| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NBP2-27103SS | |||
| Azide and BSA Free | NBP2-80749 | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB300-318SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB100-2288SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB100-56113SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB100-2219SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB110-39113SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| Non-Recombinant Monoclonal | NB600-1159SS | |||
| Azide and BSA Free | NBP2-33250 | |||
| Non-Recombinant Monoclonal | NB600-1159 | |||
| BSA Free | NBP3-07012SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB100-56565SS | |||
| Azide and BSA Free | NBP2-33230 | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB110-40877SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB600-582SS | |||
| Azide and BSA Free | NBP2-80959 | |||
![Immunocytochemistry/Immunofluorescence: GAPDH Antibody (13H12) [NBP2-27103] - GAPDH antibody was tested in HeLa cells with Dylight 488 (green). Nuclei and alpha-tubulin were counterstained with DAPI (blue) and Dylight 550 (red). A dilution of 1:10 was used. Image objective 40x.](http://images.novusbio.com/fullsize/GAPDH-Antibody-13H12-Immunocytochemistry-Immunofluorescence-NBP2-27103-img0013.jpg "Immunocytochemistry/Immunofluorescence: GAPDH Antibody (13H12) [NBP2-27103] - GAPDH antibody was tested in HeLa cells with Dylight 488 (green). Nuclei and alpha-tubulin were counterstained with DAPI (blue) and Dylight 550 (red). A dilution of 1:10 was used. Image objective 40x.")
![Western Blot: GAPDH Antibody (13H12) [NBP2-27103] - WB detection of GAPDH protein (theoretical molecular weight: 36 kDa) in HeLa cells lysate using GAPDH antibody (clone 13H12) in (A) the absence and (B) the presence of immunizing peptide.](http://images.novusbio.com/fullsize/GAPDH-Antibody-13H12-Western-Blot-NBP2-27103-img0001.jpg)
![Immunohistochemistry-Paraffin: GAPDH Antibody (13H12) [NBP2-27103] - IHC-P detection GAPDH protein in a formalin-fixed paraffin-embedded section of human rectal carcinoma tissue using GAPDH antibody (clone 13H12) at 5 ug/ml concentration.](http://images.novusbio.com/fullsize/GAPDH-Antibody-13H12-Immunohistochemistry-Paraffin-NBP2-27103-img0011.jpg)
![Immunohistochemistry-Paraffin: GAPDH Antibody (13H12) [NBP2-27103] - IHC-P detection GAPDH protein in a formalin-fixed paraffin-embedded section of normal human breast tissue using GAPDH antibody (clone 13H12) at 5 ug/ml concentration.](http://images.novusbio.com/fullsize/GAPDH-Antibody-13H12-Immunohistochemistry-Paraffin-NBP2-27103-img0008.jpg)
![Western Blot: GAPDH Antibody (13H12) [NBP2-27103] - Characterization of lncR492.(B) Northern blot of lncR494 using increasing amounts of loaded total. Black arrow signifies lncR492-specific signal at approximately 1400 bp. A probe targeting Gapdh mRNA served as the loading control. (D) RT-PCR analysis of lncR492 and Gapdh expression. RNA extract was treated with a 5'-phosphate-dependent exonuclease, resulting in a degradation of f.ex. ribosomal RNA.Citation: Winzi M, Casas Vila N, Paszkowski-Rogacz M, Ding L, Noack S, Theis M, et al. (2018) The long noncoding RNA lncR492 inhibits neural differentiation of murine embryonic stem cells. PLoS ONE 13(1): e0191682. //doi.org/10.1371/journal.pone.0191682](http://images.novusbio.com/fullsize/GAPDH-Antibody-13H12-Western-Blot-NBP2-27103-img0017.jpg)
![Western Blot: GAPDH Antibody (13H12) [NBP2-27103] - Serum from trauma patients induces intrinsic apoptosis resistance by up-regulating AAT expression in neutrophils. AAT protein expression was analyzed in neutrophils after 18 h of culture by western blot analysis. Relative expression was quantified vs. GAPDH expression. One representative blot of five independent experiments is depicted. **p<0.01 (one-way ANOVA with Newman keuls post-hoc test). Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0177450), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/GAPDH-Antibody-13H12-Western-Blot-NBP2-27103-img0018.jpg)
![Western Blot: GAPDH Antibody (13H12) [NBP2-27103] - WB detection of GAPDH protein (theoretical molecular weight 36 kDa) in lysates of Mouse cell lines (A) NIH 3T3 (B) RAW 264.7 using GAPDH antibody (clone 13H12) at a concentration of 0.25 ug/ml.](http://images.novusbio.com/fullsize/GAPDH-Antibody-13H12-Western-Blot-NBP2-27103-img0005.jpg)
![Western Blot: GAPDH Antibody (13H12) [NBP2-27103] - analysis of GAPDH in HeLa and HEK 293 cells (25ug/lane) using anti-GAPDH antibody. Image from verified customer review.](http://images.novusbio.com/fullsize/GAPDH-Antibody-13H12-Western-Blot-NBP2-27103-img0014.jpg)
![Immunohistochemistry-Paraffin: GAPDH Antibody (13H12) [NBP2-27103] - IHC-P detection GAPDH protein in a formalin-fixed paraffin-embedded section of normal human stomach tissue using GAPDH antibody (clone 13H12) at 5 ug/ml concentration.](http://images.novusbio.com/fullsize/GAPDH-Antibody-13H12-Immunohistochemistry-Paraffin-NBP2-27103-img0007.jpg)
![Immunohistochemistry-Paraffin: GAPDH Antibody (13H12) [NBP2-27103] - IHC-P detection GAPDH protein in a formalin-fixed paraffin-embedded section of human colon tissue using GAPDH antibody (clone 13H12) at 5 ug/ml concentration.](http://images.novusbio.com/fullsize/GAPDH-Antibody-13H12-Immunohistochemistry-Paraffin-NBP2-27103-img0009.jpg)
![Immunohistochemistry-Paraffin: GAPDH Antibody (13H12) [NBP2-27103] - IHC-P detection GAPDH protein in a formalin-fixed paraffin-embedded tissue section of human esophageal squamous cell carcinoma (SCC) using GAPDH antibody (clone 13H12) at 5 ug/ml concentration.](http://images.novusbio.com/fullsize/GAPDH-Antibody-13H12-Immunohistochemistry-Paraffin-NBP2-27103-img0010.jpg)
![Simple Western: GAPDH Antibody (13H12) [NBP2-27103] - GAPDH/G3PDH Antibody (13H12) [NBP2-27103] - Simple Western lane view shows a specific band for GAPDH in 0.1 mg/ml of HeLa lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system.](http://images.novusbio.com/fullsize/GAPDH-Antibody-13H12-Simple-Western-NBP2-27103-img0015.jpg)
![Western Blot: GAPDH Antibody (13H12) - BSA Free [NBP2-27103] - Effect of AAT on Mcl-1 phosphorylation, the activity of MAP kinases & caspases.Neutrophils from healthy volunteers (2.5 × 106/ml) were cultured in medium supplemented with patient serum (3 mg protein/ml; 1%) & those containing low levels of AAT (AAT-reduce serum; 1%) in the presence of STS (0.2 μM). After 3 h, the expression of pMcl-1 (A, n = 7), pAkt (B, n = 8) & pERK1/2 (C, n = 10) were analyzed by western blot. Expression levels of the phosphorylated proteins were normalized to that of the unphosphorylated forms. GAPDH was used as loading control. One representative blot is displayed. *p<0.05; **p<0.01; n.s. = not significant. D. After 4 h of incubation the activities of caspase-9 & caspase-3/-7 were quantified. Results are presented as means ± SEM of eight independent experiments. No significant differences were found (one-way ANOVA with Newman keuls post-hoc test). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28493974), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nbp2-27103_mouse-monoclonal-gapdh-antibody-13h12-imgenex-img-6665a-25-31020241612222.jpg)
![Western Blot: GAPDH Antibody (13H12) - BSA Free [NBP2-27103] - Effect of AAT on Mcl-1 phosphorylation, the activity of MAP kinases & caspases.Neutrophils from healthy volunteers (2.5 × 106/ml) were cultured in medium supplemented with patient serum (3 mg protein/ml; 1%) & those containing low levels of AAT (AAT-reduce serum; 1%) in the presence of STS (0.2 μM). After 3 h, the expression of pMcl-1 (A, n = 7), pAkt (B, n = 8) & pERK1/2 (C, n = 10) were analyzed by western blot. Expression levels of the phosphorylated proteins were normalized to that of the unphosphorylated forms. GAPDH was used as loading control. One representative blot is displayed. *p<0.05; **p<0.01; n.s. = not significant. D. After 4 h of incubation the activities of caspase-9 & caspase-3/-7 were quantified. Results are presented as means ± SEM of eight independent experiments. No significant differences were found (one-way ANOVA with Newman keuls post-hoc test). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28493974), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nbp2-27103_mouse-monoclonal-gapdh-antibody-13h12-imgenex-img-6665a-25-310202416114762.jpg)
![Western Blot: GAPDH Antibody (13H12) - BSA Free [NBP2-27103] - Effect of AAT on Mcl-1 phosphorylation, the activity of MAP kinases & caspases.Neutrophils from healthy volunteers (2.5 × 106/ml) were cultured in medium supplemented with patient serum (3 mg protein/ml; 1%) & those containing low levels of AAT (AAT-reduce serum; 1%) in the presence of STS (0.2 μM). After 3 h, the expression of pMcl-1 (A, n = 7), pAkt (B, n = 8) & pERK1/2 (C, n = 10) were analyzed by western blot. Expression levels of the phosphorylated proteins were normalized to that of the unphosphorylated forms. GAPDH was used as loading control. One representative blot is displayed. *p<0.05; **p<0.01; n.s. = not significant. D. After 4 h of incubation the activities of caspase-9 & caspase-3/-7 were quantified. Results are presented as means ± SEM of eight independent experiments. No significant differences were found (one-way ANOVA with Newman keuls post-hoc test). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28493974), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nbp2-27103_mouse-monoclonal-gapdh-antibody-13h12-imgenex-img-6665a-25-310202416121949.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)
![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)
![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)
![Immunohistochemistry: Caspase-3 Antibody - (active/cleaved) [NB100-56113] - Immunohistochemistry analysis of sectioned tumor tissues from the MDA-MB-231 study. Each section was subjected to the specified antibody followed by a biotinylated secondary antibody. Detection was done using a DAB Peroxidase HRP Substrate Kit (brown) followed by Hematoxylin counterstaining (purple). Images were obtained using inverted bright field microscopy. Sectioning results are representative of three individual tumors. Scale bar is 50 microns. Statistical analysis using One-Way ANOVA. *p<0.05 vs tumor volume of the control. Image collected and cropped by CiteAb from the following publication (nature.com/articles/s41598-017-01230-4), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/Caspase-3-Antibody-active-cleaved-Immunohistochemistry-NB100-56113-img0005.jpg "<b>Biological Strategies Validation. </b>Immunohistochemistry: Caspase-3 Antibody - (active/cleaved) [NB100-56113] - Immunohistochemistry analysis of sectioned tumor tissues from the MDA-MB-231 study. Each section was subjected to the specified antibody followed by a biotinylated secondary antibody. Detection was done using a DAB Peroxidase HRP Substrate Kit (brown) followed by Hematoxylin counterstaining (purple). Images were obtained using inverted bright field microscopy. Sectioning results are representative of three individual tumors. Scale bar is 50 microns. Statistical analysis using One-Way ANOVA. *p<0.05 vs tumor volume of the control. Image collected and cropped by CiteAb from the following publication (nature.com/articles/s41598-017-01230-4), licensed under a CC-BY license.")
![<b>Biological Strategies Validation. </b>Western Blot: Caspase-3 Antibody - (active/cleaved) [NB100-56113] - The protein expression levels of Bcl-2, Bax and cleaved caspase-3 were detected in the different groups using Western blotting and were normalized to the housekeeping gene GAPDH. Image collected and cropped by CiteAb from the following publication (onlinelibrary.wiley.com/doi/abs/10.1111/jcmm.14135), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/Caspase-3-Antibody-active-cleaved-Western-Blot-NB100-56113-img0006.jpg)
![Western Blot: Caspase-3 Antibody - (active/cleaved) [NB100-56113] - Cell apoptosis was detected by flow cytometric analysis, and the percentage of apoptotic cells transfected with miR-200c inhibitor or NC inhibitor and treated with AngII or PBS for 48 h was determined. Image collected and cropped by CiteAb from the following publication (onlinelibrary.wiley.com/doi/abs/10.1111/jcmm.14135), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/Caspase-3-Antibody-active-cleaved-Western-Blot-NB100-56113-img0007.jpg)
![Immunohistochemistry-Paraffin: Caspase-3 Antibody - (active/cleaved) [NB100-56113] - Dog ischemic brain stained for Active/Cleaved Caspase-3 expression using Caspase-3 Antibody - (active/cleaved)( NB100-56113) at 1:2000. Staining is seen in the nuclei of dying neurons (black arrow) but not in the morphologically normal nuclei (open arrows). Caspase-3 expression in the nucleus is considered to be a marker of active/caspase-3 expression and apoptosis. Hematoxylin-eosin counterstain.](http://images.novusbio.com/fullsize/Caspase-3-Antibody-active-cleaved-Immunohistochemistry-Paraffin-NB100-56113-img0003.jpg)
![Immunohistochemistry-Paraffin: Caspase-3 Antibody - (active/cleaved) [NB100-56113] - Irradiated mouse spleen stained for Active/Cleaved Caspase-3 expression using Caspase-3 Antibody - (active/cleaved) (NB100-56113) at 1:2000. Staining is seen in the nuclei of a subset of the cell population. Caspase-3 expression in the nucleus is considered to be a marker of active/caspase-3 expression and apoptosis. Hematoxylin-eosin counterstain.](http://images.novusbio.com/fullsize/Caspase-3-Antibody-active-cleaved-Immunohistochemistry-Paraffin-NB100-56113-img0004.jpg)
![Immunohistochemistry: Caspase-3 Antibody - (active/cleaved) [NB100-56113] - Pathology in DOX treated acute & recovery phase mice. Regions of myofiber loss & frank replacement fibrosis were noted, most commonly in atria (A, acute phase), & rarely in ventricles (D, recovery phase). These areas were accompanied by macrophage infiltration (B, E) & myofibroblast proliferation (C) consistent with fibroplasia. Rare myofibers were matrix metalloproteinase 2 (F, recovery phase animal) or caspase-3 positive (G, acute phase animal). Reticulin staining (A, D); Immunohistochemistry: Iba 1(B, E; macrophages), alpha SMA (C), MMP-2 (F) & cleaved caspase -3 (G) Bar = 100µm (A-C); 50µm (D-F); 20µm (G). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31263061), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-56113_rabbit-polyclonal-caspase-3-antibody-active-cleaved-31020241530428.jpg)
![Western Blot: Caspase-3 Antibody - (active/cleaved) [NB100-56113] - Antidepressants-mediated effect on cellular protein content. HT-22 cells were treated with antidepressants for 48 & 96 h & densitometry analysis of NF-kappa B (b), p16 (c), p21 (d), p27 (e), p53 (f), TRF1 (g), TRF2 (h), calnexin (i), NuMa (j), cleaved caspase 3 (k), Bcl-2 (l) was evaluated. Representative Western Blots are presented (a). Bars indicate SD, n = 3, ***/^^^p < 0.001, **/^^p < 0.01, */^p < 0.05, no indication—no statistical significance (one-way ANOVA & Dunnett’s a posteriori test) Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31278507), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-56113_rabbit-polyclonal-caspase-3-antibody-active-cleaved-310202415175224.jpg)
![Immunocytochemistry/ Immunofluorescence: Caspase-3 Antibody - (active/cleaved) [NB100-56113] - Morphological changes & expression of key apoptosis-related molecules in 4T1 cells after DE-EDCP treatment(A) Morphological changes of 4T1 cells exposed to various concentrations of DE-EDCP for 24h. (B) Immunofluorescence staining for Bcl-2 (green), Bax (green) & cleaved caspase-3 (green) together with DNA staining with DAPI (blue) in 4T1 cells incubated with DE-EDCP or cisplatin (31.25 μM) for 24h, as well as in untreated cells (magnification at x200). (C) mRNA expression of Bcl-2, Bax & caspase-3 quantified by RT-PCR in 4T1 cells after DE-EDCP 24h treatment. DE-EDCP treatment markedly increased the expression of Bax & caspase-3 mRNA & decreased the expression of Bcl-2 mRNA in 4T1 cells. beta -actin mRNA was used as an internal control. Data points are represented by the expression ratio & mean±SD fold of control in 4T1 cells. (* Bcl-2-: DE-EDCP vs. untreated p=0.03; DE-EDCP vs. cisplatin p=0.006; cislatin vs. untreated p=0.001; Bax-: DE-EDCP vs. untreated p=0.011; cislatin vs. untreated p=0.009; caspase-3-: DE-EDCP vs. untreated p=0.015; DE-EDCP vs. cisplatin p=0.021) Image collected & cropped by CiteAb from the following publication (//www.oncotarget.com/lookup/doi/10.18632/oncotarget.25610), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-56113_rabbit-polyclonal-caspase-3-antibody-active-cleaved-31020241682116.jpg)
![Immunohistochemistry: EGLN1/PHD2 Antibody [NB100-2219] - IHC and Immunofluorescence of wounded tissue and normal unwounded skin. Representative images for immunofluorescent staining of PHD-2 on healed wounded skin and adjacent normal unwounded skin of wild type, heterozygous K14-Cre/homozygous floxed PHD-2, and heterozygous Col1 alpha2-Cre-ER/homozygous floxed PHD-2 mice at 400x magnification. Image collected and cropped by CiteAb from the following publication (//doi.org/10.1371/journal.pone.0093373), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/EGLN1-PHD2-Antibody-Immunohistochemistry-NB100-2219-img0015.jpg "Immunohistochemistry: EGLN1/PHD2 Antibody [NB100-2219] - IHC and Immunofluorescence of wounded tissue and normal unwounded skin. Representative images for immunofluorescent staining of PHD-2 on healed wounded skin and adjacent normal unwounded skin of wild type, heterozygous K14-Cre/homozygous floxed PHD-2, and heterozygous Col1 alpha2-Cre-ER/homozygous floxed PHD-2 mice at 400x magnification. Image collected and cropped by CiteAb from the following publication (//doi.org/10.1371/journal.pone.0093373), licensed under a CC-BY license.")
![<b>Genetic Strategies Validation. </b>Western Blot: EGLN1/PHD2 Antibody [NB100-2219] - In vitro analysis of PHD-2 knockout and protein quantification.Western blot data for PHD-2 knockout in fibroblasts of heterozygous Col1 alpha2-Cre-ER/homozygous floxed PHD-2 mice compared to wild type mice (*p<0.05). D') Western blot data for PHD-2 knockout in keratinocytes of heterozygous K14-Cre/homozygous floxed PHD-2 mice compared to wild type mice (*p<0.05). Image collected and cropped by CiteAb from the following publication (//doi.org/10.1371/journal.pone.0093373), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/EGLN1-PHD2-Antibody-Knockdown-Validated-NB100-2219-img0016.jpg)
![Immunohistochemistry-Paraffin: EGLN1/PHD2 Antibody [NB100-2219] - Analysis of an FFPE mouse lung section using 1:200 dilution of EGLN1/PHD2 antibody. The staining was developed using HRP conjugated anti-rabbit secondary antibody and DAB reagent. The antibody generated a specific staining in the cytoplasm and nuclei of alveolar as well as bronchiolar epithelial cells. Cytoplasmic staining was observed in almost all cells while the nuclear positivity was seen in a subset of cells only.](http://images.novusbio.com/fullsize/EGLN1-PHD2-Antibody-Immunohistochemistry-Paraffin-NB100-2219-img0014.jpg)
![Western Blot: EGLN1/PHD2 Antibody [NB100-2219] - Detection of EGLN1/PHD2 in mouse kidney lysate. ECL exposure, 20 seconds.](http://images.novusbio.com/fullsize/EGLN1-PHD2-Antibody-Western-Blot-NB100-2219-img0013.jpg)
![Immunocytochemistry/Immunofluorescence: EGLN1/PHD2 Antibody [NB100-2219] - EGLN1/PHD2 antibody at 1:500 in HeLa cells with DyLight 488 (green). Nuclei and alpha-tubulin were counterstained with DAPI (blue) and DyLight 550 (red).](http://images.novusbio.com/fullsize/EGLN1-PHD2-Antibody-Immunocytochemistry-Immunofluorescence-NB100-2219-img0012.jpg)
![Immunocytochemistry/Immunofluorescence: EGLN1/PHD2 Antibody [NB100-2219] - Analysis of EGLN1/PHD2 in ARPE-19 cells using anti-PHD2 antibody. ICC/IF image submitted by a veriifed customer review.](http://images.novusbio.com/fullsize/EGLN1-PHD2-Antibody-Immunocytochemistry-Immunofluorescence-NB100-2219-img0009.jpg)
![Immunohistochemistry: EGLN1/PHD2 Antibody [NB100-2219] - Staining of renal tubular epithelium in mouse using NB100-2219 at 2.5 ug/mL.](http://images.novusbio.com/fullsize/EGLN1-PHD2-Antibody-Immunohistochemistry-NB100-2219-img0010.jpg)
![Western Blot: Glut1 Antibody [NB110-39113] - PrP-mediated increase in IC iron downregulates glucose transporters in the brain, neuroretina, and the liver: A similar evaluation of retinal lysates shows upregulation of Glut1 in PrP-/- relative to Tg40 PrP samples (lanes 1 & 3). Iron overloading downregulates Glut1 in Tg40 PrP samples relative to untreated controls, but has minimal effect on similarly treated PrP-/- samples (lanes 2 & 4). Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/s41598-018-24786-1) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/Glut1-Antibody-Western-Blot-NB110-39113-img0019.jpg "<b>Biological Strategies Validation. </b>Western Blot: Glut1 Antibody [NB110-39113] - PrP-mediated increase in IC iron downregulates glucose transporters in the brain, neuroretina, and the liver: A similar evaluation of retinal lysates shows upregulation of Glut1 in PrP-/- relative to Tg40 PrP samples (lanes 1 & 3). Iron overloading downregulates Glut1 in Tg40 PrP samples relative to untreated controls, but has minimal effect on similarly treated PrP-/- samples (lanes 2 & 4). Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/s41598-018-24786-1) licensed under a CC-BY license.")
![<b>Biological Strategies Validation. </b>Western Blot: Glut1 Antibody [NB110-39113] - Western blot of GLUT1 on mouse kidney membrane protein (lane A) and rat kidney membrane protein (lane B).](http://images.novusbio.com/fullsize/Glut1-Antibody-Western-Blot-NB110-39113-img0006.jpg)
![Immunohistochemistry-Paraffin: Glut1 Antibody [NB110-39113] - Immunohistochemical analysis of FFPE tissue section of human placenta using 1:200 dilution of Glut1 antibody. The staining was developed using HRP-DAB detection method and the sections were further counterstained with hematoxylin. This antibody generated a specific strong membrane cytoplasmic staining of Glut1 primarily in the syncytiotrophoblast layers of various villi and in the red blood cells (RBCs). Cytotrophoblasts showed a very weak expression of this protein.](http://images.novusbio.com/fullsize/Glut1-Antibody-Immunohistochemistry-Paraffin-NB110-39113-img0011.jpg)
![Flow Cytometry: Glut1 Antibody [NB110-39113] - An intracellular stain was performed on HepG2 with NB110-39113 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/Glut1-Antibody-Flow-Cytometry-NB110-39113-img0018.jpg)
![Immunocytochemistry/Immunofluorescence: Glut1 Antibody [NB110-39113] - HepG2 cells were fixed for 10 minutes using 10% formalin and then permeabilized for 5 minutes using 1X TBS + 0.5% Triton X-100. The cells were incubated with anti-GLUT1 at a 1:200 dilution overnight at 4C and detected with an anti-rabbit DyLight 488 (Green) at a 1:500 dilution. Alpha tubulin (DM1A) NB100-690 was used as a co-stain at a 1:1000 dilution and detected with an anti-mouse DyLight 550 (Red) at a 1:500 dilution. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 40X objective](http://images.novusbio.com/fullsize/Glut1-Antibody-Immunocytochemistry-Immunofluorescence-NB110-39113-img0013.jpg)
![Western Blot: Glut1 Antibody [NB110-39113] - Analysis of HeLa lysates using NB110-39113. Image courtesy of Gregg Semenza (PMID: 21620138).](http://images.novusbio.com/fullsize/Glut1-Antibody-Western-Blot-NB110-39113-img0007.jpg)
![Western Blot: Glut1 Antibody [NB110-39113] - Glut1 in human brain lysate (55 kDa). Antibody at 1:500. Western blot image submitted by a verified customer review.](http://images.novusbio.com/fullsize/Glut1-Antibody-Western-Blot-NB110-39113-img0016.jpg)
![<b>Biological Strategies Validation. </b>Flow Cytometry: Glut1 Antibody [NB110-39113] - Flow cytometry analysis using the PE conjugate of NB110-39113. Staining of Glut 1 expression on CD4+ T cells stimulated with anti-CD3/CD28 beads and insulin (1ug/mL) for 5 days in culture media with additional glucose provided. FMO control (red) and isotype control (blue, NBP2-24983) were compared to CD4+ T cells (orange), and this PE conjugated Glut 1 antibody positively stained CD4+ lymphocytes isolated from Mouse. Flow cytometry image submitted by a verified customer review.](http://images.novusbio.com/fullsize/Glut1-Antibody-Flow-Cytometry-NB110-39113-img0014.jpg)
![Immunocytochemistry/ Immunofluorescence: Glut1 Antibody - BSA Free [NB110-39113] - LAIR-1 inhibits Glut1-related glucose uptake in OS cells. a Heatmap showing the levels of differentially expressed mRNAs. b Top 20 KEGG pathway annotation categories for target gene functions of predicted mRNAs. c Selected significantly differentially expressed mRNA-related to EMT in RNA-seq data between two groups, ***P < 0.001. d qPCR validation of differentially expressed EMT-related genes in LV-NC & LV-LAIR-1-overexpressing OS cells, **P < 0.01. e Glut1 expression analyzed by western blotting. f Immunofluorescence staining of Glut1 in the LV-LAIR-1-overexpressing OS cells. Scale bar = 50 μm. Data were obtained from at least two independent experiments. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32563267), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-39113_rabbit-polyclonal-glut1-antibody-310202415175286.jpg)
![Western Blot: Glut1 Antibody - BSA Free [NB110-39113] - LAIR-1 inhibits Glut1-related glucose uptake in OS cells. a Heatmap showing the levels of differentially expressed mRNAs. b Top 20 KEGG pathway annotation categories for target gene functions of predicted mRNAs. c Selected significantly differentially expressed mRNA-related to EMT in RNA-seq data between two groups, ***P < 0.001. d qPCR validation of differentially expressed EMT-related genes in LV-NC & LV-LAIR-1-overexpressing OS cells, **P < 0.01. e Glut1 expression analyzed by western blotting. f Immunofluorescence staining of Glut1 in the LV-LAIR-1-overexpressing OS cells. Scale bar = 50 μm. Data were obtained from at least two independent experiments. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32563267), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-39113_rabbit-polyclonal-glut1-antibody-310202415334922.jpg)
![Simple Western: Glut1 Antibody - BSA Free [NB110-39113] - Protein changes in ONHAs corroborate bioenergetics data. (A) Glucose transporter-1 protein levels in Stretched ONH astrocytes are significantly higher than Control (*p = 0.0225, n = 7 Control, n = 8 Stretch). Retinal lysate from a 2 month-old mouse was used as a positive control for each protein analyzed, while negative control was the signal obtained when no primary antibody was included in the capillary. (B) Lactate dehydrogenase-A, the astrocyte-specific isoform of the enzyme that catalyzes the interconversion of pyruvate & lactate, has equivalent protein levels in Control & Stretch ONH astrocytes. (C) Glucose-6-phosphate dehydrogenase, the enzyme that shunts glucose into the pentose phosphate pathway, is no different in Control & Stretch ONH astrocytes. (D) Glutamine synthetase, the enzyme that synthesizes glutamine from glutamate, is no different in Control & Stretch ONH astrocytes. (E) The monomeric form of glutamate-aspartate transporter (GLAST) has significantly higher protein levels in the Stretch as compared to the Control ONH astrocytes (p = 0.020; n = 4 Control, n = 5 Stretch). (F) GLAST dimer protein levels are no different in Control & Stretch ONH astrocytes. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35992925), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-39113_rabbit-polyclonal-glut1-antibody-310202416284917.jpg)
![Western Blot: Noxa Antibody (114C307.1R) [NBP3-07012] - Doc counteracts the ABT-737-mediated increase in Mcl-1 protein. Western blot showing treatment of LNCaP and PC3 cells with 1 uM ABT-737. In LNCaP and PC3, there are few difference in Noxa. Image collected and cropped by CiteAb from the following publication (//peerj.com/articles/144), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/Noxa-Antibody-114C307-1R-Western-Blot-NBP3-07012-img0003.jpg "Western Blot: Noxa Antibody (114C307.1R) [NBP3-07012] - Doc counteracts the ABT-737-mediated increase in Mcl-1 protein. Western blot showing treatment of LNCaP and PC3 cells with 1 uM ABT-737. In LNCaP and PC3, there are few difference in Noxa. Image collected and cropped by CiteAb from the following publication (//peerj.com/articles/144), licensed under a CC-BY license.")
![Immunocytochemistry/Immunofluorescence: Noxa Antibody (114C307.1R) [NBP3-07012] - ICC/IF analysis using the azide-free version of NB600-1159 at 1:10. HeLa cells with DyLight 488 (green). Nuclei and alpha-tubulin were counterstained with DAPI (blue) and DyLight 550 (red). Image objective 40X.](http://images.novusbio.com/fullsize/Noxa-Antibody-114C307-1R-Immunocytochemistry-Immunofluorescence-NBP3-07012-img0004.jpg)
![Flow Cytometry: Noxa Antibody (114C307.1R) [NBP3-07012] - An intracellular stain was performed on Ntera2 cells with Noxa Antibody [114C307.1R] NBP3-07012 (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 1.0 ug/mL for 30 minutes at room temperature, followed by Mouse IgG (H+L) Cross-Adsorbed Secondary Antibody, Dylight 550 (35503, Thermo Fisher).](http://images.novusbio.com/fullsize/Noxa-Antibody-114C307-1R-Flow-Cytometry-NBP3-07012-img0002.jpg)
![Immunocytochemistry/Immunofluorescence: Noxa Antibody (114C307.1R) [NBP3-07012] - HeLa 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 anti-Noxa Antibody (114C307.1R) NBP3-07012 at 2 ug/ml overnight at 4C and detected with an anti-mouse Dylight 488 (Green) at a 1:1000 dilution for 60 minutes. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 100X objective and digitally deconvolved.](http://images.novusbio.com/fullsize/Noxa-Antibody-114C307-1R-Immunocytochemistry-Immunofluorescence-NBP3-07012-img0001.jpg)
![Immunohistochemistry-Paraffin: Noxa Antibody (114C307.1R) - BSA Free [NBP3-07012] - Immunohistochemical analysis of bouin-fixed, paraffin-embedded chronic lymphocytic leukemia (CLL) xenograft stained with Noxa antibody (1:2000), peroxidase-conjugate and DAB chromogen. Staining for 2 hr at RT was used.](http://images.novusbio.com/fullsize/nbp3-07012_mouse-monoclonal-noxa-antibody-114c307-1r-1772024104467.jpg)
![Western Blot: Noxa Antibody (114C307.1R) - BSA Free [NBP3-07012] - Detection by Western blot in RL-7 cells (a follicular lymphoma).](http://images.novusbio.com/fullsize/nbp3-07012_mouse-monoclonal-noxa-antibody-114c307-1r-1772024959411.jpg)
![Flow Cytometry: Noxa Antibody (114C307.1R) - BSA Free [NBP3-07012] - Flow cytometry after an intracellular stain was performed on MCF7 cells with Noxa [114C307.1] antibody NB600-1159AF700 (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 directly conjugated to Alexa Fluor 700.](http://images.novusbio.com/fullsize/nbp3-07012_mouse-monoclonal-noxa-antibody-114c307-1r-1772024959421.jpg)
![Flow Cytometry: Noxa Antibody (114C307.1R) - BSA Free [NBP3-07012] - Flow cytometry after an intracellular stain was performed on HeLa cells with Noxa [114C307.1] antibody NB600-1159AF700 (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 directly conjugated to Alexa Fluor 700.](http://images.novusbio.com/fullsize/nbp3-07012_mouse-monoclonal-noxa-antibody-114c307-1r-17720249362613.jpg)
![<b>Biological Strategies Validation. </b>P. gingivalis and its OMVs differentially induce inflammasome signaling and pyroptosis in murine macrophages. BMM were infected as before (2 h at MOI of 25:1, see Materials and Methods) with viable P. gingivalis (Pg), heat-killed-Pg (HK-Pg), OMVs, or heat-inactivated-OMVs (HI-OMVs) and the activation of inflammasome components in the lysates [or supernatants (sup) where indicated] measured after 24 h by Western blot; beta-actin serves as a loading control throughout. Western blot data are representative of at least three independent experiments. Image collected and cropped by CiteAb from the following publication (//journal.frontiersin.org/article/10.3389/fcimb.2017.00351/full), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/Caspase-1-Antibody-14F468-Western-Blot-NB100-56565-img0015.jpg)
![Detection of Caspase-1 protein in a section of normal human colon using 5 ug/ml concentration of Caspase 1 antibody (clone 14F468). Distinct cytoplasmic staining along with some nuclear positivity was observed in crypts/mucosa, and staining was found to be more intense in the absorptive columnar epithelial cells. [10X Magnification]](http://images.novusbio.com/fullsize/Caspase-1-Antibody-14F468-Immunohistochemistry-Paraffin-NB100-56565-img0009.jpg)
![Normal lung from human using 5 ug/ml concentration of Caspase 1 antibody (clone 14F468). In this representative lung section, different type of cells including pseudostratified columnar epithelium of bronchiole and the simple squamous epithelium of alveoli may be seen to develop immunoreactivity for Caspase 1. [10X Magnification]](http://images.novusbio.com/fullsize/Caspase-1-Antibody-14F468-Immunohistochemistry-Paraffin-NB100-56565-img0010.jpg)
![Normal skin from human using 5 ug/ml concentration of Caspase 1 antibody (clone 14F468). Strong cytoplasmic/nuclear staining developed in all the epidermal cells, blood vessels and some cells of the dermal connective tissues layer. [10X Magnification]](http://images.novusbio.com/fullsize/Caspase-1-Antibody-14F468-Immunohistochemistry-Paraffin-NB100-56565-img0011.jpg)
![Western Blot: Caspase-1 Antibody (14F468) - BSA Free [NB100-56565] - Glucose fluctuations promoted the activation of NLRP3 inflammasome. (A) Immunofluorescence staining of NLRP3-ASC interaction in rat hearts. The heart sections were labeled with anti-NLRP3 (red), anti-ASC (green), & DAPI (blue) (n = 3 per group). (B–D) The mRNA levels of NLRP3, IL-1 beta & IL-18 in rat hearts of the three groups (n = 4 per group). (E–H) The protein expressions of NLRP3, ASC & cleaved caspase-1 in rat hearts of the three groups (n = 4 per group). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35592403), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-56565_mouse-monoclonal-caspase-1-antibody-14f468-310202415175246.jpg)
![Western Blot: Caspase-1 Antibody (14F468) - BSA Free [NB100-56565] - Caspase-1 expression increases with age in human fibroblasts: a Immunoblot analysis of caspase-1 & ASC in human fibroblasts obtained from a donor at the ages of 49, 52 & 64 y/o. b Immunocytochemistry image of human fibroblasts stained for caspase-1 (green) & Phalloidin (red) from a donor at three different ages (49, 52 & 64 y/o). Bar graph: 100 μm Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30473634), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-56565_mouse-monoclonal-caspase-1-antibody-14f468-310202415345329.jpg)
![Western Blot: Caspase-1 Antibody (14F468) - BSA Free [NB100-56565] - Aging alters expression of NLRP1 inflammasome components. Representative immunoblots & densitometric analysis of immunoblots for caspase-1 (Casp1), caspase-11 (Casp11), NLRP1, ASC, cleaved XIAP, P2X7 receptor (P2X7R) & pannexin-1 (PanX1) in brain lysates of young (Y) & aged (A) animals. Protein levels of cleaved caspase-1 & -11 are higher in aged animals compared to young. Protein levels of NLRP1 & ASC did not change with age whereas P2X7 receptor, the pannexin-1 protein & the cleaved fragment of XIAP are higher in aged animals than in young animals. beta -Tubulin was used as an internal standard & control for protein loading. Data are presented as mean +/- SEM. *p < 0.05, **p < 0.01, ***p < 0.005 compared with young. n = 6 per group. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/22133203), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-56565_mouse-monoclonal-caspase-1-antibody-14f468-310202415384197.jpg)
![Western Blot: Caspase-1 Antibody (14F468) - BSA Free [NB100-56565] - Role of NF-kappa B in glucose fluctuation-induced inflammasome-related myocardial fibrosis. (A) Immunofluorescence staining of NF-kappa B/p65 nucleation (n = 3 per group). (B,C) The phosphorylation level of NF-kappa B/p65 in rat hearts of the three groups (n = 4 per group). (D) Immunofluorescence staining of intracellular NLRP3–ASC interaction in the GF & GF + TPCA-1 groups. The NRCFs were labeled with anti-NLRP3 (red), anti-ASC (green), & DAPI (blue) (n = 3 per group). (E–G) After application of TPCA-1 (0.5 μM), the protein expressions of cleaved caspase-1 & collagen I were measured by western blot (n = 3 per group). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35592403), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-56565_mouse-monoclonal-caspase-1-antibody-14f468-31020241539719.jpg)
![Western Blot: Caspase-1 Antibody (14F468) - BSA Free [NB100-56565] - Inflammasome proteins are elevated in the cytosolic fraction of aged mice: a Representative image of immunoblot analyses of inflammasome proteins in the cytosolic fraction of the cortex of young (Y) & aged (A) mice. Quantification of immunoblot analysis of NLRC4 (b), caspase-1 (c), ASC (d), IL-18 (e) in the cortex. a Representative image of immunoblot analyses of inflammasome proteins in the cytosolic fraction of the hippocampus of young (Y) & aged (A) mice. Quantification of immunoblot analysis of NLRC4 (g), caspase-1 (h), caspase-11 (i), ASC (j), IL-1 beta (k) in the hippocampus. Data presented as mean+/-SEM. N = 5 per group. *p < 0.05 Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30473634), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-56565_mouse-monoclonal-caspase-1-antibody-14f468-310202415392595.jpg)
![Western Blot: Caspase-1 Antibody (14F468) - BSA Free [NB100-56565] - NLRP3 inhibition with MCC950 reversed myocardial fibrosis induced by glucose fluctuations. (A) Representative images of hematoxylin & eosin (HE) staining for myocardial tissue in the FBG + NaCl & FBG + MCC950 groups (n = 3 per group). (B–C) Representative images of myocardial fibrosis & fibrosis area (%) in the FBG + NaCl & FBG + MCC950 groups (n = 4 per group). (D–K) The protein expressions of NLRP3, cleaved caspase-1, TGF-beta 1, collagen I & collagen III in the FBG + NaCl & FBG + MCC950 groups (n = 6 per group). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35592403), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-56565_mouse-monoclonal-caspase-1-antibody-14f468-310202415175211.jpg)
![Western Blot: Caspase-1 Antibody (14F468) - BSA Free [NB100-56565] - Inflammasome proteins are elevated in the cytosolic fraction of aged mice: a Representative image of immunoblot analyses of inflammasome proteins in the cytosolic fraction of the cortex of young (Y) & aged (A) mice. Quantification of immunoblot analysis of NLRC4 (b), caspase-1 (c), ASC (d), IL-18 (e) in the cortex. a Representative image of immunoblot analyses of inflammasome proteins in the cytosolic fraction of the hippocampus of young (Y) & aged (A) mice. Quantification of immunoblot analysis of NLRC4 (g), caspase-1 (h), caspase-11 (i), ASC (j), IL-1 beta (k) in the hippocampus. Data presented as mean+/-SEM. N = 5 per group. *p < 0.05 Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30473634), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-56565_mouse-monoclonal-caspase-1-antibody-14f468-310202415395949.jpg)
![Western Blot: Caspase-1 Antibody (14F468) - BSA Free [NB100-56565] - Role of inflammasome in glucose fluctuation-induced myocardial fibrosis. (A) Immunofluorescence staining of intracellular NLRP3–ASC interaction examined by confocal microscopy. The NRCFs were labeled with anti-NLRP3 (red), anti-ASC (green), & DAPI (blue) (n = 3 per group). (B–G) After siRNA targeting NLRP3 transfection, the protein expressions of NLRP3, cleaved caspase-1 & collagen I were measured by western blot (n = 3 per group). (H) Representative images of immunofluorescence staining of intracellular alpha -SMA in the NG, HG, GF, & GF + siRNA groups (n = 3 per group). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35592403), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-56565_mouse-monoclonal-caspase-1-antibody-14f468-31020241534326.jpg)
![Western Blot: Caspase-1 Antibody (14F468) - BSA Free [NB100-56565] - Epirubicin suppresses the NLRP3 inflammasome in presence of autophagy inhibitors. (A) LPS/ATP-induced IL-1 beta secretion from PM in the absence or presence of bafilomycin & 3-MA is shown. Means ± SEM from 10 (IL-1 beta ) independent experiments are shown. (B) Representative immunoblot of LC3b after epirubicin & LPS/ATP treatments. (C,D) Representative immunoblots of inflammasome & autophagy components after inhibition with (C) bafilomycin or (D) 3-MA in PM whole cell lysates. Cells were treated with indicated concentrations of epirubicin treatment over 24 h, followed by LPS (10 ng/mL) in the absence or presence of bafilomycin (300 nM) or 3-MA (10 mM) for 3 h & NLRP3 activation by ATP (1 mM, 1 h). Whole cell lysates were subjected to SDS-PAGE (10% gel) & processed for immunoblot analysis with specific antibodies. Here, beta -actin served as loading control. Statistical tests: one-sample t-test (A) ** p < 0.01, *** p < 0.001. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31905600), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-56565_mouse-monoclonal-caspase-1-antibody-14f468-31020241612614.jpg)
![Western Blot: Caspase-1 Antibody (14F468) - BSA Free [NB100-56565] - Genetic or pharmacologic disruption of Caspase 1 blocks LukAB-induced cytokine secretion but not cell death.(A) THP1 cells were transfected with siRNA against Caspase 1, ASC or a non-targeting sequence. Cell lysates were collected & analyzed by immunoblot to confirm knockdown of pro-Caspase 1 & ASC. (B) THP1 siRNA cells were incubated with propidium iodide & intoxicated with 50 ng/mL LukAB for 1 hour then analyzed by flow cytometry. (C & D) THP1 siRNA cells were either primed with LTA (500ng/mL) (C) or untreated (D) then intoxicated with LukAB (50ng/mL) for 1 hr before culture supernatants were analyzed for release of IL-1 beta (C) or IL-18 (D). (E & F) Primary CD14+ human monocytes were incubated with the indicated concentration of z-YVAD-FMK or VX-765 for 30 minutes. Primary monocytes were incubated in the presence of propidium iodide (E) then intoxicated with LukAB (50ng/mL) & analyzed by flow cytometry. (F) Primary monocytes were intoxicated with LukAB (50ng/mL) & culture supernatants were analyzed for release of IL-18. Propidium iodide staining & IL-18 secretion are reported as a fraction of measurement in primary cells not treated with inhibitor. Bars represent the mean ± standard error of the mean for at least two independent experiments, each performed in triplicate. Asterisks indicate significance at a p-value of ≤ 0.05 by Tukey’s multiple comparisons post-test for 1-way or 2-way ANOVA, as appropriate. Image collected & cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.ppat.1004970), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-56565_mouse-monoclonal-caspase-1-antibody-14f468-310202415541952.jpg)
![Western Blot: Caspase-1 Antibody (14F468) - BSA Free [NB100-56565] - Probenecid reduces protein expression of NLRP1 inflammasome & ameliorates spatial learning deficits in aged rats. (A) Representative immunoblots of cleaved caspase-1, pannexin1 & P2X7R in hippocampal lysates of vehicle (Veh)-treated & probenecid (Pr)-treated 18-month-old rats. beta -tubulin was used as an internal control. (B) Densitometric analysis of immunoblots from brain lysates of cleaved caspase-1 (Casp1), P2X7 receptor (P2X7R), & pannexin1 (PanX1). (C-D) Aged animals underwent behavioral testing following either probenecid or vehicle treatment. (C) In a hippocampal-dependent spatial learning task via Morris water maze, latency to platform was measured on days 1-3 & 8-10. Probenecid-treatment improved latency to platform measured on the final day of testing (D) Mean path length was determined on day 10 of testing & probenecid-treated rats demonstrated significantly shorter mean path lengths than vehicle-treated controls. Drug treatment was administered twice daily for 3 days (days 7-9). Data are presented as mean +/- SEM *p < 0.05, **p < 0.005 compared to vehicle. N = 6-8/per group. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/22133203), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb100-56565_mouse-monoclonal-caspase-1-antibody-14f468-310202415541990.jpg)
![Western Blot: GAPDH Antibody [NB300-320] - Staining of Human Liver (A) and Tonsil (B) with antibody at 0.001 ug/mL and Rat Brain lysate (C) with antibody at 0.3 ug/mL (35 ug protein in RIPA buffer). Detected by chemiluminescence. Approx. 37 kDa band observed in Rat Brain lysates and approx. 35 kDa in Human Liver and Tonsil lysates (calculated MW of 36.1 kDa according to Human NP_002037.2 and 35.8 kDa according to Rat NP_058704.1).](http://images.novusbio.com/fullsize/GAPDH-Antibody-Western-Blot-NB300-320-img0008.jpg "Western Blot: GAPDH Antibody [NB300-320] - Staining of Human Liver (A) and Tonsil (B) with antibody at 0.001 ug/mL and Rat Brain lysate (C) with antibody at 0.3 ug/mL (35 ug protein in RIPA buffer). Detected by chemiluminescence. Approx. 37 kDa band observed in Rat Brain lysates and approx. 35 kDa in Human Liver and Tonsil lysates (calculated MW of 36.1 kDa according to Human NP_002037.2 and 35.8 kDa according to Rat NP_058704.1).")
![Immunocytochemistry/Immunofluorescence: GAPDH Antibody [NB300-320] - Immunofluorescence analysis of paraformaldehyde fixed HeLa cells, permeabilized with 0.15% Triton. Primary incubation 1hr (10 ug/mL) followed by Alexa Fluor 488 secondary antibody (2 ug/mL), showing cytoplasmic and vesicle staining. The nuclear stain is DAPI (blue). Negative control: Unimmunized goat IgG (10 ug/mL) followed by Alexa Fluor 488 secondary antibody (2 ug/mL). Strong expression of the protein seen in the cytoplasm and vesicles of HeLa cells.](http://images.novusbio.com/fullsize/GAPDH-Antibody-Immunocytochemistry-Immunofluorescence-NB300-320-img0010.jpg)
![Immunohistochemistry-Paraffin: GAPDH Antibody [NB300-320] - Staining of paraffin embedded Human Pancreas. Antibody at 2.5 ug/mL. Steamed antigen retrieval with citrate buffer pH 6, AP-staining.](http://images.novusbio.com/fullsize/GAPDH-Antibody-Immunohistochemistry-Paraffin-NB300-320-img0011.jpg)
![Western Blot: GAPDH Antibody [NB300-320] - stai Mutants Have Reduced Levels of alpha-Tubulin, Acetylated alpha-Tubulin, and Kinesin Heavy Chain Protein. Representative western blots of total protein extracted from stai mutant third instar larvae. Heterozygous stai/+ mutant larvae exhibit mild reductions in the levels of alpha-tubulin and acetylated alpha-tubulin compared with wild type larvae. Homozygous stai mutant larvae have dramatic reductions in the levels of alpha-tubulin, acetylated alpha-tubulin and the heavy chain subunit of the microtubule motor protein kinesin compared to wildtype. Df(2L) BSC239 represents a second chromosomal deficiency that excludes the stai gene. GAPDH is used as a loading control. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0068324), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/GAPDH-Antibody-Western-Blot-NB300-320-img0005.jpg)
![Western Blot: GAPDH Antibody [NB300-320] - Staining of HEK293 (A) and HeLa (B) cell lysate (35 ug protein in RIPA buffer). Antibody at 0.001 ug/mL. Detected by chemiluminescence. Approx 36 kDa band observed in lysates of cell line HEK293 and approx. 35 kDa in HeLa cell lysates.(calculated MW of 36.1 kDa according to Human NP_002037.2).](http://images.novusbio.com/fullsize/GAPDH-Antibody-Western-Blot-NB300-320-img0007.jpg)
![Immunocytochemistry/Immunofluorescence: GAPDH Antibody [NB300-320] - Immunofluorescence analysis of paraformaldehyde fixed A549 cells, permeabilized with 0.15% Triton. Primary incubation 1hr (10 ug/mL) followed by Alexa Fluor 488 secondary antibody (2 ug/mL), showing cytoplasmic and vesicle staining. The nuclear stain is DAPI (blue). Negative control: Unimmunized goat IgG (10 ug/mL) followed by Alexa Fluor 488 secondary antibody (2 ug/mL). Strong expression of the protein seen in the cytoplasm and vesicles of A549 cells.](http://images.novusbio.com/fullsize/GAPDH-Antibody-Immunocytochemistry-Immunofluorescence-NB300-320-img0009.jpg)
![Immunohistochemistry-Paraffin: GAPDH Antibody [NB300-320] - Upregulation of GAPDH and Tom20 in C6 gliomas. A small glioma labeled with antibodies against GAPDH. The brightness and contrast have been increased. Image collected and cropped by CiteAb from the following publication (//www.biomedcentral.com/1756-0500/8/207), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/GAPDH-Antibody-Immunohistochemistry-Paraffin-NB300-320-img0006.jpg)
![Western Blot: GAPDH Antibody [NB300-320] - PAR2 causes contraction of smooth muscle cells from human prostate. (A & B) Decrease in diameter of collagen hydrogels after PAR2 activation with SLIGKV (80 µM). (C) Representative western blot & (D) densitometry showing time dependent increase in level of phosphorylated MLC20 in PSMC after PAR2 is activated. Data represent mean ± SEM of at least three independent experiments. Diameter of collagen hydrogels were measured in ImageJ (version 1.50i) & significance analyzed in Prism (version 7.04) with one‐way ANOVA followed by Tukey's multiple comparison test. *P < 0.05, **P < 0.01 Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31198907), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-320_goat-polyclonal-gapdh-antibody-img-3073-31020241534329.jpg)
![Immunocytochemistry/ Immunofluorescence: GAPDH Antibody [NB300-320] - Upregulation of GAPDH & Tom20 in C6 gliomas. a A section of rat brain stained with hematoxilin & eosin to show a glioma produced by implantation of C6 cells in the right caudate nucleus. In this case, cells also grew in the region of the syringe needle track through the cortex. (b–d). A small glioma labeled by bisbenzamide (b) & with antibodies against Tom20 (c) & GAPDH (d). The brightness & contrast have been increased. e Illustration of a strip perpendicular to the rim of a glioma (labeled with bisbenzamide) & along which intensity profiles were measured. f, g Tom20 & GAPDH fluorescence along such a strip (barely visible without enhancement). The graphs show the raw intensity values given by ImageJ. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26032618), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-320_goat-polyclonal-gapdh-antibody-img-3073-310202415392578.jpg)
![Western Blot: GAPDH Antibody [NB300-320] - CDC20B was the protein effector regulated by hsa-miR-633. (a) CDC20B level was up-regulated after ox-LDL treatment revealed by Western blotting. (b) CDC20B level was decreased after the treatment of hsa-miR-633 mimics revealed by Western blotting. (c) CDC20B level was increased after the treatment of hsa-miR-633 inhibitor revealed by Western blotting. (d) The luciferase reporter plasmids were constructed as illustrated. (e) Relative luciferase activities after co-transfection CDC20B WT & hsa-miR-633/Control, or CDC20B Mut & hsa-miR-633/Control were measured. (f) The expression levels of two proliferation markers, Ki67 & PCNA after the treatment of si-CDC20B were measured using Western blotting. (g) Colony formation assay was conducted to examine the proliferation abilityafter the treatment of si-CDC20B. (h) Transwell migration & invasion assays were conducted to examine the migration & invasion abilities of VSMCs after the treatment of si-CDC20B. (i) Quantification results of (g). (j) Quantification results of (h). *P < 0.05, **P < 0.01, ***P < 0.001. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35212610), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-320_goat-polyclonal-gapdh-antibody-img-3073-310202416205177.jpg)
![Simple Western: GAPDH Antibody [NB300-320] - MiR-34a affects stroke outcomes via interacting with cytochrome c. (A) WES system image showing CYC, VDAC & GAPDH expression from hemispheres of WT & miR-34a−/− mice at 6 h post-stroke. (B) Relative CYC expression normalized to GAPDH from the data generated by the WES system. CYC level is significantly decreased in ischemic hemispheres of WT mice but no significant changes in miR-34a−/− mice between contralateral hemispheres (Control) & ischemic hemispheres (Ischemia). N = 5 per group, **p < 0.01, One-way ANOVA followed by post hoc Tuckey’s test was used for data analysis. Data are expressed as mean ± S.D. (C) Relative VDAC expression normalized to GAPDH from the data generated by the WES system. VDAC was not significantly altered in WT mice nor miR-34a−/− mice. (D) Multiplexed WES system image showing CYC & GAPDH expression from purified pCECs of WT & miR-34a−/− mice (n = 10 per group, pooled cell samples) at 6 h post-stroke. (E) Relative CYC expression by normalization to GAPDH. A 2.8 fold decrease of CYC level was observed in WT mice but no changes were observed in miR-34a−/− mice between contralateral hemispheres & ischemic hemispheres. (F) A CYC reporter was coexpressed with a miR-34a plasmid, a miR-34a mimic, a miR-34c mimic, or a plasmid control in cultured cerebral vascular endothelial cells for 24 hours. Relative firefly luciferase activity was evaluated & normalized to renilla luciferase activity. Relative firefly luciferase activity was reduced by miR-34a plasmid & miR-34a mimic. The experiment was repeated 3 times & triplicates were used for each analysis. Data represents the mean ± S.D. *p < 0.05. One-way ANOVA followed by post-hoc Tuckey’s test was used for analysis. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32094435), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-320_goat-polyclonal-gapdh-antibody-img-3073-3102024162180.jpg)
![Western Blot: GAPDH Antibody [NB300-320] - Hsa-miR-633 inhibitor could reverse the si-circ_0008896 phenotypes. (a) CCK8 assay was conducted to measure cell viability after up-regulation of hsa-miR-633. (b) The expression levels of two proliferation markers, Ki67 & PCNA after up-regulation of hsa-miR-633 were measured using Western blotting. (c) CCK8 assay was conducted to measure cell viability after the treatment of si-circ0008896, hsa-miR-633 inhibitor & si-circ0008896+ hsa-miR-633 inhibitor. (d) The expression levels of two proliferation markers, Ki67 & PCNA after the treatment of si-circ0008896, hsa-miR-633 inhibitor & si-circ0008896+ hsa-miR-633 inhibitor were measured using Western blotting. (e) Colony formation assay was conducted to examine proliferation ability number of colonies after the treatment of si-circ0008896, hsa-miR-633 inhibitor & si-circ0008896+ hsa-miR-633 inhibitor. (f) Quantification results of (e). (g) Transwell migration & invasion assays were conducted to examine the migration & invasion abilities of VSMCs after the treatment of si-circ0008896, hsa-miR-633 inhibitor & si-circ0008896+ hsa-miR-633 inhibitor. (h) Quantification results of (g). *P < 0.05, **P < 0.01, ***P < 0.001. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35212610), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-320_goat-polyclonal-gapdh-antibody-img-3073-31020241620373.jpg)
![Western Blot: GAPDH Antibody [NB300-320] - Down-regulation of hsa_circ_0008896 inhibited proliferation, migration & invasion in vitro. (a) The expression level of hsa_circ_0008896 after si-circ_0008896 transfection was detected using quantitative PCR. (b) CCK8 assay was conducted to measure cell viability after down-regulation of hsa_circ_0008896. (c) The expression levels of two proliferation markers, Ki67 & PCNA after down-regulation of hsa_circ_0008896 were detected using Western blotting. (d) Colony formation assay was conducted to examine proliferation ability after down-regulation of hsa_circ_0008896. (e) The quantification results of (d). (f) Transwell migration & invasion assays were conducted to examine the migration & invasion abilities of VSMCs after down-regulation of hsa_circ_0008896. (g) The quantification results of (f). *P < 0.05, **P < 0.01, ***P < 0.001. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35212610), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-320_goat-polyclonal-gapdh-antibody-img-3073-31020241621234.jpg)
![Western Blot: GAPDH Antibody [NB300-320] - CDC20B was the protein effector regulated by hsa-miR-633. (a) CDC20B level was up-regulated after ox-LDL treatment revealed by Western blotting. (b) CDC20B level was decreased after the treatment of hsa-miR-633 mimics revealed by Western blotting. (c) CDC20B level was increased after the treatment of hsa-miR-633 inhibitor revealed by Western blotting. (d) The luciferase reporter plasmids were constructed as illustrated. (e) Relative luciferase activities after co-transfection CDC20B WT & hsa-miR-633/Control, or CDC20B Mut & hsa-miR-633/Control were measured. (f) The expression levels of two proliferation markers, Ki67 & PCNA after the treatment of si-CDC20B were measured using Western blotting. (g) Colony formation assay was conducted to examine the proliferation abilityafter the treatment of si-CDC20B. (h) Transwell migration & invasion assays were conducted to examine the migration & invasion abilities of VSMCs after the treatment of si-CDC20B. (i) Quantification results of (g). (j) Quantification results of (h). *P < 0.05, **P < 0.01, ***P < 0.001. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35212610), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-320_goat-polyclonal-gapdh-antibody-img-3073-310202416205198.jpg)
![Simple Western: GAPDH Antibody [NB300-320] - MiR-34a affects stroke outcomes via interacting with cytochrome c. (A) WES system image showing CYC, VDAC & GAPDH expression from hemispheres of WT & miR-34a−/− mice at 6 h post-stroke. (B) Relative CYC expression normalized to GAPDH from the data generated by the WES system. CYC level is significantly decreased in ischemic hemispheres of WT mice but no significant changes in miR-34a−/− mice between contralateral hemispheres (Control) & ischemic hemispheres (Ischemia). N = 5 per group, **p < 0.01, One-way ANOVA followed by post hoc Tuckey’s test was used for data analysis. Data are expressed as mean ± S.D. (C) Relative VDAC expression normalized to GAPDH from the data generated by the WES system. VDAC was not significantly altered in WT mice nor miR-34a−/− mice. (D) Multiplexed WES system image showing CYC & GAPDH expression from purified pCECs of WT & miR-34a−/− mice (n = 10 per group, pooled cell samples) at 6 h post-stroke. (E) Relative CYC expression by normalization to GAPDH. A 2.8 fold decrease of CYC level was observed in WT mice but no changes were observed in miR-34a−/− mice between contralateral hemispheres & ischemic hemispheres. (F) A CYC reporter was coexpressed with a miR-34a plasmid, a miR-34a mimic, a miR-34c mimic, or a plasmid control in cultured cerebral vascular endothelial cells for 24 hours. Relative firefly luciferase activity was evaluated & normalized to renilla luciferase activity. Relative firefly luciferase activity was reduced by miR-34a plasmid & miR-34a mimic. The experiment was repeated 3 times & triplicates were used for each analysis. Data represents the mean ± S.D. *p < 0.05. One-way ANOVA followed by post-hoc Tuckey’s test was used for analysis. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32094435), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-320_goat-polyclonal-gapdh-antibody-img-3073-31020241621811.jpg)
![Western Blot: GAPDH Antibody [NB300-320] - Hsa-miR-633 inhibitor could reverse the si-circ_0008896 phenotypes. (a) CCK8 assay was conducted to measure cell viability after up-regulation of hsa-miR-633. (b) The expression levels of two proliferation markers, Ki67 & PCNA after up-regulation of hsa-miR-633 were measured using Western blotting. (c) CCK8 assay was conducted to measure cell viability after the treatment of si-circ0008896, hsa-miR-633 inhibitor & si-circ0008896+ hsa-miR-633 inhibitor. (d) The expression levels of two proliferation markers, Ki67 & PCNA after the treatment of si-circ0008896, hsa-miR-633 inhibitor & si-circ0008896+ hsa-miR-633 inhibitor were measured using Western blotting. (e) Colony formation assay was conducted to examine proliferation ability number of colonies after the treatment of si-circ0008896, hsa-miR-633 inhibitor & si-circ0008896+ hsa-miR-633 inhibitor. (f) Quantification results of (e). (g) Transwell migration & invasion assays were conducted to examine the migration & invasion abilities of VSMCs after the treatment of si-circ0008896, hsa-miR-633 inhibitor & si-circ0008896+ hsa-miR-633 inhibitor. (h) Quantification results of (g). *P < 0.05, **P < 0.01, ***P < 0.001. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35212610), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-320_goat-polyclonal-gapdh-antibody-img-3073-31020241621849.jpg)
![Western Blot: Perilipin-2/ADFP Antibody - BSA Free [NB110-40877] - Western blot images (A) & quantifications (B–I) of muscle samples from WT & UCHL1 smKO mice for lipase ATGL (B), HSL (C), & MAGL (D), the fatty acid transport protein CD36 (E), the key lipid synthesis enzyme DGAT2 (F), perilipin 3 (G), perilipin 2 (H), & UCHL1 (I). n = 4-5 per group. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35464088), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-40877_rabbit-polyclonal-perilipin-2-adfp-antibody-310202415171328.jpg)
![Western Blot: Perilipin-2/ADFP Antibody - BSA Free [NB110-40877] - Western blot images (A) & quantifications (B–G) of cell lysates from C2C12 myotubes with control or UCHL1 siRNA knockdown for perilipin 2 (B), perilipin 5 (C), CD36 (D), HSL (E), MAGL (F), & SDHB (G). n = 4 per group. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35464088), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-40877_rabbit-polyclonal-perilipin-2-adfp-antibody-310202415384159.jpg)
![Immunocytochemistry/ Immunofluorescence: Perilipin-2/ADFP Antibody - BSA Free [NB110-40877] - Lack of MT4-MMP in patrolling monocytes leads to the accumulation of Mafb+AIM+ macrophages in incipient atherosclerotic plaques. a Representative images of transverse sections of aortic sinus from Ldlr–/– mice transplanted with MT4-MMP+/+ (MT4+/+) or MT4-MMP–/– (MT4–/–) BM cells & fed a HFD for 1 week; sections were labeled for Mac3 (green), Mafb (red), & AIM (white), & with Hoechst (blue; nuclei); scale bar, 10 µm. b Number of Mac3+ cells (left), Mac3+Mafb+ cells (middle), & Mac3+Mafb+AIM+ cells (right) in the plaques of BM-transplanted Ldlr–/– mice fed a HFD for 1 week. c Representative images of transverse sections of aortic sinus from BM-transplanted Ldlr–/– mice fed a HFD for 1 week; sections were labeled for Mac3 (green), Mafb (red), & adipophilin (white), & with Hoechst (blue; nuclei); scale bar, 10 µm. d Relative % of adipophilin-positive & adipophilin-negative cells within the Mac3+Mafb+ population of BM-transplanted Ldlr–/– mice (1 week on HFD); n = 7 mice per genotype in two independent experiments. Data were tested by two-tailed Student’s t-test in b & by Fisher’s exact test in d. Results are expressed as mean ± SEM. *p < 0.05 Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/s41467-018-03351-4), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb110-40877_rabbit-polyclonal-perilipin-2-adfp-antibody-310202416235522.jpg)
![Western Blot: SREBP1 Antibody (2A4) [NB600-582] - Hepatic SREBP1c and SREBP2 protein abundance in C57BL/6 mice assigned to a high-fat (HF) or a high-fat/exercise (HF + EX) group for 8 weeks. Cytosolic and nuclear SREBP1c abundance. Image collected and cropped by CiteAb from the following publication (//www.hindawi.com/journals/jl/2013/908048/), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/SREBP1-Antibody-2A4-Western-Blot-NB600-582-img0004.jpg "Western Blot: SREBP1 Antibody (2A4) [NB600-582] - Hepatic SREBP1c and SREBP2 protein abundance in C57BL/6 mice assigned to a high-fat (HF) or a high-fat/exercise (HF + EX) group for 8 weeks. Cytosolic and nuclear SREBP1c abundance. Image collected and cropped by CiteAb from the following publication (//www.hindawi.com/journals/jl/2013/908048/), licensed under a CC-BY license.")
![Western Blot: SREBP1 Antibody (2A4) [NB600-582] - Analysis of whole cell lysate from HeLa cells showing a single specific band for the expression of SREBP1 precursor protein (~120 kDa).](http://images.novusbio.com/fullsize/SREBP1-Antibody-2A4-Western-Blot-NB600-582-img0002.jpg)
![Simple Western: SREBP1 Antibody (2A4) [NB600-582] - Lane view shows a specific band for SREBP1 in 1.0 mg/ml of HeLa lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system.](http://images.novusbio.com/fullsize/SREBP1-Antibody-2A4-Simple-Western-NB600-582-img0003.jpg)
![<b>Genetic Strategies Validation. </b>Western Blot: SREBP1 Antibody (2A4) [NB600-582] - KO and OE of SREBP1 influenced lipid metabolism in Bel-7402 cells. The protein level of lipid-associated genes in SREBP1-KO, SREBP1-OE, and WT Bel-7402 cells. Data were expressed as mean -/+ standard error of the mean. *P < 0.05, **P < 0.01, and ***P < 0.001 vs. WT group, respectively.](http://images.novusbio.com/fullsize/SREBP1-Antibody-2A4-Knockout-Validated-NB600-582-img0005.jpg)
![Western Blot: SREBP1 Antibody (2A4) - BSA Free [NB600-582] - Effect of GEN on the expression of Nrf2‐related signalling proteins in OA (660 μmol/L) & PA (330 μmol/L)‐induced HepG2 cells. GEN was added into HepG2 cells prior 1 h to stimulation of OA & PA for 18 h. A‐C, Protein expression of Nrf2, PPAR alpha , PPAR gamma in nucleus & HO‐1 in cytoplasm was detected by Western blot. (D & E) Protein expression of P‐ACC, ACC, P‐AKT, AKT, P‐AMPK alpha , AMPK alpha , P‐AMPK beta & AMPK beta was detected by Western blot. F‐H, Protein expression of PI3K, P‐mTORC, mTORC, P‐S6K, S6K, P‐S6, S6, SREBP‐1c & HMGB1 was detected by Western blot. The similar results were collected from three dependent experiments. All data were expressed by mean ± SEM (n = 5 in each group). ##P < .01 vs Control Group; *P < .05 & **P < .01 vs OA & PA Group Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32293113), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-582_mouse-monoclonal-srebp1-antibody-2a4-31020241534375.jpg)
![Western Blot: SREBP1 Antibody (2A4) - BSA Free [NB600-582] - KO & OE of SREBP1 influenced lipid metabolism in Bel-7402 cells. (A) Total cellular TG content of SREBP1-KO, SREBP1-OE, & WT Bel-7402 cells. (B) HPLC-MS determination of the SFAs to MUFAs ratios (palmitic acid to palmitoleic acid, 16:0 to 16:1) (stearic acid to oleic acid, 18:0 to 18:1) as well as the content of 16:0, 16:1, 18:0, & 18:1 in SREBP1-KO, SREBP1-OE, & WT Bel-7402 cells. (C) The transcript level of lipid-associated genes in SREBP1-KO, SREBP1-OE, & WT Bel-7402 cells. (D & E) The protein level of lipid-associated genes in SREBP1-KO, SREBP1-OE, & WT Bel-7402 cells. Data were expressed as mean ± standard error of the mean. *P < 0.05, **P < 0.01, & ***P < 0.001 vs. WT group, respectively. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31297058), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-582_mouse-monoclonal-srebp1-antibody-2a4-310202415384185.jpg)
![Western Blot: SREBP1 Antibody (2A4) - BSA Free [NB600-582] - Construction of knockout (KO) & overexpression (OE) cell lines. (A) The sequencing results of KO positive clone cells; (B) The messenger RNA (mRNA) level of SREBP1 in wild type (WT) & OE Bel-7402 cells. Data were expressed as mean ± standard error of the mean. ***P < 0.001 vs. WT group; (C & D) The protein level of SREBP1 in WT, OE, & KO Bel-7402 cells. Data were expressed as mean ± standard error of the mean. ***P < 0.001 vs. WT group. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31297058), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-582_mouse-monoclonal-srebp1-antibody-2a4-31020241539748.jpg)
![Western Blot: SREBP1 Antibody (2A4) - BSA Free [NB600-582] - p75NTR stimulation activated SREBP1 & SREBP2 in Huh7 hepatocyte cells.Human Huh7 cells were stimulated with 10 ng/ml pro-NGF or 50 ng/ml NGF for 16 h followed by immunoblotting using antibodies to detect the presence of cleaved/activated SREBP1 & SREBP2. a SREBP1, immunoblots & b quantification. Values are mean ± SD, n = 3. **P < 0.01 & *p < 0.05 for treated vs. control cells. c, d SREBP2. Cells were treated with 10 ng/ml pro-NGF in the absence or presence of 0.5 μM PF429242 (PF), which is a selective inhibitor of the Site 1 protease (S1P). c Immunoblots & d quantification. PF decreased the amount of processed SREBP2 in these cells; however, addition of pro-NGF increased the relative level of cleaved SREBP2. Values are mean ± SD, n = 3. *p < 0.05 for treated vs. the corresponding control Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31296846), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-582_mouse-monoclonal-srebp1-antibody-2a4-310202416161836.jpg)
![Western Blot: SREBP1 Antibody (2A4) - BSA Free [NB600-582] - p75NTR stimulation activated SREBP1 & SREBP2 in Huh7 hepatocyte cells.Human Huh7 cells were stimulated with 10 ng/ml pro-NGF or 50 ng/ml NGF for 16 h followed by immunoblotting using antibodies to detect the presence of cleaved/activated SREBP1 & SREBP2. a SREBP1, immunoblots & b quantification. Values are mean ± SD, n = 3. **P < 0.01 & *p < 0.05 for treated vs. control cells. c, d SREBP2. Cells were treated with 10 ng/ml pro-NGF in the absence or presence of 0.5 μM PF429242 (PF), which is a selective inhibitor of the Site 1 protease (S1P). c Immunoblots & d quantification. PF decreased the amount of processed SREBP2 in these cells; however, addition of pro-NGF increased the relative level of cleaved SREBP2. Values are mean ± SD, n = 3. *p < 0.05 for treated vs. the corresponding control Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31296846), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-582_mouse-monoclonal-srebp1-antibody-2a4-310202416175210.jpg)
![Western Blot: SREBP1 Antibody (2A4) - BSA Free [NB600-582] - Effect of GEN on the protein expression of Nrf2, ACC & mTORC signalling pathways in tyloxapol‐induced mice. GEN (50, 75, 100 mg/kg) was administered to WT or Nrf2−/− mice prior 1 h to stimulation of tyloxapol (500 mg/kg) for 18 h. A‐C, Protein expression of Nrf2, PPAR alpha , PPAR gamma in nucleus & HO‐1 in cytoplasm of WT mice was detected by Western blot. (D & E) Protein expression of Nrf2, PPAR alpha & PPAR gamma in Nrf2−/− mice was detected by Western blot. F‐H, Protein expression of P‐ACC, ACC, P‐AKT, AKT, P‐AMPK alpha , AMPK alpha , P‐AMPK beta , AMPK beta in WT & Nrf2−/− mice was detected by Western blot. I‐M, Protein expression of PI3K, P‐mTORC, mTORC, P‐S6K, S6K, P‐S6, S6, SREBP‐1c & HMGB1 WT & Nrf2−/− mice was detected by Western blot. The similar results were collected from three dependent experiments. All data were expressed by mean ± SEM (n = 5 in each group). ##P < .01 vs Control group; *P < .05 & **P < .01 vs Tyloxapol group Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32293113), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-582_mouse-monoclonal-srebp1-antibody-2a4-310202416171460.jpg)