| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB400-105SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB400-132SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB300-605SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NBP2-61137 | |||
| BSA Free | NB300-146SS | |||
| Azide and BSA Free | NBP2-80956 | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB400-148SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB600-717SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NBP2-22119SS | |||
| Azide and BSA Free | NBP2-80814 | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB100-402SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB200-540SS | |||
| Azide and BSA Free | NBP2-80677 | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB300-500SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB300-140-0.025ml | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB400-128SS | |||
![Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - (A) Upregulation of ABCA1 & ABCG1 & (B) enhancement of cholesterol efflux by purple Perilla frutescens extracts (PPE) in 50 μg/ml Cu2+-oxidized low-density lipoproteins (LDL)-exposed J774A.1 murine macrophages. (A) For the measurement of ABCA1 & ABCG1 expression, total cell lysates were subjected to western blot analysis with a primary antibody against ABCA1 or ABCG1. beta -actin was used as an internal control. Bar graphs (means ± SEM, n=3) represent quantitative densitometric results of the upper bands. (B) Cholesterol efflux was expressed as the percentage of fluorescence in the medium relative to the total fluorescence. Bar graphs denoted without a common letter indicate significant difference, P<0.05. Image collected & cropped by CiteAb from the following publication (//www.spandidos-publications.com/10.3892/ijmm.2015.2101), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-105_rabbit-polyclonal-abca1-antibody-310202415382446.jpg)
![Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - 6‐Dihydroparadol increases A) ABCA1 & B) ABCG1, but not C) SR‐BI protein levels in cholesterol‐loaded THP‐1‐derived macrophages. THP‐1 cells were differentiated as described in Figure 2, & then loaded with unlabeled cholesterol for 24 h. Cells were treated with increasing concentrations of 6‐dihydroparadol (1–30 μm) for another 24 h. The protein levels of ABCA1, ABCG1, & SR‐B1 were detected by Western blot analysis. The control was treated with solvent vehicle (0.1% DMSO). As a positive control, TO901317 (5 μm, 24 h) was used. The bar graphs represent mean ± SD from three independent experiments. *p < 0.05, **p < 0.01, & ***p < 0.001 versus control (determined by Student's t‐test or ANOVA with Bonferroni's post hoc test). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29802792), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-105_rabbit-polyclonal-abca1-antibody-310202415384115.jpg)
![Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - Akt inhibition suppresses mTORC1 activity.BHK-ABCA1 cells were induced overnight with mifepristone (10 nM) & then incubated with DEBC, LY294002 or rapamycin at indicated concentrations for 2 h. Cells were then lysed & analyzed for ABCA1 & phosphorylated S6K by Western blotting. Actin was also blotted as loading control. Image collected & cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0113789), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-105_rabbit-polyclonal-abca1-antibody-31020241538240.jpg)
![Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - Reversal of hepatic steatosis by reduction of SREBP-1 levels.(a) Western blotting analysis of SREBP-1 & ABCA1 levels in livers of miR-33+/+Srebf1+/+, miR-33+/+Srebf1+/−, miR-33−/−Srebf1+/+ & miR-33−/−Srebf1+/− mice. Representative western blot images are shown (n=4). Image collected & cropped by CiteAb from following publication (//pubmed.ncbi.nlm.nih.gov/24300912), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-105_rabbit-polyclonal-abca1-antibody-310202415291985.jpg)
![Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - 6‐Dihydroparadol increases A) ABCA1 & B) ABCG1 protein stability. THP‐1 cells were differentiated as described in Figure 2. Then cells were loaded with unlabeled cholesterol & treated with 6‐dihydroparadol (10 μm), or solvent vehicle (0.1% DMSO, control) for 24 h. Cells were lysed at different time points (0, 1, 2, 3, 4, & 6 h) after treatment with the protein synthesis inhibitor cycloheximide (CHX, 100 μm). The protein levels of both ABCA1 & ABCG1 were detected by Western blot analysis. The data points represent mean ± SD from three independent experiments. *p < 0.05 & **p < 0.01 versus control at the same time point (determined by Student's t‐test). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29802792), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-105_rabbit-polyclonal-abca1-antibody-310202415394516.jpg)
![Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - Ligand activation of LXR inhibits LPS-induced MAP kinase activation through Abca1 induction.(A–D) Bone marrow-derived macrophages from Lxr alpha −/−Lxr beta −/− & control wild-type mice (A, B), or bone marrow-derived macrophages from myeloid-specific Abca1−/− & control wild-type mice (C, D) were pretreated with GW3965 (1 µM) overnight, followed by stimulation with LPS (10 ng/ml) for 20 min or 1 hr. Whole cell lysates were harvested & protein expression was analyzed by immunoblotting with the indicated antibodies (A, C). Protein expression was quantified by Image Quant TL7.0 (B, D). N = 4–6 per group. *p < 0.05, **p < 0.01, NS, not significant. Error bars represent means ± SEM.DOI://dx.doi.org/10.7554/eLife.08009.012 Image collected & cropped by CiteAb from the following publication (//elifesciences.org/articles/08009), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-105_rabbit-polyclonal-abca1-antibody-310202415392521.jpg)
![Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - 6‐Dihydroparadol increases A) ABCA1 & B) ABCG1, but not C) SR‐BI protein levels in cholesterol‐loaded THP‐1‐derived macrophages. THP‐1 cells were differentiated as described in Figure 2, & then loaded with unlabeled cholesterol for 24 h. Cells were treated with increasing concentrations of 6‐dihydroparadol (1–30 μm) for another 24 h. The protein levels of ABCA1, ABCG1, & SR‐B1 were detected by Western blot analysis. The control was treated with solvent vehicle (0.1% DMSO). As a positive control, TO901317 (5 μm, 24 h) was used. The bar graphs represent mean ± SD from three independent experiments. *p < 0.05, **p < 0.01, & ***p < 0.001 versus control (determined by Student's t‐test or ANOVA with Bonferroni's post hoc test). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29802792), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-105_rabbit-polyclonal-abca1-antibody-310202415392590.jpg)
![Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - Western Blotting for ABCA1, as detailed in Supplementary Protocol #5 (Additional file 1). Caco-2 cells cultivated on filter inserts were treated for 48 h with bexarotene (RXR agonist, 5 μM), T0901317 (LXR agonist, 10 μM), GW3965 (LXR agonist, 10 μM) or the vehicle control (DMSO 0.1%). Protein expression was then determined by western blot analysis. Results were normalized for interexperimental variance & then set in relation to the vehicle control. Bar graphs represent mean ± SD from three independent experiments. A representative blot is shown - the bands stem from the same membrane & the vertical line indicates excised irrelevant bands. ns not significant, *P < 0.05, **P < 0.01 versus solvent vehicle (determined by paired t-test) Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32308567), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-105_rabbit-polyclonal-abca1-antibody-310202415284512.jpg)
![Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - Ligand activation of LXR inhibits LPS-induced MAP kinase activation through Abca1 induction.(A–D) Bone marrow-derived macrophages from Lxr alpha −/−Lxr beta −/− & control wild-type mice (A, B), or bone marrow-derived macrophages from myeloid-specific Abca1−/− & control wild-type mice (C, D) were pretreated with GW3965 (1 µM) overnight, followed by stimulation with LPS (10 ng/ml) for 20 min or 1 hr. Whole cell lysates were harvested & protein expression was analyzed by immunoblotting with the indicated antibodies (A, C). Protein expression was quantified by Image Quant TL7.0 (B, D). N = 4–6 per group. *p < 0.05, **p < 0.01, NS, not significant. Error bars represent means ± SEM.DOI://dx.doi.org/10.7554/eLife.08009.012 Image collected & cropped by CiteAb from the following publication (//elifesciences.org/articles/08009), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-105_rabbit-polyclonal-abca1-antibody-310202415384110.jpg)
![Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - Ligand activation of LXR inhibits LPS-induced MAP kinase activation through Abca1 induction.(A–D) Bone marrow-derived macrophages from Lxr alpha −/−Lxr beta −/− & control wild-type mice (A, B), or bone marrow-derived macrophages from myeloid-specific Abca1−/− & control wild-type mice (C, D) were pretreated with GW3965 (1 µM) overnight, followed by stimulation with LPS (10 ng/ml) for 20 min or 1 hr. Whole cell lysates were harvested & protein expression was analyzed by immunoblotting with the indicated antibodies (A, C). Protein expression was quantified by Image Quant TL7.0 (B, D). N = 4–6 per group. *p < 0.05, **p < 0.01, NS, not significant. Error bars represent means ± SEM.DOI://dx.doi.org/10.7554/eLife.08009.012 Image collected & cropped by CiteAb from the following publication (//elifesciences.org/articles/08009), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-105_rabbit-polyclonal-abca1-antibody-31020241534346.jpg)
![Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - Expression of ABCA1 & CROT in livers & RIP140 in macrophages is elevated in miR-33−/−Apoe−/− mice compared with miR-33+/+Apoe−/− mice. A, Quantitative real-time PCR analysis of Abca1, Crot, Cpt1a, & Prkaa1in livers from miR-33+/+Apoe−/− & miR-33−/−Apoe−/− mice. Values from miR-33+/+Apoe−/− mice were set at 100%. Values are mean±SE (n=9 to 11each); **P<0.01. B, Western analysis of ABCA1, CROT, CPT1a, & AMPK alpha in livers from miR-33+/+Apoe−/− & miR-33−/−Apoe−/− mice. beta -actin was used as a loading control. C, Densitometry of ABCA1, CROT, CPT1a, & AMPK alpha in livers from miR-33+/+Apoe−/− & miR-33−/−Apoe−/− mice. Values from miR-33+/+Apoe−/− mice were set at 100%. Values are mean±SE (n=4 each); *P<0.05. D, Total cholesterol, free cholesterol, cholesterol ester, & triglyceride levels in livers of miR-33+/+Apoe−/− & miR-33−/−Apoe−/− mice. Values are mean±SE (n=9 to 11 each). E, HE staining of livers of miR-33+/+Apoe−/− & miR-33−/−Apoe−/− mice at age 20 weeks fed NC. Scale bar: 100 μm. F, Quantitative real-time PCR analysis of Nrip1 (RIP140) in peritoneal macrophages from miR-33+/+Apoe−/− & miR-33−/−Apoe−/− mice. Values from miR-33+/+Apoe−/− mice were set at 100%. Values are mean±SE (n=7 each). G, Western analysis of NRIP1 (RIP140) in peritoneal macrophages from miR-33+/+Apoe−/− & miR-33−/−Apoe−/− mice. GAPDH was used as a loading control. H, Densitometry of NRIP1 (RIP140) in peritoneal macrophages from miR-33+/+Apoe−/− & miR-33−/−Apoe−/− mice. Values from miR-33+/+Apoe−/− mice were set at 100%. Values are mean±SE (n=4 each); *P<0.05. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/23316322), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-105_rabbit-polyclonal-abca1-antibody-31020241616095.jpg)
![Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - Basal ABCA1 expression & function in patient-derived iRPEs. (A) Representation of patient-derived iPSC lines & genotypes harboring polymorphisms in ABCA1 that are associated with decreased or increased risk for AMD development. (B) Relative expression of ABCA1 mRNA in patient-derived iRPEs under basal conditions normalized to RPL28 & decreased risk group. (C) Western blot analysis of ABCA1 levels in patient-derived iRPEs under basal conditions. Actin was detected as loading control. ABCA1 expression was quantified & normalized to actin. (D,E) Relative expression of ABCG1 (D) & NR1H3 (E) mRNA in patient-derived iRPEs under basal conditions normalized to RPL28 & decreased risk group. (F) Cholesterol efflux in patient-derived iRPEs after direct cell labeling & in the presence of ApoAI. (G) Cholesterol efflux in patient-derived iRPEs after phagocytosis of BODIPY-cholesterol-loaded POSs & in the presence of ApoAI. (H) Quantification of phagocytosed POSs per nuclei in patient-derived iRPEs. Values shown are means ± SD (n = 3). * p < 0.05; *** p < 0.001. Unpaired Student’s t-test. (I) Representative fluorescence microscopy images of phagocytosed FITC-labeled POSs (green) & staining for ZO-1 (red) & DAPI (blue) of increased risk cell line IPS19-00096. Scale bar = 100 μm. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35328615), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-105_rabbit-polyclonal-abca1-antibody-310202416171459.jpg)
![Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - A–C) Effects of 6‐dihydroparadol & specific proteasomal, lysosomal, & calpain inhibitors on the ABCA1 protein levels. THP‐1 cells were differentiated as described in Figure 2, & then loaded with unlabeled cholesterol for 24 h. Cells were treated with or without 6‐dihydroparadol (6‐DP, 30 μm) for 24 h & incubated for another 3 h with or without the proteasome inhibitor lactacystin (10 μm), the lysosomal inhibitor chloroquine (100 μm), or the calpain inhibitor calpeptin (30 μg mL−1). The ABCA1 protein levels were detected by Western blot analysis. The bar graphs represent mean ± SD from three independent experiments. *p < 0.05, **p < 0.01, & ***p < 0.001 versus control; n.s., not significant versus control (determined by Student's t‐test or ANOVA with Bonferroni's post hoc test). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29802792), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-105_rabbit-polyclonal-abca1-antibody-310202416165615.jpg)
![Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - Suppressive effects of Ucn1 on foam cell formation & related protein expression in human monocyte-derived macrophages.Human monocytes were incubated for 7 days with RPMI-1640 supplemented with 10% human serum & the indicated concentrations of Ucn1, followed by a 19 h-incubation with 50 µg/ml oxLDL in the presence of 0.1 mmol/l [3H]oleate. Intracellular CE accumulation was determined from the radioactivity of cholesterol-[3H]oleate. Otherwise, before the addition of oxLDL, cells were harvested & subjected to immunoblotting analyses for CD36, ACAT1, or ABCA1. beta -Actin served as a loading control. Data are expressed as means ± SEM from 4–6 independent experiments with monocytes from 4–6 different donors. Baseline (1 fold) = 8.4±2.2 nmol/mg cell protein. *P<0.05, †P<0.001 vs. 0 nmol/l of Ucn1. Image collected & cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0110866), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-105_rabbit-polyclonal-abca1-antibody-310202416182616.jpg)
![Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - Effect of evodiamine on ABCA1 transcription & the degradation rate of ABCA1 protein. (a) Differentiated THP-1 macrophages were incubated with 10 μM evodiamine or 10 μM pioglitazone as positive control for 24 h. Total RNA was extracted & ABCA1 mRNA expression levels were quantified by qRT-PCR. (b) 293 T cells were transfected with a luciferase reporter construct driven by the human ABCA1 promoter as described in the Materials & Methods section. After transfection, cells were treated with 10 μM Evodiamine or 1 μM T0901317 as positive control for 24 h. (c) Differentiated THP-1 macrophages were incubated for 24 h with (black circle) or without (Veh; white circle) evodiamine (10 μM) & lysed after addition of cycloheximide (CHX; 140 μM) at different time points (0, 10, 20, 40 min). Western blot analysis shows the decline of ABCA1 protein level with cycloheximide in the presence & absence of evodiamine. All data are means ± S.D. (n = 3) vs. solvent vehicle control (DMSO), *p < 0.05, **p < 0.01, n.s. no significance (ANOVA/Bonferroni). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30038271), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-105_rabbit-polyclonal-abca1-antibody-310202416173512.jpg)
![Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - miR-33 deficiency improved cholesterol efflux in macrophages. A, Quantitative real-time PCR analysis of Abca1 & Abcg1 in macrophages from miR-33+/+Apoe−/− & miR-33−/−Apoe−/− mice. Values from miR-33+/+Apoe−/− were set at 100%. Values are mean±SE (n=7 each); ***P<0.001. B, Western blotting analysis of ABCA1 & ABCG1 in thioglycollate-elicited peritoneal macrophages from miR-33+/+Apoe−/− & miR-33−/−Apoe−/− mice. GAPDH was used as a loading control. C, Cholesterol efflux from thioglycollate-elicited peritoneal macrophages in the presence or absence of apoA-I (5 or 10 μg/mL). Values are mean±SE (n=6 each); **P<0.01. D, Cholesterol efflux from thioglycollate-elicited peritoneal macrophages in the presence or absence of HDL-C (50 or 100 μg/mL). Values are mean±SE (n=6 each); **P<0.01. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/23316322), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-105_rabbit-polyclonal-abca1-antibody-31020241616047.jpg)
![Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - A–C) Effects of 6‐dihydroparadol & specific proteasomal, lysosomal, & calpain inhibitors on the ABCA1 protein levels. THP‐1 cells were differentiated as described in Figure 2, & then loaded with unlabeled cholesterol for 24 h. Cells were treated with or without 6‐dihydroparadol (6‐DP, 30 μm) for 24 h & incubated for another 3 h with or without the proteasome inhibitor lactacystin (10 μm), the lysosomal inhibitor chloroquine (100 μm), or the calpain inhibitor calpeptin (30 μg mL−1). The ABCA1 protein levels were detected by Western blot analysis. The bar graphs represent mean ± SD from three independent experiments. *p < 0.05, **p < 0.01, & ***p < 0.001 versus control; n.s., not significant versus control (determined by Student's t‐test or ANOVA with Bonferroni's post hoc test). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29802792), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-105_rabbit-polyclonal-abca1-antibody-310202416165626.jpg)
![Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - Srebf1 is a miR-33 target gene.(a) Relative changes in lipid metabolism-related genes in the livers of miR-33−/− mice compared with miR-33+/+ mice fed NC at 16 weeks of age. (n=5–8 each,*P<0.05 in Student’s t-test). (b) Conservation of miR-33 target regions in the 3′UTR of Srebf1. Underlined sequences are the potential binding site of miR-33 seed sequences. * indicates the conservation among spieces. (c) 3′UTR reporter assay used to verify the target. Luciferase reporter activity of human & mouse SREBP-1 gene 3′UTR constructs in 293T cells overexpressing miR-control (miR-Con) & miR-33 (n=4 each, *P<0.05 & ***P<0.001 in Student’s t-test). (d) miR-33 dose-dependent changes in luciferase reporter activity of mouse Srebf1 3′UTR construct in 293T cells. miR-Con & miR-146a is used as a negative control (n=4 each, *P<0.05 & ***P<0.001 in one-way analysis of valiance test). (e) Luciferase reporter activity of the WT or mutant Srebf1 3′UTR at the potential miR-33 binding site in 293T cells (n=4 each, **P<0.01 in Student’s t-test). (f,g) Luciferase reporter activity of SRE-promoter (f) or FAS-promoter (g) in 293T cells. 293T cells were co-transfected with mouse Srebf1 with the full-length 3′UTR or without the 3′UTR, along with expression plasmids for miR-negative control, or miR-33. Values are the mean±s.e. (n=4 each, **P<0.01 versus miR-Con. ***P<0.001 versus miR-Con in one-way analysis of valiance test). (h) Western blotting analysis of SREBP-1, ABCA1, & IRS-2 in miR-33 transduced HepG2 cells & primary hepatocytes & hepatocytes prepared from miR-33+/+ & miR-33−/− mice. Representative western blot images are shown (n=4). Values are the means±s.e.m. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/24300912), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-105_rabbit-polyclonal-abca1-antibody-310202416165627.jpg)
![Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - (A) Chemical structure, (B) cytotoxicity of alpha -asarone, (C) enhancement of cholesterol efflux by alpha -asarone, (D & E) upregulation of ABCA1 & ABCG1 by alpha -asarone & beta -asarone, & (F) elevation of retinoid X receptor (RXR) alpha transcription. J774A.1 murine macrophages were exposed to 50 μg/ml oxidized low-density lipoprotein (LDL) & treated with 1–10 μM purple Perilla frutescens extracts (PPE)-alpha -asarone & 5–10 μM beta -asarone. (B) MTT assay was performed for the measurement of alpha -asarone toxicity. Graph data represent 1 of 4 independent experiments with multiple estimations. Values are expressed as the percentage cell survival relative to the untreated control cells (cell viability, 100%). (C) Cholesterol efflux was expressed as the percentage fluorescence in the medium relative to total fluorescence. (D & E) For the measurement of ABCA1 & ABCG1 expression, total cell lysates were subjected to western blot analysis with a primary antibody against ABCG1 or ABCG1. beta -actin was used as an internal control. Bar graphs (means ± SEM, n=3) represent quantitative densitometric results of the upper bands. Bar graphs denoted without a common letter indicate significant difference, P<0.05. (F) RXR alpha mRNA expression was measured by RT-PCR. GAPDH was used as a housekeeping gene for the co-amplification with RXR alpha . Image collected & cropped by CiteAb from the following publication (//www.spandidos-publications.com/10.3892/ijmm.2015.2101), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-105_rabbit-polyclonal-abca1-antibody-310202416161846.jpg)
![Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - Bilirubin significantly decreases expression of ATP‐binding cassette transporter A1 (ABCA1) protein in THP‐1 macrophages treated with LXR agonist (TO901317) to upregulate ABCA1 protein. THP‐1 cells were differentiated for 72 hours with 200 nmol/L phorbol‐12‐myristate‐13‐acetate & then loaded with unlabeled cholesterol for another 24 hours. Cells were treated with TO901317 (5 μmol/L) or solvent vehicle (0.1% dimethyl sulfoxide [DMSO]) for 24 hours. Afterward, cells were treated with bilirubin (17.1 μmol/L) or solvent vehicle (0.1% DMSO) for 16 hours. The protein levels of ABCA1 were detected by western blot analysis. The bar graphs present mean±SD from 3 independent experiments. ***P<0.001 vs control (determined by ANOVA with Bonferroni post hoc test). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28455345), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-105_rabbit-polyclonal-abca1-antibody-310202416175272.jpg)
![Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - Induction of cholesterol efflux attenuates the enhancement in HIV-1infectivity in NPCD55 cells. (A) Normal & NPCD55 cells were treated with 5 μM TO-901317 at 24 h post-infection & cultured for 72 h in the presence of the compound. At 96 h post-infection the cells were harvested & ABCA1, Gag, & beta -actin expression was detected by Western blotting analysis. All samples were loaded on the same gel. (B) AmplexRed assay was performed to measure free cholesterol content of untreated (filled) & TO-901317-treated (slashed) cells. Cholesterol content was normalized to protein concentration. (C) AmplexRed assay was performed to measure virion-associated cholesterol from purified virus produced in untreated (filled) & TO-901317-treated (slashed) infected cells. Virion-associated cholesterol content was normalized to p24 concentration. (D) TZM-bl reporter assay was performed to measure virus infectivity when cholesterol efflux was induced via TO-901317 stimulation. The ρ values were calculated by performing student T-test (*denotes < 0.05). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/22273177), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-105_rabbit-polyclonal-abca1-antibody-31020241617529.jpg)
![Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - Effects of apabetalone on ABCA1 expression & carboplatin response in ovarian cancer cells. (A) Apabetalone treatment reduced expression of ABCA1 in OVCAR-5 & OVCAR-5 CBPR cell lines. Cells were treated for 72 h with control medium (DMSO) or apabetalone (80 µM). Protein extracts from OVCAR-5 (~30 µg) were electrophoresed & immunoblotted with rabbit polyclonal ABCA1 antibody (1/1000, NB400-105, Novus Biological) & beta -actin (1/2000, Abcam) was used as a loading control. (B) Quantification of Western blot. OVCAR-5 (C), CaOV3 (D), OVCAR-5 CBPR (E) & CaOV3 CBPR (F) cell survival following treatment with carboplatin (CBP) alone (0-200 µM, black line) & in combination with apabetalone (Apa, 80 µM, purple line). (G) Carboplatin IC50 for OVCAR-5 & OVCAR-5 CBPR cells ± apabetalone. Data are mean ± SEM from three independent experiments. *P < 0.05, Student’s t-test. (H) Carboplatin IC50 for CaOV3 & CaOV3 CBPR cells ± apabetalone. Data are mean ± SEM from three independent experiments. P < 0.05, Student’s t-test. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35582032), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-105_rabbit-polyclonal-abca1-antibody-310202416161826.jpg)
![Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - Expression of ATP‐binding cassette transporter A1 (ABCA1) protein in THP‐1 macrophages treated with bilirubin & in peripheral blood mononuclear cells (PBMCs) from Gilbert syndrome (GS) patients. A, Bilirubin suppresses the expression of ABCA1 protein in THP‐1‐derived macrophages time‐dependently. THP‐1 cells were differentiated as described in Figure 1 & then loaded with unlabeled cholesterol for another 24 hours. Cells were treated with bilirubin (17.1 μmol/L) for 4, 8, 16, & 24 hours. The protein levels of ABCA1 were detected by western blotting. Control was treated with solvent vehicle (0.1% dimethyl sulfoxide). The bar graph presents mean±SD from 3 independent experiments. B, Expression of ABCA1 protein is decreased in PBMCs from participants with high bilirubin blood levels (GS) compared with healthy controls. The protein levels of ABCA1 were detected by western blotting. The bar graph presents mean±SEM (n=28 per group). *P<0.05, **P<0.01 & ***P<0.001 vs control. ns indicates not significant (determined by Student t test). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28455345), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-105_rabbit-polyclonal-abca1-antibody-31020241616374.jpg)
![Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - (A) Time course response of ABCA1 induction by pioglitazone, & (B) enhancement of ABCA1 & (C) peroxisome proliferator-activated receptor gamma (PPAR gamma ) by purple Perilla frutescens extracts (PPE). J774A.1 murine macrophages were incubated with 10 μM pioglitazone & 50 μg/ml oxidized low-density lipoprotein (LDL) in the absence or presence of 1–10 μg/ml PPE. For the measurement of expression of (A & B) ABCA1 & (C) PPAR gamma , total cell lysates were subjected to western blot analysis with a primary antibody against ABCA1 or PPAR gamma . beta -actin was used as an internal control. Bar graphs (means ± SEM, n=3) represent quantitative densitometric results of the upper bands. Bar graphs denoted without a common letter indicate significant difference, P<0.05. Image collected & cropped by CiteAb from the following publication (//www.spandidos-publications.com/10.3892/ijmm.2015.2101), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-105_rabbit-polyclonal-abca1-antibody-3102024161896.jpg)
![Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - LXR agonist-stimulated ABCA1 expression & function in patient-derived iRPEs. Patient-derived iRPE lines were stimulated for 16 h with LXR agonist & are relative to unstimulated cells shown in Figure 2. (A) Expression of ABCA1 mRNA normalized to RPL28 & relative to unstimulated cells shown in Figure 2B. (B) Western blot analysis of ABCA1 protein levels. Actin was detected as loading control. ABCA1 expression was quantified & normalized to actin. (C) Cholesterol efflux assay after direct cell labeling & in the presence of ApoAI. (D) Cholesterol efflux assay after phagocytosis of BODIPY-cholesterol-loaded POSs & in the presence of ApoAI. Data are relative to unstimulated cells shown in Figure 2F,G, respectively. Data are presented as means ± SD (n = 3). Unpaired Student’s t-test. * p < 0.05. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35328615), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-105_rabbit-polyclonal-abca1-antibody-310202416171457.jpg)
![Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - Akt inhibition by LY294002 or Akt1/2 also enhances cholesterol efflux to apoA-I from ABCA1-expressing BHK cells.A) BHK cells were induced as in Fig. 1 & then incubated with LY294002 (200 µM) for 2 h. Cells were then lysed & analysed for ABCA1, phosphorylated Akt (p-Akt) & total Akt by Western-blotting. Hsp70 was also blotted as loading control. B & C) BHK cells were labeled with [3H] cholesterol & induced with 10 nM mifepristone overnight. Cholesterol efflux was measured after 2 h incubation with BSA (1 mg/ml) or BSA plus apoA-I (5 µg/ml). Some of cells were also incubated with indicated doses of LY294002 (B) or Akt1/2 (C), in addition to apoA-I, during 2 h efflux period. Results are presented as the average of triplicate wells with standard deviation & representative of more than three independent experiments. *** P<0.0001, **P<0.001 & *P<0.05 vs apoA-I only. Image collected & cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0113789), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-105_rabbit-polyclonal-abca1-antibody-310202416163770.jpg)
![Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - Generation, differentiation & analysis of ABCA1-deficient iRPEs. (A) Immunofluorescence staining for ZO-1 (red) in 4-week cultured iRPEs. Nuclei were stained with DAPI (blue). Scale bar = 100 μm. (B) Bright-field microscopy of iRPEs. (C) Ct values of RPE marker genes BEST1, OTX2, RLBP1 & RPE65 in iRPEs & parental iPSCs obtained by qPCR. Values shown are means ± SD (n = 3). Unpaired Student’s t-test. **** p < 0.0001. (D) Sequence alignment of parts of exon 14 (top) & exon 46 (bottom) of ABCA1-deficient iRPE cell clones & parental line. (E) Western blot of ABCA1 protein levels in ABCA1-deficient iRPE cell lines & parental cell line after 16 h of stimulation with 1 μM LXR agonist. Actin was detected as loading control. (F) Relative expression of ABCA1 mRNA in ABCA1-deficient iRPE cell lines & parental cell line normalized to ACTB. Values shown are means ± SD (n = 3). One-way ANOVA with Tukey’s post hoc test. **** p < 0.0001. (G) Relative expression of ABCG1 mRNA in ABCA1-deficient iRPE cell lines & parental cell line normalized to ACTB. Values shown are means ± SD (n = 3). One-way ANOVA with Tukey’s post hoc test. ** p < 0.01; *** p < 0.001. (H) Cholesterol efflux assay in iRPEs in the presence of ApoAI and/or LXR agonist (LXR ag). Values shown are means ± SD (n = 3). Two-way ANOVA with Bonferroni post hoc test vs. DMSO + BSA control. **** p < 0.0001. (I) Bright-field (BF) microscopy & Nile Red fluorescence microscopy (overview & close-up view marked with white squares) of 4-week cultured ABCA1-deficient iRPE cell lines & parental cell line. Relative fluorescence was quantified & is shown as mean ± SD (n = 8). One-way ANOVA with Tukey’s post hoc test. * p < 0.05, **** p < 0.0001. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35328615), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-105_rabbit-polyclonal-abca1-antibody-310202416173523.jpg)
![Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - Akt inhibition enhances cholesterol efflux to apoA-I from wt MEFs, but not from TSC2-/- MEFs where mTORC1 is constitutively activated.A) Mouse embryonic fibroblasts (MEFs), wt & TSC2-/-, were induced overnight with T0901317 (10 µM). Cell lysates were collected for Western blotting for phosphorylated S6K & total S6K. B) wt & TSC2-/- MEFs were incubated with or without T0901317 (10 µM) overnight. Some of cells were then incubated with apoA-I (10 µg/ml) or apoA-I plus DEBC (25 µM) for 2 h. The expression of ABCA1, phosphorylated Akt, total Akt & loading control hsp70 were analyzed by Western blotting. C) wt & TSC2-/- were labeled with [3H] cholesterol for 1 day & then incubated with or without T0901317 (10 µM) overnight. Some of cells were then incubated with apoA-I (10 µg/ml) or apoA-I plus DEBC (25 µM) for 2 h to analyze cholesterol efflux. Data presented as the average of triplicate wells with standard deviation & representative of at least three independent experiments. *** P<0.0001 vs apoA-I only. Image collected & cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0113789), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-105_rabbit-polyclonal-abca1-antibody-310202416163724.jpg)
![Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - Akt inhibition by DEBC enhances cholesterol efflux to apoA-I specifically from ABCA1-expressing BHK cells.A) BHK-ABCA1 cells were induced with mifepristone (10 nM) overnight & then incubated with indicated doses of DEBC for 2 h. Cells were then lysed & Western-blotted for ABCA1, phosphorylated Akt (p-Akt) & total Akt. Hsp70 was also blotted as loading control. B) BHK-ABCA1 cells were labeled with [3H] cholesterol & induced overnight as above. After 2 h incubation with BSA (1 mg/ml) or BSA plus apoA-I (5 µg/ml), cholesterol efflux was measured as described in the Methods section. Some of the cells were also incubated with indicated doses of DEBC, in addition to apoA-I, during 2 h efflux period. C) BHK-ABCA1 & BHK-A937V cells were induced with mifepristone (10 nM) overnight. 2 h Cholesterol efflux was measured as above either with or without DEBC (25 µM). Results are presented as the average of triplicate wells with standard deviation & representative of more than three independent experiments. *** P<0.0001 & **P<0.001 vs apoA-I only. Image collected & cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0113789), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-105_rabbit-polyclonal-abca1-antibody-310202416175212.jpg)
![Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - LXRs control expression of genes involved in cholesterol homeostasis & fatty acid synthesis in MPECs.(A) qPCR analysis of Abca1, Abcg1 & Idol levels in WT (+/+) & Lxr alpha beta −/− (lxr−/−) MPECs after DMSO (vehicle) or T0901317 stimulation (B) Effect of 9-cis retinoic acid and/or T0901317 stimulation on Abca1 accumulation levels in WT (+/+) & Lxr alpha beta −/− (lxr−/−) MPECs (C) qPCR analysis of Srebp1, Acc, & Fas levels in WT (+/+) & Lxr alpha beta −/− (lxr−/−) MPECs after DMSO (vehicle) or T0901317 stimulation. (qPCR analysis results from 4 independant experiments & was normalized using 36b4 gene). *p<0.05, **p<0.01, ***p<0.001 in Student’s t test. Error bars represent mean ± SEM. (D) Western blot analysis was performed on WT (+/+) or Lxr alpha beta −/− MPECs using Srebp1c, Abca1 & beta -Actin antibodies. (E) Oil-Red O staining (ORO) & Normarski/Dapi of WT (+/+) & Lxr alpha beta −/− MPECs, or WT MEFs, treated for 48h with DMSO (vehicle) or T0901317 (1 µM). Head arrows indicate lipid droplets. Scale bars 100 µm. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/23554947), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-105_rabbit-polyclonal-abca1-antibody-31020241616059.jpg)
![Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - (A) Time course response of ABCA1 induction by pioglitazone, & (B) enhancement of ABCA1 & (C) peroxisome proliferator-activated receptor gamma (PPAR gamma ) by purple Perilla frutescens extracts (PPE). J774A.1 murine macrophages were incubated with 10 μM pioglitazone & 50 μg/ml oxidized low-density lipoprotein (LDL) in the absence or presence of 1–10 μg/ml PPE. For the measurement of expression of (A & B) ABCA1 & (C) PPAR gamma , total cell lysates were subjected to western blot analysis with a primary antibody against ABCA1 or PPAR gamma . beta -actin was used as an internal control. Bar graphs (means ± SEM, n=3) represent quantitative densitometric results of the upper bands. Bar graphs denoted without a common letter indicate significant difference, P<0.05. Image collected & cropped by CiteAb from the following publication (//www.spandidos-publications.com/10.3892/ijmm.2015.2101), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-105_rabbit-polyclonal-abca1-antibody-310202416171495.jpg)
![Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - Anti-ApoA-1 IgGs upregulate ABCA1. ABCA1 was increased after 16 & 24 h of anti-ApoA-1 IgG exposure to HMDM at the mRNA level as revealed by RT-PCR (a) as well as at the protein level after 24 h anti-apoA-1 IgG stimulation, as revealed by Western blot analysis (b). In panel a, data are expressed as fold change expression of the mean ± SD of ABCA1 calculated by delta delta CT method of six independent experiments (n = 6) & values were normalized to untreated condition. p-values were calculated using the Student’s t-test: * p < 0.05, ** p < 0.01, **** p < 0.0001. (b) One of four representative Western blots is shown. Data are the mean ± SD of band intensity volume/actin intensity volume of four independent experiments (n = 4). p-values were calculated using the Student’s t-test: * p = 0.02, ** p = 0.005. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31766415), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-105_rabbit-polyclonal-abca1-antibody-31020241616076.jpg)
![Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - A–C) Effects of 6‐dihydroparadol & specific proteasomal, lysosomal, & calpain inhibitors on the ABCA1 protein levels. THP‐1 cells were differentiated as described in Figure 2, & then loaded with unlabeled cholesterol for 24 h. Cells were treated with or without 6‐dihydroparadol (6‐DP, 30 μm) for 24 h & incubated for another 3 h with or without the proteasome inhibitor lactacystin (10 μm), the lysosomal inhibitor chloroquine (100 μm), or the calpain inhibitor calpeptin (30 μg mL−1). The ABCA1 protein levels were detected by Western blot analysis. The bar graphs represent mean ± SD from three independent experiments. *p < 0.05, **p < 0.01, & ***p < 0.001 versus control; n.s., not significant versus control (determined by Student's t‐test or ANOVA with Bonferroni's post hoc test). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29802792), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-105_rabbit-polyclonal-abca1-antibody-31020241618917.jpg)
![Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - ABCA1 protein expression is upregulated in ovarian cancer cells with acquired carboplatin resistance. ABCA1 expression in OVCAR-5 (A) & CaOV3 (C) & carboplatin resistant OVCAR-5 CBPR (B) & CaOV3 CBPR (D) by immunocytochemistry using rabbit polyclonal ABCA1 antibody (1/100, NB400-105, Novus Biological). (E) OVCAR-5 cells with Rabbit IgG & (F) CaOV3 cells with Rabbit IgG. (G) Protein extracts from OVCAR-5 (~30 µg) & CaOV3 cell lines (~60 µg) were electrophoresed & immunoblotted with rabbit polyclonal ABCA1 antibody (1/1000, NB400-105, Novus Biological), & beta -actin (1/2000, Abcam) was used as a loading control. A major band was detected at ~250 kDa, which is the predicted size for ABCA1. (H) Quantitation of ABCA1 Western blots. Data are from 2-4 independent experiments. Statistical significance was determined using the Student’s t-test, *P < 0.05. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35582032), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-105_rabbit-polyclonal-abca1-antibody-310202416171478.jpg)
![Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - Evodiamine enhances apo A1-mediated ChE from THP-1 macrophages & increases ABCA1 protein level. (a) Differentiated THP-1 cells were loaded with [3H]-cholesterol together with the indicated treatments for 24 h. On the next day, the cells were washed twice with PBS & incubated with the same compounds [solvent vehicle control (Veh; ≤0.1% DMSO), evodiamine (1–20 μM), & the PPAR gamma agonist pioglitazone (10 μM) as positive control] with or without 10 µg/mL apo A1. Extracellular as well as intracellular radioactivities were quantified with scintillation counter. Differentiated THP-1-derived macrophages were treated with solvent vehicle control (Veh; ≤0.1% DMSO), evodiamine (10 μM), & the PPAR gamma agonist pioglitazone (10 μM) as positive control. After 24 h incubation, the cells were lysed & 20 μg protein was resolved via SDS-PAGE. Immunodetection was performed with antibodies against the indicated proteins, ABCA1 (b), ABCG1 (c), & SR-B1 (d), & visualized by chemiluminescence detection. All experiments were performed at least three times & data are presented as means ± S.D. vs. solvent vehicle control, *p < 0.05, **p < 0.01, ***p < 0.001, n.s. no significance (ANOVA/Bonferroni). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30038271), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-105_rabbit-polyclonal-abca1-antibody-310202416161816.jpg)
![Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - A–C) Effects of 6‐dihydroparadol & specific proteasomal, lysosomal, & calpain inhibitors on the ABCA1 protein levels. THP‐1 cells were differentiated as described in Figure 2, & then loaded with unlabeled cholesterol for 24 h. Cells were treated with or without 6‐dihydroparadol (6‐DP, 30 μm) for 24 h & incubated for another 3 h with or without the proteasome inhibitor lactacystin (10 μm), the lysosomal inhibitor chloroquine (100 μm), or the calpain inhibitor calpeptin (30 μg mL−1). The ABCA1 protein levels were detected by Western blot analysis. The bar graphs represent mean ± SD from three independent experiments. *p < 0.05, **p < 0.01, & ***p < 0.001 versus control; n.s., not significant versus control (determined by Student's t‐test or ANOVA with Bonferroni's post hoc test). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29802792), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-105_rabbit-polyclonal-abca1-antibody-310202416161840.jpg)
![Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - Functional miR-33 responsive elements in the 3′UTR of ATP8B1 & ABCB11A,B. Conserved sequences in the 3′UTR of ATP8B1 & ABCB11 are partially complementary to miR-33. The element in human ATP8B1 is located 1877–1897 nt after the stop codon. The element in ABCB11 overlaps the stop codon in primates, while rodents show a conserved sequence 732–751 nt after the stop codon.C,D. Luciferase assays in HEK293 cells using the whole 3′UTR of human or murine ATP8B1 & ABCB11, or a single copy of the responsive elements (RE) identified above, or mutant responsive elements (RE*; where AATGCA was mutated to GGGTTG to prevent complementarity to the seed sequence of the miRNA), co-transfected with (closed bars) or without (open bars) a vector to overexpress miR-33. In grey, data from empty (negative control) & R33 (positive control containing a 100% match to miR-33) reporter vectors.E,F. Relative mRNA expression of canalicular transporters in primary murine hepatocytes (n = 4 dishes/condition) & human HuH-7 hepatoma cells (n = 3 dishes/condition) transduced 48 h with empty or miR-33 adenovirus.G. Relative protein levels in HuH7 cells transduced with empty or miR-33 adenovirus. Some cells were incubated for 16 h in the presence of FXR:RXR agonists (2 µmol/L GW4064 : 1 µmol/L 9-cis-retinoic acid) to induce ABCB11. Asterisk indicates a non-specific band. Data shown as mean ± SD; **p < 0.01. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/22767443), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-105_rabbit-polyclonal-abca1-antibody-31020241616034.jpg)
![Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - (A) Chemical structure, (B) cytotoxicity of alpha -asarone, (C) enhancement of cholesterol efflux by alpha -asarone, (D & E) upregulation of ABCA1 & ABCG1 by alpha -asarone & beta -asarone, & (F) elevation of retinoid X receptor (RXR) alpha transcription. J774A.1 murine macrophages were exposed to 50 μg/ml oxidized low-density lipoprotein (LDL) & treated with 1–10 μM purple Perilla frutescens extracts (PPE)-alpha -asarone & 5–10 μM beta -asarone. (B) MTT assay was performed for the measurement of alpha -asarone toxicity. Graph data represent 1 of 4 independent experiments with multiple estimations. Values are expressed as the percentage cell survival relative to the untreated control cells (cell viability, 100%). (C) Cholesterol efflux was expressed as the percentage fluorescence in the medium relative to total fluorescence. (D & E) For the measurement of ABCA1 & ABCG1 expression, total cell lysates were subjected to western blot analysis with a primary antibody against ABCG1 or ABCG1. beta -actin was used as an internal control. Bar graphs (means ± SEM, n=3) represent quantitative densitometric results of the upper bands. Bar graphs denoted without a common letter indicate significant difference, P<0.05. (F) RXR alpha mRNA expression was measured by RT-PCR. GAPDH was used as a housekeeping gene for the co-amplification with RXR alpha . Image collected & cropped by CiteAb from the following publication (//www.spandidos-publications.com/10.3892/ijmm.2015.2101), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-105_rabbit-polyclonal-abca1-antibody-310202416175262.jpg)
![Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - Gas6 treatment enhances expression of LXR alpha & LXR beta & their target genes in BMDM.Mouse BMDM were stimulated with 400 ng/ml Gas6, 1 μM T0901317, 10 ng/ml interferon (IFN)-gamma , 10 ng/ml IL-4, or 100 ng/ml LPS for 4 h (a,b) or 400 ng/ml Gas6 for the indicated times (c–g). (a,b,e) The amounts of the LXR alpha , LXR beta , ABCA1, ABCG1, ApoE, AIM, Arg2, VEGF, YM1, & Arg1 mRNAs were analyzed by real-time PCR & normalized to that of Hprt mRNA. (c,d,f,g) The relative abundances of LXR alpha , LXR beta , ABCA1, ABCG1, ApoE, Aim, Arg2, & VEGF proteins were determined by Western blotting analysis. The relative densitometric intensity was determined for each band & normalized to beta -actin. Data in all bar graphs are means ± SEM of three independent experiments. *P < 0.05 compared with control. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27406916), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-105_rabbit-polyclonal-abca1-antibody-310202416175244.jpg)
![Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - (A) Time course response of ABCA1 induction by TO-091317 & (B) upregulation of ABCA1 by purple Perilla frutescens extracts (PPE), & (C) enhancement of liver X receptor (LXR) alpha induction by PPE. J774A.1 murine macrophages were cultured with 1 μM TO-091317 or 50 μg/ml Cu2+-oxidized low-density lipoprotein (LDL) in the absence or presence of 1–10 μg/ml PPE. For the measurement of expression of (A & B) ABCA1 & (C) LXR alpha , total cell lysates were subjected to western blot analysis with a primary antibody against ABCA1 or LXR alpha . beta -actin was used as an internal control. Bar graphs (means ± SEM, n=3) represent quantitative densitometric results of the upper bands. Bar graphs denoted without a common letter indicate significant difference, P<0.05. Image collected & cropped by CiteAb from the following publication (//www.spandidos-publications.com/10.3892/ijmm.2015.2101), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-105_rabbit-polyclonal-abca1-antibody-31020241616565.jpg)
![Western Blot: ABCG1 Antibody - BSA Free [NB400-132] - ABCG-1 protein level in control and glycolaldehyde-treated macrophages. J774 macrophages were overloaded with oxidized LDL (50 ug/mL de DMEM) for 48 h. In the last 5h, cells were incubated with 0.25 mM glycolaldehyde (GAD; black bars) and 1 uM LXR agonist (T0901317). Control cells (C; gray bars) were incubated with T0901317 alone. Cells were scrapped into TBS containing protease inhibitors. Equal amounts of cell protein were applied into a 6% polyacrylamide electrophoresis gel and immunoblot was performed utilizing anti ABCG-1 antibody. Data (arbitrary units; n = 4) were corrected per beta-actin. Image collected and cropped by CiteAb from the following publication (//lipidworld.biomedcentral.com/articles/10.1186/1476-511X-10-172), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/ABCG1-Antibody---BSA-Free-Western-Blot-NB400-132-img0016.jpg "Western Blot: ABCG1 Antibody - BSA Free [NB400-132] - ABCG-1 protein level in control and glycolaldehyde-treated macrophages. J774 macrophages were overloaded with oxidized LDL (50 ug/mL de DMEM) for 48 h. In the last 5h, cells were incubated with 0.25 mM glycolaldehyde (GAD; black bars) and 1 uM LXR agonist (T0901317). Control cells (C; gray bars) were incubated with T0901317 alone. Cells were scrapped into TBS containing protease inhibitors. Equal amounts of cell protein were applied into a 6% polyacrylamide electrophoresis gel and immunoblot was performed utilizing anti ABCG-1 antibody. Data (arbitrary units; n = 4) were corrected per beta-actin. Image collected and cropped by CiteAb from the following publication (//lipidworld.biomedcentral.com/articles/10.1186/1476-511X-10-172), licensed under a CC-BY license.")
![Immunohistochemistry-Paraffin: ABCG1 Antibody - BSA Free [NB400-132] - Staining of human lung, alveolar macrophages.](http://images.novusbio.com/fullsize/ABCG1-Antibody---BSA-Free-Immunohistochemistry-Paraffin-NB400-132-img0013.jpg)
![Flow (Intracellular): ABCG1 Antibody - BSA Free [NB400-132] - RAW 246.7 cells were either untreated (A) or serum starved for 24 hours, and then treated with 1uM TO9 for 24 hours (B). An intracellular stain was performed with NB400-132 (blue) and a matched isotype control NB810-56910 (orange). Cells were fixed with 4% paraformaldehyde, following fixation, cells were permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 5 ug/mL for 30 minutes at room temperature, followed by Goat Anti-Rabbit Dylight 550-conjugated antibody.](http://images.novusbio.com/fullsize/ABCG1-Antibody-BSA-Free-Flow-Intracellular-NB400-132-img0012.jpg)
![<b>Biological Strategies Validation. </b>Western Blot: ABCG1 Antibody - BSA Free [NB400-132] - Cells were pretreated with 5 uM F12511 or 5 uM MG132 for 30 min and then exposed to 5 or 50 uM 24S-OHC for 6 h. Whole-cell lysates were immunoblotted with antibodies specific for ABCG1 or beta-actin. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31285856/) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/ABCG1 Antibody - BSA Free-Western Blot-NB400-132-img0017.jpg)
![Western Blot: ABCG1 Antibody - BSA Free [NB400-132] - Detection of ABCG1 in J774 mouse macrophages. Image provided by Dr. Angeliki Chroni of the National Centre for Scientific Research Demokritos.](http://images.novusbio.com/fullsize/ABCG1-Antibody---BSA-Free-Western-Blot-NB400-132-img0005.jpg)
![Western Blot: ABCG1 Antibody - BSA Free [NB400-132] - Raw 264.7 (A), and Raw 264.7 + 10uM T09 18 hr (B) cell lysate using ABCG1 antibody at 2 ug/mL.](http://images.novusbio.com/fullsize/ABCG1-Antibody---BSA-Free-Western-Blot-NB400-132-img0009.jpg)
![Western Blot: ABCG1 Antibody - BSA Free [NB400-132] - Detection of ABCG1 in mouse peritoneal macrophages. Lane 1: untreated mouse peritoneal macrophages, Lane 2: 22-(R)-hydrocholesterol treated macrophages, Lane 3: T0901713 treated macrophages, Lane 4: T091713 treated macrophages.](http://images.novusbio.com/fullsize/ABCG1-Antibody---BSA-Free-Western-Blot-NB400-132-img0004.jpg)
![Western Blot: ABCG1 Antibody - BSA Free [NB400-132] - SAA has little impact on the impairment in biliary and fecal excretion of macrophage-derived 3H-cholesterol during endotoxemia. WT and SAAKO mice were injected subcutaneously with PBS or 0.8 ug/g LPS as indicated, followed 4 hr later by intraperitoneal injection of 3H-cholesterol-labeled J774 macrophages. ABCG1 in liver lysates (40 ug protein) was identified by immunoblotting and quantified by densitometry. Results from each of the 3 experiments (n = 4-5 per group per experiment) were expressed relative to PBS-injected WT mice after normalization to beta-actin. A representative western blot is shown. Image collected and cropped by CiteAb from the following publication (//www.hindawi.com/journals/jl/2013/283486/), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/ABCG1-Antibody---BSA-Free-Western-Blot-NB400-132-img0014.jpg)
![Western Blot: ABCG1 Antibody - BSA Free [NB400-132] - 6‐Dihydroparadol increases A) ABCA1 & B) ABCG1 protein stability. THP‐1 cells were differentiated as described in Figure 2. Then cells were loaded with unlabeled cholesterol & treated with 6‐dihydroparadol (10 μm), or solvent vehicle (0.1% DMSO, control) for 24 h. Cells were lysed at different time points (0, 1, 2, 3, 4, & 6 h) after treatment with the protein synthesis inhibitor cycloheximide (CHX, 100 μm). The protein levels of both ABCA1 & ABCG1 were detected by Western blot analysis. The data points represent mean ± SD from three independent experiments. *p < 0.05 & **p < 0.01 versus control at the same time point (determined by Student's t‐test). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29802792), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-132_rabbit-polyclonal-abcg1-antibody-310202415291917.jpg)
![Western Blot: ABCG1 Antibody - BSA Free [NB400-132] - Evodiamine enhances apo A1-mediated ChE from THP-1 macrophages & increases ABCA1 protein level. (a) Differentiated THP-1 cells were loaded with [3H]-cholesterol together with the indicated treatments for 24 h. On the next day, the cells were washed twice with PBS & incubated with the same compounds [solvent vehicle control (Veh; ≤0.1% DMSO), evodiamine (1–20 μM), & the PPAR gamma agonist pioglitazone (10 μM) as positive control] with or without 10 µg/mL apo A1. Extracellular as well as intracellular radioactivities were quantified with scintillation counter. Differentiated THP-1-derived macrophages were treated with solvent vehicle control (Veh; ≤0.1% DMSO), evodiamine (10 μM), & the PPAR gamma agonist pioglitazone (10 μM) as positive control. After 24 h incubation, the cells were lysed & 20 μg protein was resolved via SDS-PAGE. Immunodetection was performed with antibodies against the indicated proteins, ABCA1 (b), ABCG1 (c), & SR-B1 (d), & visualized by chemiluminescence detection. All experiments were performed at least three times & data are presented as means ± S.D. vs. solvent vehicle control, *p < 0.05, **p < 0.01, ***p < 0.001, n.s. no significance (ANOVA/Bonferroni). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30038271), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-132_rabbit-polyclonal-abcg1-antibody-31020241618932.jpg)
![Western Blot: iNOS Antibody [NB300-605] - Analysis of iNOS was performed by loading 20 ug of RAW264 whole cell lysate untreated (left lane) or stimulated with LPS at 1 ug/mL for 16 hours (right lane) and 10 uL of PageRuler Plus Prestained Protein Ladder onto a 4-20% Tris-Glycine polyacrylamide gel. Proteins were transferred to a nitrocellulose membrane and blocked with 5% Milk in TBST for at least 1 hour. The membrane was probed with an iNOS Rabbit polyclonal antibody at a dilution of 1:1000 overnight at 4C on a rocking platform, washed in TBST, and probed with a Goat anti-Rabbit IgG (H+L) Secondary Antibody, HRP conjugate at a dilution of 1:1000 for 1 hour. Chemiluminescent detection was performed using SuperSignal West Pico.](http://images.novusbio.com/fullsize/iNOS-Antibody-Western-Blot-NB300-605-img0015.jpg "<b>Biological Strategies Validation. </b>Western Blot: iNOS Antibody [NB300-605] - Analysis of iNOS was performed by loading 20 ug of RAW264 whole cell lysate untreated (left lane) or stimulated with LPS at 1 ug/mL for 16 hours (right lane) and 10 uL of PageRuler Plus Prestained Protein Ladder onto a 4-20% Tris-Glycine polyacrylamide gel. Proteins were transferred to a nitrocellulose membrane and blocked with 5% Milk in TBST for at least 1 hour. The membrane was probed with an iNOS Rabbit polyclonal antibody at a dilution of 1:1000 overnight at 4C on a rocking platform, washed in TBST, and probed with a Goat anti-Rabbit IgG (H+L) Secondary Antibody, HRP conjugate at a dilution of 1:1000 for 1 hour. Chemiluminescent detection was performed using SuperSignal West Pico.")
![<b>Biological Strategies Validation. </b>Immunohistochemistry-Paraffin: iNOS Antibody [NB300-605] - Immunohistochemistry was performed on normal deparaffinized human Lung tissue.](http://images.novusbio.com/fullsize/iNOS-Antibody-Immunohistochemistry-Paraffin-NB300-605-img0010.jpg)
![Immunohistochemistry-Paraffin: iNOS Antibody [NB300-605] - Immunohistochemistry was performed on normal deparaffinized human Heart tissue.](http://images.novusbio.com/fullsize/iNOS-Antibody-Immunohistochemistry-Paraffin-NB300-605-img0016.jpg)
![Immunocytochemistry/Immunofluorescence: iNOS Antibody [NB300-605] - Analysis of iNOS in A549 Cells. Cells were grown on chamber slides and fixed with formaldehyde prior to staining. Cells were probed without (control) or with a iNOS polyclonal antibody at a dilution of 1:20 overnight at 4C, washed with PBS and incubated with a DyLight 488 conjugated secondary antibody. iNOS staining (green), F-Actin staining with Phalloidin (red) and nuclei with DAPI (blue) is shown.](http://images.novusbio.com/fullsize/iNOS-Antibody-Immunocytochemistry-Immunofluorescence-NB300-605-img0012.jpg)
![<b>Biological Strategies Validation. </b>Western Blot: iNOS Antibody [NB300-605] - iNOS in stimulated astrocytes. Western blot image submitted by a verified customer review.](http://images.novusbio.com/fullsize/iNOS-Antibody-Western-Blot-NB300-605-img0005.jpg)
![<b>Biological Strategies Validation. </b>Western Blot: iNOS Antibody [NB300-605] - LCA-induced oxidative stress in 4T1 breast cancer cells. The 4T1 cells were treated with LCA for 48 h, then the indicated measurements were performed. The level of iNOS protein was detected by western blotting (n = 3). Image collected and cropped by CiteAb from the following publication (//www.mdpi.com/2072-6694/11/9/1255), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/iNOS-Antibody-Western-Blot-NB300-605-img0017.jpg)
![Immunocytochemistry/Immunofluorescence: iNOS Antibody [NB300-605] - Analysis of iNOS in NIH-3T3 Cells. Cells were grown on chamber slides and fixed with formaldehyde prior to staining. Cells were probed without (control) or with a iNOS polyclonal antibody at a dilution of 1:20 overnight at 4C, washed with PBS and incubated with a DyLight 488 conjugated secondary antibody. iNOS staining (green), F-Actin staining with Phalloidin (red) and nuclei with DAPI (blue) is shown.](http://images.novusbio.com/fullsize/iNOS-Antibody-Immunocytochemistry-Immunofluorescence-NB300-605-img0013.jpg)
![Western Blot: iNOS Antibody - BSA Free [NB300-605] - Stimulation of IMA 2.1 cells had no effect on relative survival after viral infection. IMA 2.1 cells were stimulated with LPS (10 µg/ml), IFN-gamma , (10 ng/ml) LPS + IFN-gamma , IL-4 (10 ng/ml), FGF (5 ng/ml) or FGF + LPS for 24 h in medium with 2% FBS. Polarization of cells was analyzed by Griess assay (a), Western blot (b) & FACS analysis by detection of MHCII+ cells (c). d MTT assay was performed to detect the relative percentage of VACV-mediated cell death in the presence of stimulating factors. e Viral replication was analyzed by standard plaque assay in the presence of stimulating factors. All experiments were performed in triplicate. Image collected & cropped by CiteAb from the following publication (//www.translational-medicine.com/content/13/1/216), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-605_rabbit-polyclonal-inos-antibody-310202415371975.jpg)
![Immunocytochemistry/ Immunofluorescence: iNOS Antibody - BSA Free [NB300-605] - Nfix is mainly expressed by anti-inflammatory MPs. (a) Percentage of F4/80+ MPs positive for Nfix in Tibialis Anterior muscles (TA) of WT mice injected by CTX at D2, D4 & D7, post-injury. Immunostaining for F4/80 (green), Nfix (red) & DAPI (blue) at D4 & D7 after CTX injection; (b) Percentage of Ly6C+ & Ly6C- sorted MPs positive for Nfix in TA muscles of WT mice injected by CTX at D2, D4 & D7 post-injury; (c) Percentage of Nfix+ MPs after M1 & M2c polarization (with IFN gamma & IL10, respectively). * p < 0.05; *** p < 0.001; for (b) * p < 0.05 Ly6C+ vs. Ly6C+ at D4 & D7; # p < 0.05 Ly6C− D7 vs. D2. Results are means ± SEM of at least three independent experiments. Scale bar = 50 μm. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32183151), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-605_rabbit-polyclonal-inos-antibody-31020241517136.jpg)
![Western Blot: iNOS Antibody - BSA Free [NB300-605] - Indolepropionic acid (IPA) induced oxidative stress, cellular energy stress, & decreased the proportions of cancer stem cells. 500,000 cells/well 4T1 cells were treated with IPA in the concentrations indicated for 24 h; then, (A) lipid peroxidation was measured by TBARS assay, & (B) 4HNE expression was assessed by Western blotting (representative figure, n = 3). In the same cells (C), the protein expression of NRF2 (at 68 kDa) & iNOS were determined by Western blotting (n = 3), while (D) the mRNA expression of catalase (cat) was determined by RT-qPCR (n = 3). (E) The expression of the indicated proteins (pACC, ACC, FOXO1, & PGC-1 beta ) were determined by Western blotting (n = 3, except for PGC-1 beta , where n = 2). (F) 100,000 cells/well 4T1 cells were treated with the indicated concentration of IPA for 24 h; then, the proportions of aldehyde dehydrogenase-positive cells were determined in Aldefluor assays using flow cytometry (n = 3). For Western blots, a typical experiment was displayed. Fold data were log2 transformed to achieve normal distribution. Statistical significance was determined using the ANOVA test followed by Dunnett’s post-hoc test, except for panel F, where Student’s t-test was used. * & *** indicate statistically significant difference between control & treated samples at p < 0.05 & p < 0.001, respectively. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32854297), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-605_rabbit-polyclonal-inos-antibody-310202416175250.jpg)
![Western Blot: iNOS Antibody - BSA Free [NB300-605] - NRF2 activation modulated LCA-induced oxidative stress responses in 4T1 breast cancer cells. The 4T1 cells were treated with 0.3 μm LCA & the NRF2 activator RA839 or tBHQ in the concentrations indicated for 48 h. Lipid peroxidation was determined by measuring (A) TBARS (n = 4) & (B,C) 4-HNE levels using western blotting (n = 3). (D) The 4T1 cells were treated with LCA (0.3 μm) and/or GSH & NAC (both at 5 mm) antioxidants for 48 h, then total protein concentration was determined using the sulforhodamine B assay (n = 3). For statistical analysis ANOVA test was used followed by the Dunnett post-hoc test, where all groups were compared to the LCA-treated cohort. Data are plotted as mean ± SEM. ** p < 0.01, LCA vs. LCA/NRF2-activator-treated groups (GSH, reduced glutathione; LCA, lithocholic acid; NAC, N-acetylcysteine; TBARS, thiobarbituric acid reactive substances; 4HNE, 4-hydroxynonenal). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31461945), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-605_rabbit-polyclonal-inos-antibody-31020241616373.jpg)
![Western Blot: iNOS Antibody - BSA Free [NB300-605] - Impaired amount of virus progeny after stimulation of BV-2 cells with IFN-gamma or IFN-gamma & LPS. BV-2 cells were stimulated with LPS (10 µg/ml), IFN-gamma , (10 ng/ml), LPS + IFN-gamma or IL-4 (10 ng/ml) for 24 h in medium with 2% FBS. Polarization of cells was analyzed by Griess assay (a), Western blot (b) & by detection of the percentage of MHCII+ cells by FACS analysis (c). The amount of virus progeny (pfu/ml) was analyzed by standard plaque assay in the presence of stimulating factors & in normal growth medium in cells & supernatants (d). Statistical analysis was performed related to infection medium. To analyze the recovery of viral replication, normal growth medium was applied after infection of pre-stimulated cells. Standard plaque assay was performed to determine viral progeny in cells & supernatant after 24, 48, 72 & 96 hpi (e). To analyze the relative survival of the cells in the presence of stimulating factors a MTT assay was performed (f). The cellular density of stimulated cells relative to unstimulated (w/o) cells was detected via optical density measurement after 24 & 48 h of cultivation (g). Two-sided t test with unequal variances was used for statistics *p < 0.05, **p < 0.01, ***p < 0.001. Active replication was defined as virus titer above the virus titer of the infection medium (red line). All experiments were performed in triplicate & repeated in an independent experiment. Image collected & cropped by CiteAb from the following publication (//www.translational-medicine.com/content/13/1/216), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-605_rabbit-polyclonal-inos-antibody-310202416175240.jpg)
![Western Blot: iNOS Antibody - BSA Free [NB300-605] - Inhibitory effect of MMPP on amyloidogenesis & STAT3 translocation in astrocytes & microglia cells. The expression of APP, BACE1 & C99 was detected by Western blotting using specific antibodies in astrocytes (a) & microglia cells (b). Each blot is representative of three experiments. The activity of beta -secretase was investigated using assay kit in astrocytes (c) & microglia cells (d). Values are presented as mean ± S.D. of the three independent experiments performed in triplicate. #p < 0.05 compared to control, *p < 0.05 compared to LPS. Iba-1, COX-2, & iNOS proteins were detected by Western blotting using specific antibodies in astrocytes (e) & microglia cells (f). NO level was measured in astrocytes (g) & microglia cells (h). Activation of STAT3 was investigated using EMSA in astrocytes (i) microglial cells (j) were determined & the expression of STAT3 & phopho-STAT3 was also detected by Western blotting using specific antibodies (k), (l). For the cropped images, samples were run in the same gels under same experimental conditions & processed in parallel. Each band is representative for three experiments Image collected & cropped by CiteAb from the following publication (//link.springer.com/10.1007/s12017-017-8469-3), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-605_rabbit-polyclonal-inos-antibody-310202416163790.jpg)
![Western Blot: Sodium Potassium ATPase Alpha 1 Antibody (464.6) [NB300-146] - Transfected SK-N-AS cells express ICAM-2 transcripts and proteins. ICAM-2 WT and variants localized to cell membranes. Experimental details are included in Methods. Image collected and cropped by CiteAb from the following publication (//bmccancer.biomedcentral.com/articles/10.1186/1471-2407-13-261), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/Sodium-Potassium-ATPase-Alpha-1-Antibody-464-6-Western-Blot-NB300-146-img0022.jpg "Western Blot: Sodium Potassium ATPase Alpha 1 Antibody (464.6) [NB300-146] - Transfected SK-N-AS cells express ICAM-2 transcripts and proteins. ICAM-2 WT and variants localized to cell membranes. Experimental details are included in Methods. Image collected and cropped by CiteAb from the following publication (//bmccancer.biomedcentral.com/articles/10.1186/1471-2407-13-261), licensed under a CC-BY license.")
![Immunocytochemistry/Immunofluorescence: Sodium Potassium ATPase Alpha 1 Antibody (464.6) [NB300-146] - The cellular model of the blood-CSF barrier. Immunofluorescent staining of Na+K+ ATPase and ABCC1, showing the expected respective apical and basolateral membrane localization in the choroidal epithelial cells. The left image is a close up of a single cell to better appreciate the polarity of distribution of the 2 proteins. Nuclei appear in blue. Arrows show the lateral cellular membranes best seen in the z direction by confocal analysis, arrowheads show the basal labeling of ABCC1. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0150945), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/Sodium-Potassium-ATPase-Alpha-1-Antibody-464-6-Immunocytochemistry-Immunofluorescence-NB300-146-img0023.jpg)
![Immunohistochemistry: Sodium Potassium ATPase Alpha 1 Antibody (464.6) [NB300-146] - Staining of human enodmetrial glands within the uterus using NB300-146. Note the absence of staining in the surrounding myometrial smooth muscle.](http://images.novusbio.com/fullsize/Sodium-Potassium-ATPase-Alpha-1-Antibody-464-6-Immunohistochemistry-NB300-146-img0012.jpg)
![Flow Cytometry: Sodium Potassium ATPase Alpha 1 Antibody (464.6) [NB300-146] - An intracellular stain was performed on NIH3T3 cells with Sodium Potassium ATPase Alpha 1 Antibody (464.6) NB300-146 (blue) and a matched isotype control MAB002 (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 1 ug/mL for 30 minutes at room temperature, followed by Mouse IgG (H+L) Cross-Adsorbed Secondary Antibody, Dylight 550 (84540, Thermo Fisher).](http://images.novusbio.com/fullsize/Sodium-Potassium-ATPase-Alpha-1-Antibody-464-6-Flow-Cytometry-NB300-146-img0027.jpg)
![Western Blot: Sodium Potassium ATPase Alpha 1 Antibody (464.6) [NB300-146] - Analysis detecting Na, K-ATPase (alpha) in porcine proximal tubule protein.](http://images.novusbio.com/fullsize/Sodium-Potassium-ATPase-Alpha-1-Antibody-464-6-Western-Blot-NB300-146-img0013.jpg)
![Immunocytochemistry/Immunofluorescence: Sodium Potassium ATPase Alpha 1 Antibody (464.6) [NB300-146] - Hek293 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-Sodium Potassium ATPase Alpha 1 (464.6) at 10 ug/ml overnight at 4C and detected with an anti-mouse DyLight 488 (Green) at a 1:500 dilution. Actin was detected with Phalloidin 568 (Red) at a 1:200 dilution. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 40X objective.](http://images.novusbio.com/fullsize/Sodium-Potassium-ATPase-Alpha-1-Antibody-464-6-Immunocytochemistry-Immunofluorescence-NB300-146-img0014.jpg)
![Immunocytochemistry/Immunofluorescence: Sodium Potassium ATPase Alpha 1 Antibody (464.6) [NB300-146] - HeLa cells were fixed for 10 minutes using 10% formalin and then permeabilized for 5 minutes using 1X TBS + 0.5% Triton X-100. The cells were incubated with anti-Sodium Potassium ATPase Alpha 1 (464.6) at 10 ug/ml overnight at 4C and detected with an anti-mouse DyLight 488 (Green) at a 1:500 dilution. Actin was detected with Phalloidin 568 (Red) at a 1:200 dilution. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 40X objective.](http://images.novusbio.com/fullsize/Sodium-Potassium-ATPase-Alpha-1-Antibody-464-6-Immunocytochemistry-Immunofluorescence-NB300-146-img0015.jpg)
![Immunocytochemistry/Immunofluorescence: Sodium Potassium ATPase Alpha 1 Antibody (464.6) [NB300-146] - Detection of ATPA1 (Green) in HepG2 cells using NB300-146. Nuclei (Blue) were counterstained using Hoechst 33258.](http://images.novusbio.com/fullsize/Sodium-Potassium-ATPase-Alpha-1-Antibody-464-6-Immunocytochemistry-Immunofluorescence-NB300-146-img0007.jpg)
![Immunocytochemistry/Immunofluorescence: Sodium Potassium ATPase Alpha 1 Antibody (464.6) [NB300-146] - The cellular model of the blood-CSF barrier. Immunofluorescent staining of Na+K+ ATPase and ABCC1, showing the expected respective apical and basolateral membrane localization in the choroidal epithelial cells. The left image is a close up of a single cell to better appreciate the polarity of distribution of the 2 proteins. Nuclei appear in blue. Arrows show the lateral cellular membranes best seen in the z direction by confocal analysis, arrowheads show the basal labeling of ABCC1. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0150945), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/Sodium-Potassium-ATPase-Alpha-1-Antibody-464-6-Immunocytochemistry-Immunofluorescence-NB300-146-img0019.jpg)
![Immunocytochemistry/Immunofluorescence: Sodium Potassium ATPase Alpha 1 Antibody (464.6) [NB300-146] - ARPE-19 cells cultured on transwell inserts for 4 weeks are not completely polarized. ARPE-19 cells were cultured up to 4 weeks on transwell inserts covered with laminin. The expression of Na+, K+-ATPase using anti-alpha1 antibody was observed mostly at the basolateral membrane. Scale bar: 10 um. Image collected and cropped by CiteAb from the following publication (//journal.frontiersin.org/article/10.3389/fphys.2016.00450/full), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/Sodium-Potassium-ATPase-Alpha-1-Antibody-464-6-Immunocytochemistry-Immunofluorescence-NB300-146-img0020.jpg)
![Flow Cytometry: Sodium Potassium ATPase Alpha 1 Antibody (464.6) [NB300-146] - An intracellular stain was performed on A549 cells with NB300-146 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 1 ug/mL for 30 minutes at room temperature, followed by mouse F(ab)2 IgG (H+L) APC-conjugated secondary antibody (F0101B, R&D Systems).](http://images.novusbio.com/fullsize/Sodium-Potassium-ATPase-Alpha-1-Antibody-464-6-Flow-Cytometry-NB300-146-img0016.jpg)
![Flow Cytometry: Sodium Potassium ATPase Alpha 1 Antibody (464.6) [NB300-146] - An intracellular stain was performed on A549 cells with NBP2-61137AF647 (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. Image using the Alexa Fluor 647 form of this antibody.](http://images.novusbio.com/fullsize/Sodium-Potassium-ATPase-Alpha-1-Antibody-464-6-Flow-Cytometry-NB300-146-img0017.jpg)
![Flow Cytometry: Sodium Potassium ATPase Alpha 1 Antibody (464.6) [NB300-146] - An intracellular stain was performed on A549 cells with - Purified NBP2-61137 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 1 ug/mL for 30 minutes at room temperature, followed by mouse F(ab)2 IgG (H+L) APC-conjugated secondary antibody (F0101B, R&D Systems). Image using the Purified form of this antibody.](http://images.novusbio.com/fullsize/Sodium-Potassium-ATPase-Alpha-1-Antibody-464-6-Flow-Cytometry-NB300-146-img0018.jpg)
![Flow Cytometry: Sodium Potassium ATPase Alpha 1 Antibody (464.6) [NB300-146] - An intracellular stain was performed on RCC4 cells with Sodium Potassium ATPase Alpha 1 Antibody (464.6) NB300-146 (blue) and a matched isotype control MAB002 (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 1 ug/mL for 30 minutes at room temperature, followed by Mouse IgG (H+L) Cross-Adsorbed Secondary Antibody, Dylight 550 (84540, Thermo Fisher).](http://images.novusbio.com/fullsize/Sodium-Potassium-ATPase-Alpha-1-Antibody-464-6-Flow-Cytometry-NB300-146-img0025.jpg)
![Flow Cytometry: Sodium Potassium ATPase Alpha 1 Antibody (464.6) [NB300-146] - An intracellular stain was performed on SK-MEL-28 cells with Sodium Potassium ATPase Alpha 1 Antibody (464.6) NB300-146 (blue) and a matched isotype control MAB002 (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 1 ug/mL for 30 minutes at room temperature, followed by Mouse IgG (H+L) Cross-Adsorbed Secondary Antibody, Dylight 550 (84540, Thermo Fisher).](http://images.novusbio.com/fullsize/Sodium-Potassium-ATPase-Alpha-1-Antibody-464-6-Flow-Cytometry-NB300-146-img0026.jpg)
![Sodium Potassium ATPase Alpha 1 Antibody (464.6) [NB300-146] - ARPE-19 cells cultured on transwell inserts for 4 weeks are not completely polarized. ARPE-19 cells were cultured up to 4 weeks on transwell inserts covered with laminin. The expression of Na+, K+-ATPase using anti-alpha1 antibody was observed mostly at the basolateral membrane. Scale bar: 10 um. Image collected and cropped by CiteAb from the following publication (//journal.frontiersin.org/article/10.3389/fphys.2016.00450/full), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/Sodium-Potassium-ATPase-Alpha-1-Antibody-464-6-NB300-146-img0024.jpg)
![Immunocytochemistry/ Immunofluorescence: Sodium Potassium ATPase Alpha 1 Antibody (464.6) [NB300-146] - The cellular model of the blood-CSF barrier.(A) Schematic representation of a choroidal villus & of the experimental set up illustrating the two-chamber culture device. Left: the choroidal epithelium which forms the actual tight barrier controlling access into the CSF [18] delimits a stroma, in which the fenestrated vessels lacking a typical blood-brain barrier phenotype, express P-selectin [4]. Right: The epithelial cell monolayer grown on the lower side of the filter separates the upper chamber corresponding to the blood/stromal or basolateral space, from the bottom chamber representing the CSF or apical compartment (adapted from [18,41]. (B & C) Immunofluorescent staining of occludin (B) & claudin 1/3 (C) showing a typical intercellular distribution of the tight junction proteins in the confluent inverted monolayers of choroidal epithelial cells. (D) Immunofluorescent staining of Na+K+ ATPase & ABCC1, showing the expected respective apical & basolateral membrane localization in the choroidal epithelial cells. The left image is a close up of a single cell to better appreciate the polarity of distribution of the 2 proteins. Nuclei appear in blue. Arrows show the lateral cellular membranes best seen in the z direction by confocal analysis, arrowheads show the basal labeling of ABCC1. Image collected & cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0150945), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-146_mouse-monoclonal-sodium-potassium-atpase-alpha-1-antibody-464-6-310202416205173.jpg)
![Western Blot: Sodium Potassium ATPase Alpha 1 Antibody (464.6) [NB300-146] - Endothelial-mesenchymal transformation (EMT) of RCECs using specific endothelial-mesenchymal transformation medium (SEMTM). (A) Immunohistochemistry of the fibroblastic markers alpha -SMA & vimentin were characteristic of fibroblasts in EMT-RCECs compared to the hexogonal morphology of Fresh RCECs (Scale bar upper panel = 100 µm, Scale bar middle & bottom panel = 50 µm). (B) RT-PCR showed that both Fresh RCECs & EMT-RCECs expressed alpha -Sma. Original gel is shown in Supplemental Fig. S2. However, qRT-PCR in the lower panel shows alpha -Sma was significantly upregulated in EMT-RCECs. (C) Western blots showed that Fresh RCECs & EMT-RCECs expressed Vimentin, Atp1a1, a marker of differentiated endothelial cells, & b-actin. Original gel & blots are shown in Supplemental Figs S3, 4. Semiquantitative analysis shows significant upregulation of the protein levels of Vimentin (p = 0.048) & downregulation of the protein level of Atp1a1 (p = 0.0043). Data expressed as mean ± SD of three replicate experiments. Student’s t test (*p < 0.05, **p < 0.01). (n = 3). RCECs: rabbit corneal endothelial cells, alpha -SMA: smooth muscle alpha -actin. Atp1a1: Na,K‐ATPase alpha ‐subunit. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30442918), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-146_mouse-monoclonal-sodium-potassium-atpase-alpha-1-antibody-464-6-310202416205123.jpg)
![Western Blot: Sodium Potassium ATPase Alpha 1 Antibody (464.6) [NB300-146] - SDS–PAGE western blot validation of the increased abundance of Annexin V, Na/K ATPase & alpha -tubulin in the EVs derived from TIS Cal51 cells compared with EVs derived from non-senescent non-treated controls. EVs isolated from TIS & control cells were immunoblotted to validate the protein expression of annexin V, Na/K ATPase & alpha -tubulin from the MS data. CD63 & HSP70 were used as loading controls. Densitometry was completed using Image J software (Fiji). All values are expressed as the mean of three independent experiments±s.e.m. The limit of ±1 skewness was set as normal distribution. Skewed data were transformed to Y=Log(Y) to fit a normal distribution. Results were analysed using the Student’s t-test with significant differences having a *P⩽0.05, **P⩽0.01, ***P⩽0.001. Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/oncsis201782), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-146_mouse-monoclonal-sodium-potassium-atpase-alpha-1-antibody-464-6-310202416203713.jpg)
![Immunocytochemistry/ Immunofluorescence: Sodium Potassium ATPase Alpha 1 Antibody (464.6) [NB300-146] - ARPE-19 cells cultured on transwell inserts for 4 weeks are not completely polarized. ARPE-19 cells were cultured up to 4 weeks on transwell inserts covered with laminin. The immunofluorescence image in (A) shows actin localization using rhodamine phalloidin. The cells are flat with stress fibers & very little circumferential actin microfilament bundles. The expression of CD147, a RPE marker, was detected using a specific antibody in the apical membrane domain (B). The expression of Na+, K+-ATPase using anti-alpha 1(C) & anti-beta 1 antibodies (D) was observed mostly at the basolateral membrane. Immunofluorescence detection with anti-human beta 2 antibody revealed a very weak signal (E). Scale bar: 10 μm. Image collected & cropped by CiteAb from the following publication (//journal.frontiersin.org/article/10.3389/fphys.2016.00450/full), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-146_mouse-monoclonal-sodium-potassium-atpase-alpha-1-antibody-464-6-310202416205189.jpg)
![Western Blot: Niemann-Pick C1 Antibody - BSA Free [NB400-148] - NPC proteins in mouse lungs. Western blot of wild type (W) littermates, NPC1 (Mut) or NPC2 (Mut) mutant mouse lungs using anti-NPC1 or -NPC2 antibody. beta-actin used as a loading control. 30 ug protein/lane. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0067084), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/Niemann-Pick-C1-Antibody---BSA-Free-Western-Blot-NB400-148-img0015.jpg "Western Blot: Niemann-Pick C1 Antibody - BSA Free [NB400-148] - NPC proteins in mouse lungs. Western blot of wild type (W) littermates, NPC1 (Mut) or NPC2 (Mut) mutant mouse lungs using anti-NPC1 or -NPC2 antibody. beta-actin used as a loading control. 30 ug protein/lane. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0067084), licensed under a CC-BY license.")
![Immunocytochemistry/Immunofluorescence: Niemann-Pick C1 Antibody - BSA Free [NB400-148] - NPC1 antibody was tested in HeLa cells with DyLight 488 (green). Nuclei were counterstained with DAPI (blue).](http://images.novusbio.com/fullsize/Niemann-Pick-C1-Antibody---BSA-Free-Immunocytochemistry-Immunofluorescence-NB400-148-img0010.jpg)
![Immunohistochemistry-Paraffin: Niemann-Pick C1 Antibody - BSA Free [NB400-148] - Staining of human brain, cortex, neurons and astrocytes.](http://images.novusbio.com/fullsize/Niemann-Pick-C1-Antibody---BSA-Free-Immunohistochemistry-Paraffin-NB400-148-img0011.jpg)
![Western Blot: Niemann-Pick C1 Antibody - BSA Free [NB400-148] - Protein expression analysis of normal and NPC-deficient cells after HIV-1 infection. Cells were uninfected or infected with VSVG-HIV-1 and harvested 96 h post-infection. NPC2, NPC1, and beta-actin protein expression was detected via Western blotting in uninfected and infected cells. Gag expression was also detected in the infected cells. Image collected and cropped by CiteAb from the following publication (//virologyj.biomedcentral.com/articles/10.1186/1743-422X-9-31), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/Niemann-Pick-C1-Antibody---BSA-Free-Western-Blot-NB400-148-img0016.jpg)
![<b>Biological Strategies Validation. </b>Immunocytochemistry/Immunofluorescence: Niemann-Pick C1 Antibody - BSA Free [NB400-148] - Immunocytochemical staining with corresponding colocalization analysis of ALIX (green) and NPC-1 (red) in fibroblasts exposed to LLOMe for 15 min. Nuclei are stained with DAPI (blue) and merged images show colocalization in yellow (n = 5). Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32409651/) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/Niemann-Pick C1 Antibody - BSA Free-Immunocytochemistry-Immunofluorescence-NB400-148-img0017.jpg)
![<b>Genetic Strategies Validation. </b>Western Blot: Niemann-Pick C1 Antibody - BSA Free [NB400-148] - Western blot shows lysates of HeLa human cervical epithelial carcinoma parental cell line and NPC1 knockout (KO) HeLa cell line. PVDF membrane was probed with 1:1000 of Rabbit Anti-Human NPC1 Polyclonal Antibody (Catalog # NB400-148) followed by HRP-conjugated Anti-Rabbit IgG Secondary Antibody (Catalog #HAF008). Specific band was detected for NPC1 at approximately 240-260 kDa (as indicated) in the parental HeLa cell line, but is not detectable in the knockout HeLa cell line. This experiment was conducted under reducing conditions.](http://images.novusbio.com/fullsize/Niemann-Pick-C1-Antibody---BSA-Free-Knockout-Validated-NB400-148-img0014.jpg)
![<b>Genetic Strategies Validation. </b>Western Blot: Niemann-Pick C1 Antibody - BSA Free [NB400-148] - HeLa lysate, BHK lysate, A431 lysate tested at 1:1000. Image from verified customer review.](http://images.novusbio.com/fullsize/Niemann-Pick-C1-Antibody---BSA-Free-Knockdown-Validated-NB400-148-img0012.jpg)
![Immunocytochemistry/ Immunofluorescence: Niemann-Pick C1 Antibody - BSA Free [NB400-148] - ESCRT complex recruited to LLOMe-damaged lysosomes promotes cell survival.Human fibroblasts were exposed to 1 mM LLOMe & when indicated, the cell permeable calcium chelator BAPTA-AM (1 µM) was added 10 min prior to LLOMe exposure. Immunocytochemical staining with corresponding colocalization analysis of a CHMP4B (green) & LAMP2 (red), b ALIX (green) & NPC-1 (red), & c CHMP4B (green) & LAMP2 (red) in fibroblasts exposed to LLOMe for 15 min. Nuclei are stained with DAPI (blue) & merged images show colocalization in yellow (n = 5). d Caspase-3 like activity in cells exposed to LLOMe for 8 h (n = 3). e Quantification of apoptotic & necrotic cells using Annexin V/PI staining in fibroblasts exposed to LLOMe for 6 h (n = 3). f Immunoblot of LAMP2 in digitonin-extracted cytosolic fractions from cells exposed to LLOMe for 2 h (n = 8) with corresponding quantitative analysis. *p < 0.05, **p < 0.01 & ***p < 0.001 compared to control (a–b) or LLOMe only (c–f). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32409651), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-148_rabbit-polyclonal-niemann-pick-c1-antibody-310202416165630.jpg)
![Western Blot: Niemann-Pick C1 Antibody - BSA Free [NB400-148] - Expression of proteins involved in extracellular lipid uptake & intracellular cholesterol trafficking following JQ1 (0.4 µM) administration to HepG2 cells for 48 hours. (A) Representative Western blot (left panel) & densitometric analysis (right panel) of SR-B1. n = 6 independent experiments. (B) Immunofluorescence analysis of SR-B1 (green). Nuclei were counterstained with DAPI. n = 3 different experiments. Scale bar: 50 µm. (C) Representative Western blot (left panel) & densitometric analysis (right panel) of LDLr. n = 5 independent experiments. (D) LDLr immunofluorescence (green). Nuclei were counterstained with DAPI. n = 3 different experiments. (E–F) Representative Western blots & densitometric analysis of NPC1 & TMEM97. Tubulin was chosen as loading control. n = 6 independent experiments. Data represent means ± SD. Statistical analysis was performed by using unpaired Student’s t test. ** p < 0.01; *** p < 0.001. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32075110), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-148_rabbit-polyclonal-niemann-pick-c1-antibody-310202416163786.jpg)
![Western Blot: Niemann-Pick C1 Antibody - BSA Free [NB400-148] - Effects of p75NTR modulation by LM11A-31 on cholesterol metabolism & secretion. (A–D) Representative Western blot & densitometric analysis of HMGCR, ABCA1, NPC1, & ApoE in U373 cells treated with vehicle (Ctrl) & LM11A-31 (0.1 µM) for 48 h. n = 4 different experiments. Vinculin served as a housekeeping protein to normalize protein loading. (E) Quantification of ApoE amount (µg/mL) by ELISA assay in culture medium from vehicle- & LM11A-31-treated U373 cells. n = 3 different experiments. (F) Cholesterol quantification (total cholesterol, free cholesterol, & cholesteryl esters) in the culture medium of U373 cells treated with vehicle (Ctrl) & LM11A-31 (0.1 µM) for 48 h. n = 3 different experiments. Data represent means ± SD. Statistical analysis was carried out by using unpaired Student’s t test. *** p < 0.001. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35563230), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-148_rabbit-polyclonal-niemann-pick-c1-antibody-31020241616058.jpg)
![Western Blot: MBP Antibody (12) [NB600-717] - Mouse Brain Tissue lysate probed with Rat anti MBP.](http://images.novusbio.com/fullsize/MBP-Antibody-12-Western-Blot-NB600-717-img0002.jpg "Western Blot: MBP Antibody (12) [NB600-717] - Mouse Brain Tissue lysate probed with Rat anti MBP.")
![Immunocytochemistry/Immunofluorescence: MBP Antibody (12) [NB600-717] - Histological and mRNA analysis of the inflammatory cytokines in the vehicle- or etifoxine-treated mice at onset of clinical symptoms. At day 10 p.i., drug treated animals showed significant differences in MBP staining. Animals treated with etifoxine showed an increase in retention of percentage of MBP coverage (*p = 0.001). Image collected and cropped by CiteAb from the following publication (//embomolmed.embopress.org/cgi/doi/10.1002/emmm.201202124), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/MBP-Antibody-12-Immunocytochemistry-Immunofluorescence-NB600-717-img0005.jpg)
![Immunohistochemistry-Frozen: MBP Antibody (12) [NB600-717] - Staining of MBP in mouse brain corpus callosum. Image from verified customer review.](http://images.novusbio.com/fullsize/MBP-Antibody-12-Immunohistochemistry-Frozen-NB600-717-img0004.jpg)
![Immunohistochemistry-Frozen: MBP Antibody (12) [NB600-717] - Staining of MBP in mouse spinal cord ventral white matter. Image from verified customer review.](http://images.novusbio.com/fullsize/MBP-Antibody-12-Immunohistochemistry-Frozen-NB600-717-img0003.jpg)
![Immunocytochemistry/ Immunofluorescence: MBP Antibody (12) [NB600-717] - Microglia processes appear to preferentially contact TBI-induced proximal axonal swellings. Representative 3D reconstructions of MBP+ myelinated axons (red) or APP+ axonal swellings (green) & Iba-1+ microglia (white) in sham-injured (a) or central fluid percussion injured (b) thalami. c Bar graph depicting the average number of Iba-1+ microglial processes contacting either MBP+ myelinated fibers in the sham animals or APP+ axonal swellings in injured animals. Graph depicts the mean ± standard error of the mean. *p < 0.05. Scale bar: 5 μm Image collected & cropped by CiteAb from the following publication (//jneuroinflammation.biomedcentral.com/articles/10.1186/s12974-015-0405-6), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb600-717_rat-monoclonal-mbp-antibody-12-31020241535646.jpg)
![Western Blot: iNOS Antibody (4E5) [NBP2-22119] - Analysis using iNOS mouse mAb against Jurkat (1), Jurkat (2), A549 (3), HeLa (4), NIH3T3 (5) and MCF-7 (6) cell lysate.](http://images.novusbio.com/fullsize/iNOS-Antibody-4E5-Western-Blot-NBP2-22119-img0007.jpg "Western Blot: iNOS Antibody (4E5) [NBP2-22119] - Analysis using iNOS mouse mAb against Jurkat (1), Jurkat (2), A549 (3), HeLa (4), NIH3T3 (5) and MCF-7 (6) cell lysate.")
![Immunohistochemistry-Paraffin: iNOS Antibody (4E5) [NBP2-22119] - Analysis of paraffin-embedded breast cancer tissues using iNOS mouse mAb with DAB staining.](http://images.novusbio.com/fullsize/iNOS-Antibody-4E5-Immunohistochemistry-Paraffin-NBP2-22119-img0006.jpg)
![Flow Cytometry: iNOS Antibody (4E5) [NBP2-22119] - An intracellular stain was performed on A549 cells with NBP2-22119APC (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated with antibody at 1 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to allophycocyanin (APC).](http://images.novusbio.com/fullsize/iNOS-Antibody-4E5-Flow-Cytometry-NBP2-22119-img0011.jpg)
![Flow Cytometry: iNOS Antibody (4E5) [NBP2-22119] - An intracellular stain was performed on A549 cells with NBP2-22119PE (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated with antibody at 2.5 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to phycoerythrin (PE).](http://images.novusbio.com/fullsize/iNOS-Antibody-4E5-Flow-Cytometry-NBP2-22119-img0010.jpg)
![Western Blot: iNOS Antibody (4E5) [NBP2-22119] - Analysis using iNOS mAb against human iNOS (AA: 997-1058) recombinant protein. (Expected MW is 32.6 kDa)](http://images.novusbio.com/fullsize/iNOS-Antibody-4E5-Western-Blot-NBP2-22119-img0002.jpg)
![Flow Cytometry: iNOS Antibody (4E5) - BSA Free [NBP2-22119] - An intracellular stain was performed on NIH3T3 cells with iNOS Antibody (4E5) NBP2-22119 (blue) and a matched isotype control MAB002 (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 1 ug/mL for 30 minutes at room temperature, followed by Mouse IgG (H+L) Cross-Adsorbed Secondary Antibody, Dylight 550 (84540, Thermo Fisher).](http://images.novusbio.com/fullsize/iNOS-Antibody-4E5-BSA-Free-Flow-Cytometry-NBP2-22119-img0013.jpg)
![Immunohistochemistry-Paraffin: iNOS Antibody (4E5) [NBP2-22119] - Analysis of paraffin-embedded liver cancer tissues using iNOS mouse mAb with DAB staining.](http://images.novusbio.com/fullsize/iNOS-Antibody-4E5-Immunohistochemistry-Paraffin-NBP2-22119-img0009.jpg)
![Flow Cytometry: iNOS Antibody (4E5) - BSA Free [NBP2-22119] - An intracellular stain was performed on Caco-2 cells with iNOS Antibody (4E5) NBP2-22119 (blue) and a matched isotype control MAB002 (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 1 ug/mL for 30 minutes at room temperature, followed by Mouse IgG (H+L) Cross-Adsorbed Secondary Antibody, Dylight 550 (84540, Thermo Fisher).](http://images.novusbio.com/fullsize/iNOS-Antibody-4E5-BSA-Free-Flow-Cytometry-NBP2-22119-img0012.jpg)
![ELISA: iNOS Antibody (4E5) [NBP2-22119] - Red: Control Antigen (100ng); Purple: Antigen (10ng); Green: Antigen (50ng); Blue: Antigen (100ng).](http://images.novusbio.com/fullsize/iNOS-Antibody-4E5-ELISA-NBP2-22119-img0001.jpg)
![Immunocytochemistry/Immunofluorescence: SLC31A1/CTR1 Antibody [NB100-402] - CTR1 antibody was tested in NIH-3T3 cells with DyLight 488 (green). Nuclei and alpha-tubulin were counterstained with DAPI (blue) and DyLight 550 (red).](http://images.novusbio.com/fullsize/SLC31A1-CTR1-Antibody-Immunocytochemistry-Immunofluorescence-NB100-402-img0004.jpg "Immunocytochemistry/Immunofluorescence: SLC31A1/CTR1 Antibody [NB100-402] - CTR1 antibody was tested in NIH-3T3 cells with DyLight 488 (green). Nuclei and alpha-tubulin were counterstained with DAPI (blue) and DyLight 550 (red).")
![Immunohistochemistry: SLC31A1/CTR1 Antibody [NB100-402] - Panel 1: human CTR1 staining of breast cancer tissue. Panel 2: human CTR1-antigen competition in breast cancer tissue.](http://images.novusbio.com/fullsize/SLC31A1-CTR1-Antibody-Immunohistochemistry-NB100-402-img0002.jpg)
![Immunohistochemistry: SLC31A1/CTR1 Antibody [NB100-402] - Left panel: Antibody staining of hCTR1 overexpressing cell line. Right panel: Antibody plus peptide competition staining.](http://images.novusbio.com/fullsize/SLC31A1-CTR1-Antibody-Immunohistochemistry-NB100-402-img0003.jpg)
![Flow (Intracellular): Complement C3 Antibody (11H9) [NB200-540] - An intracellular stain was performed on RAW 246.7 cells with Complement C3 (11H9-3-2) antibody NB200-540 (blue) and a matched isotype control NBP2-31382 (orange). Cells were either treated with 3uM Monensin for 3 hours to block the secretion of Complement C3 (B) or grown in normal media (A). Cells were fixed with 4% PFA and then permeablized with 0.1% saponin. Cells were incubated in an antibody dilution of 2 ug/mL for 30 minutes at room temperature, followed by mouse F(ab)2 IgG (H+L) PE-conjugated secondary antibody (F0102B, R&D Systems).](http://images.novusbio.com/fullsize/Complement-C3-Antibody-11H9-Flow-Intracellular-NB200-540-img0005.jpg "<b>Biological Strategies Validation. </b>Flow (Intracellular): Complement C3 Antibody (11H9) [NB200-540] - An intracellular stain was performed on RAW 246.7 cells with Complement C3 (11H9-3-2) antibody NB200-540 (blue) and a matched isotype control NBP2-31382 (orange). Cells were either treated with 3uM Monensin for 3 hours to block the secretion of Complement C3 (B) or grown in normal media (A). Cells were fixed with 4% PFA and then permeablized with 0.1% saponin. Cells were incubated in an antibody dilution of 2 ug/mL for 30 minutes at room temperature, followed by mouse F(ab)2 IgG (H+L) PE-conjugated secondary antibody (F0102B, R&D Systems).")
![<b>Biological Strategies Validation. </b>Immunocytochemistry/Immunofluorescence: Complement C3 Antibody (11H9) [NB200-540] - C3 protein fragments deposited on kidney cells of MPL-lpr mouse. Staining with antibody 11H9. Glomerular staining pattern. Fixation in 4% paraformaldehyde in PBS pH 7.4. Vibratome sections of 4 um. Pretreated with 3% hydrogen peroxide for 20 min to quench endogenous peroxidases. Microwaved in antigen unmasking solution for 2-5 minutes as antigen retrieval.](http://images.novusbio.com/fullsize/Complement-C3-Antibody-11H9-Immunocytochemistry-Immunofluorescence-NB200-540-img0002.jpg)
![Immunohistochemistry-Paraffin: Complement C3 Antibody (11H9) [NB200-540] - Complement C3 protein in a FFPE tissue section of mouse liver using 1:100 dilution of Complement C3 antibody (clone 11H9) NB200-540. Weak but distinct membrane-cytoplasmic immunopositivity was observed in hepatocytes and few cells developed punctate membrane staining.](http://images.novusbio.com/fullsize/Complement-C3-Antibody-11H9-Immunohistochemistry-Paraffin-NB200-540-img0004.jpg)
![Flow Cytometry: Complement C3 Antibody (11H9) [NB200-540] - Left panel: FMO, Middle panel: No primary antibody control, Right panel: sample. Day 6 murine mammary tumors processed and stained for analysis with flow cytometry. The C3b+ population of CD45+ cells is what the gate in each sample is exhibiting. WB image submitted by a verified customer review.](http://images.novusbio.com/fullsize/Complement-C3-Antibody-11H9-Flow-Cytometry-NB200-540-img0006.jpg)
![Immunohistochemistry-Paraffin: Complement C3 Antibody (11H9) [NB200-540] - Complement C3 protein in a FFPE tissue section of mouse lymph node using 1:100 dilution of Complement C3 antibody (clone 11H9) NB200-540. This representative photomicrograph shows a membrane-cytoplasmic immunopositivity in non-germinal center cells, and few cells developed an intense staining for this target protein.](http://images.novusbio.com/fullsize/Complement-C3-Antibody-11H9-Immunohistochemistry-Paraffin-NB200-540-img0003.jpg)
![Western Blot: eNOS Antibody - BSA Free [NB300-500] - Fractionated, compared to single exposure, radiation more profoundly suppressed TM and eNOS. Representative Western blot analysis and quantification of KLF2 (n = 5) and KLF4 (n = 3) levels in whole-cell lysates from nonirradiated (sham) and irradiated HUVECs 4 h and 24 h after exposure to either five fractions of 2 Gy (5 x 2 Gy) or single exposure to 10 Gy. Fractions delivered at 24-h intervals. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32382091/) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/eNOS Antibody - BSA Free-Western Blot-NB300-500-img0007.jpg "<b>Biological Strategies Validation. </b>Western Blot: eNOS Antibody - BSA Free [NB300-500] - Fractionated, compared to single exposure, radiation more profoundly suppressed TM and eNOS. Representative Western blot analysis and quantification of KLF2 (n = 5) and KLF4 (n = 3) levels in whole-cell lysates from nonirradiated (sham) and irradiated HUVECs 4 h and 24 h after exposure to either five fractions of 2 Gy (5 x 2 Gy) or single exposure to 10 Gy. Fractions delivered at 24-h intervals. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32382091/) licensed under a CC-BY license.")
![<b>Biological Strategies Validation. </b>Immunohistochemistry-Paraffin: eNOS Antibody - BSA Free [NB300-500] - Expression of endothelial markers indicate functional endothelium in TEVG. Whole mount staining of native aorta and TEVG. VE-cadherin is a marker of cellular borders of endothelial cells (green). Endothelial nitric oxide synthase (eNOS) is a marker of a functional endothelium (red). DAPI is a nuclear stain (blue). Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0120328), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/eNOS-Antibody---BSA-Free-Immunohistochemistry-Paraffin-NB300-500-img0006.jpg)
![Immunohistochemistry-Paraffin: eNOS Antibody - BSA Free [NB300-500] - Staining of eNOS in human lung tissue.](http://images.novusbio.com/fullsize/eNOS-Antibody---BSA-Free-Immunohistochemistry-Paraffin-NB300-500-img0003.jpg)
![Immunohistochemistry-Paraffin: eNOS Antibody - BSA Free [NB300-500] - Mouse Carotid Artery stained with eNOS antibody. Image from verified customer review.](http://images.novusbio.com/fullsize/eNOS-Antibody---BSA-Free-Immunohistochemistry-Paraffin-NB300-500-img0004.jpg)
![Immunohistochemistry: eNOS Antibody - BSA Free [NB300-500] - Staining of representative pulmonary artery endothelial cells from rats subjected to CON=Control Group, ALI=Acute lung injury Group, LV=Low tidal volume Group, VLV=Very low tidal volume Group, MV=Large tidal volume Group. Dark brown staining of indicates eNOS-positive cells. Magnification x400.](http://images.novusbio.com/fullsize/eNOS-Antibody---BSA-Free-Immunohistochemistry-NB300-500-img0005.jpg)
![Western Blot: eNOS Antibody - BSA Free [NB300-500] - Mevalonate pathway inhibitors reversed fractionated-radiation–induced suppression of KLF2 & its downstream target molecules. Representative Western blot analysis & quantification of KLF2, TM, & eNOS 4 h after exposure to five fractions of 2 Gy (a) in presence or absence of atorvastatin (1 μM) or GT3 (5 μM) & (b) in presence or absence of GGTi (10 μM) (n = 3). beta -actin served as a loading control. (n, number of independent experiments performed; a, significant statistical difference between nonirradiated & irradiated groups; b, significant statistical difference between fractionated irradiation & single exposure; *, p < 0.05; **, p < 0.01; ***, p < 0.001). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32382091), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-500_rabbit-polyclonal-enos-antibody-31020241534534.jpg)
![Western Blot: eNOS Antibody - BSA Free [NB300-500] - Upregulation of HMG-CoA reductase in shPLD2 cells decreases eNOS expression. (A) Representative western blot of HMG-CoA reductase in Scramble & shPLD2 cells. The regions of the Western blots containing the HMG-CoA reductase & actin immunoreactive bands were scanned & the relative abundance of the individual samples quantified using an Odyssey CLx imaging system (B) Quantification of western blots with HMG-CoA reductase normalized to actin (n = 4 experiments). (C) N-SIM microscopy of HMG-CoA reductase; Bar, 7.5 μM. (D) RT-PCR of HMG-CoA reductase in Scramble & shPLD2 cells (n = 3). (E) Western blot of eNOS after treatment with NFOT & Simvastatin. Representative image of 3 experiments. The regions of the Western blots (Suppl. Figure 2) containing the eNOS & actin immunoreactive bands were scanned & the relative abundance of the individual samples quantified using an Odyssey CLx imaging system. (F) Quantification of western blots with eNOS levels normalized to actin (n = 3). Comparisons without bars made to untreated Scramble values. (G) eNOS activity after treatment with Simvastatin (n = 7). Mean ± SEM; *p < 0.05; **p < 0.01; ***p ≤ 0.001; One-way ANOVA with Bonferroni’s Multiple Comparison Test. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28831159), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-500_rabbit-polyclonal-enos-antibody-310202416212339.jpg)
![Western Blot: eNOS Antibody - BSA Free [NB300-500] - The human PLD2 polymorphism R172C does not alter eNOS signaling but does decrease caveolin-1 protein levels. Overexpression of HA-tagged hPLD2 (A) & HA-R172C-PLD2 (B) in HeLa cells, visualized using anti-HA immunofluorescent staining (green). Arrowhead, PLD2 localization in filopodia; chevron, in peripheral actin ruffles; *, in dorsal actin ruffles; arrow, in subcortical actin network. Bar, 7.5 μM. Representative image of multiple experiments. (C) Representative western blot of eNOS after transfection of HA-hPLD2 or HA-R172C-PLD2 into shPLD2 cells. The regions of the Western blots containing the eNOS & actin immunoreactive bands were scanned & the relative abundance of the individual samples quantified using an Odyssey CLx imaging system. (D) Quantification of western blotting with eNOS levels normalized to actin (n = 3). (E) eNOS activity as measured by nitrate formation (n = 7). Lane 1 vs 2, P = 0.0021; lane 2 vs 3, P = 0.00035; lane 2 vs 4, P = 0.00012. (F–I) N-SIM microscopy of plasma membrane eNOS & caveolin-1. Bar, 7.5 μM. Representative image of multiple Scramble or shPLD2 cells imaged. Cells in H & I were selected for imaging based on expression of HA-hPLD2 or HA-R172C-PLD2 as visualized by anti-HA immunofluorescence in a separate channel (not shown). Mean ± SEM; *p < 0.05; **p < 0.01; ***p ≤ 0.001; One-way ANOVA with Bonferroni’s Multiple Comparison Test. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28831159), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb300-500_rabbit-polyclonal-enos-antibody-310202416212351.jpg)
![Western Blot: alpha-Internexin Antibody (2E3) [NB300-140] - Analysis of different tissue lysates using alpha-Internexin, dilution 1:10000 (Red): [1] protein standard, [2] rat brain, [3] rat spinal cord, [4] mouse brain, [5] mouse spinal cord, and [6] cow spinal cord lysate. The antibody reveals the alpha-Internexin protein with an apparent molecular weight of 64-66kDa, with some variability across species.](http://images.novusbio.com/fullsize/alpha-Internexin-Antibody-2E3-Western-Blot-NB300-140-img0005.jpg "Western Blot: alpha-Internexin Antibody (2E3) [NB300-140] - Analysis of different tissue lysates using alpha-Internexin, dilution 1:10000 (Red): [1] protein standard, [2] rat brain, [3] rat spinal cord, [4] mouse brain, [5] mouse spinal cord, and [6] cow spinal cord lysate. The antibody reveals the alpha-Internexin protein with an apparent molecular weight of 64-66kDa, with some variability across species.")
![Immunocytochemistry/Immunofluorescence: alpha-Internexin Antibody (2E3) [NB300-140] - Hippocampal neurons in tissue culture with neurofilament alpha internexin (red), using NB300-140 and GFAP (green), using NB300-141.](http://images.novusbio.com/fullsize/alpha-Internexin-Antibody-2E3-Immunocytochemistry-Immunofluorescence-NB300-140-img0003.jpg)
![Immunohistochemistry: alpha-Internexin Antibody (2E3) [NB300-140] - Section of rat facial nucleus 7 days following axotomy. These neurons are capable of regenerating their axons and also, concomitant with regeneration, strongly upregulate alpha-Internexin in their perikarya. Other central neurons which are not able to regenerate their axons do not upregulate this protein after axotomy and untreated facial neurons normally show only very low levels of alpha-Internexin. Both findings suggest that alpha-Internexin has a role in axonal regeneration.](http://images.novusbio.com/fullsize/alpha-Internexin-Antibody-2E3-Immunohistochemistry-NB300-140-img0006.jpg)
![Simple Western: alpha-Internexin Antibody (2E3) [NB300-140] - Simple Western lane view shows a specific band for alpha Internexin in 0.5 mg/ml of SH-SY5Y lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system.](http://images.novusbio.com/fullsize/alpha-Internexin-Antibody-2E3-Simple-Western-NB300-140-img0004.jpg)
![Western Blot: Niemann-Pick type C1 Like-1 Antibody [NB400-128] - Detection of NPC3 in rat small intestine membrane preparations (20 ug). (1) 2 ug/ml and (2) 4 ug/ml. ECL: 30 minute exposure.](http://images.novusbio.com/fullsize/Niemann-Pick-type-C1-Like-1-Antibody-Western-Blot-NB400-128-img0004.jpg "Western Blot: Niemann-Pick type C1 Like-1 Antibody [NB400-128] - Detection of NPC3 in rat small intestine membrane preparations (20 ug). (1) 2 ug/ml and (2) 4 ug/ml. ECL: 30 minute exposure.")
![Immunohistochemistry-Paraffin: Niemann-Pick type C1 Like-1 Antibody [NB400-128] - Staining of human small intestine, enterocytes.](http://images.novusbio.com/fullsize/Niemann-Pick-type-C1-Like-1-Antibody-Immunohistochemistry-Paraffin-NB400-128-img0005.jpg)
![Western Blot: Niemann-Pick type C1 Like-1 Antibody [NB400-128] - Decrease in the biliary cholesterol secretion in L1-Tg mice. Immunoblot detection of hepatic NPC1L1 protein in L1-Tg mice using an anti-NPC1L1 (Niemann-Pick type C1 Like-1) antibody. WT, wild-type. Image collected and cropped by CiteAb from the following publication (//lipidworld.biomedcentral.com/articles/10.1186/s12944-019-1179-0), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/Niemann-Pick-type-C1-Like-1-Antibody-Western-Blot-NB400-128-img0006.jpg)
![Western Blot: Niemann-Pick type C1 Like-1 Antibody - BSA Free [NB400-128] - Hepatic NPC1L1‐mediated steatosis in the liver of L1‐Tg mice. A, Hepatic expression of the human NPC1L1 protein in L1‐Tg mice demonstrated by immunoblotting using an anti‐NPC1L1 antibody. alpha ‐Tubulin, a loading control. B, Decrease of biliary cholesterol levels in L1‐Tg mice. Data are expressed as the mean ± SEM n = 6 (WT) & 7 (L1‐Tg). C, Photographic images of the livers of WT & L1‐Tg mice fed a control fat diet (CFD) or a high‐fat diet (HFD) for 2 weeks. The coin diameter was 1 cm. D, Hematoxylin & eosin (H&E) & Oil Red O staining of the livers of WT & L1‐Tg mice fed a HFD for 2 weeks. E & F, Hepatic cholesterol levels (E, left), hepatic triglyceride (TG) levels (E, right), body weight (BW) (F, left), & the ratios of liver weight to BW (L/B ratio) (F, right) in each group of mice fed a CFD or HFD for 2 weeks. Data are expressed as the mean ± SEM n = 11 (WT‐CFD) & 7 (the other groups). Statistical analyses for significant differences were performed using Bartlett's test, followed by a parametric Tukey–Kramer multiple‐comparison test (E, right; F) or a non‐parametric Steel–Dwass test (E, left) (##P < 0.01 vs CFD controls; **P < 0.01 vs. the other groups; *P < 0.05 among two groups; NS, not significantly different among groups) as well as a two‐sided t test (††P < 0.01). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32123832), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-128_rabbit-polyclonal-niemann-pick-type-c1-like-1-antibody-310202416165636.jpg)