroscopically intact cartilage (ICRS grade ≤ 1) served as control. Bars in the IHC images represent 200 µm. Statistical analysis was performed by an unpaired multiple t test; error bars indicate median & range from min to max; n = 13. Significant differences between groups were depicted as: *P < 0.05, **P < 0.01, ***P < 0.001, ****P < 0.0001 Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31527653), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-56116_rabbit-polyclonal-caspase-8-antibody-active-cleaved-imgenex-img-5703-310202415394549.jpg)
![Immunocytochemistry/ Immunofluorescence: Caspase-8 Antibody [NB100-56116] - Analysis of the cell type susceptible to apoptotic cell death in the hypothalamus of IRS2−/− mice. Immunoblots probed with antibodies against GFAP (A) & Tuj-1 (B) in the hypothalamus of wild-type (WT), non-diabetic IRS2-deficient (ND IRS2−/−) & diabetic IRS2-deficient (D IRS2−/−) mice. The average of three independent assays performed in duplicate is shown. Statistical significance by ANOVA: *P<0.05 vs WT mice. n=6/group. (C) Colocalization of TUNEL & GFAP in the hypothalamus of WT, ND IRS2−/− & D IRS2−/− mice. Arrows indicate astrocytes with apoptotic nuclei. (D) Colocalization of cleaved caspase-8 & GFAP, & of cleaved caspase-8 & NeuN, in the hypothalamus of WT, ND IRS2−/− & D IRS2−/− mice. Arrows indicate colocalization of GFAP & cleaved caspase-8. Scale bar: 50 µm; inset, 100 µm. Image collected & cropped by CiteAb from the following publication (//journals.biologists.com/dmm/article/doi/10.1242/dmm.023515/257174/Increased-oxidative-stress-and-apoptosis-in-the), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-56116_rabbit-polyclonal-caspase-8-antibody-active-cleaved-imgenex-img-5703-31020241683918.jpg)