| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB400-105SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB400-104SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB400-132SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB400-144SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB400-101SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB400-113SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB400-129SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NBP1-78159SS | |||
| Azide and BSA Free | NBP2-80833 | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB400-128SS | |||
| Formulation | Catalog # | Availability | Price | |
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| BSA Free | NBP1-06709SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB400-145SS | |||
| Formulation | Catalog # | Availability | Price | |
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| BSA Free | NB400-127SS | |||
![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)
![Simple Western: SR-BI Antibody [NB400-104] - Image shows a specific band for SR-BI in 0.5 mg/mL of HeLa lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system.](http://images.novusbio.com/fullsize/SR-BI-Antibody-Simple-Western-NB400-104-img0014.jpg "Simple Western: SR-BI Antibody [NB400-104] - Image shows a specific band for SR-BI in 0.5 mg/mL of HeLa lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system.")
![Western Blot: SR-BI Antibody [NB400-104] - SR-BI antibody was tested in human adrenal cell lysate.](http://images.novusbio.com/fullsize/SR-BI-Antibody-Western-Blot-NB400-104-img0003.jpg)
![Immunocytochemistry/Immunofluorescence: SR-BI Antibody [NB400-104] - SR-BI antibody was tested in human fibroblast samples fixed in 4% PFA and permeabilized in PBS (0.2% Tween). Primary incubation overnight at 4C using a 1:100 dilution in PBS (0.1% Tween) with 1% BSA. Secondary antibody is anti-rabbit conjugate to Alexa Fluor 488. SR-BI is shown in green and nucleus in blue (Hoescht 33342 stain).](http://images.novusbio.com/fullsize/SR-BI-Antibody-Immunocytochemistry-Immunofluorescence-NB400-104-img0030.jpg)
![Flow Cytometry: SR-BI Antibody [NB400-104] - An intracellular stain was performed on HeLa cells with SR-BI antibody NB400-104AF488 (blue) and a matched isotype control NBP2-24893AF488 (orange). Cells were fixed with 4% PFA and then permeablized with 0.1% saponin. Cells were incubated in an antibody dilution of 5 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to Alexa Fluor 488.](http://images.novusbio.com/fullsize/SR-BI-Antibody-Flow-Cytometry-NB400-104-img0026.jpg)
![Western Blot: SR-BI Antibody [NB400-104] - Detection of SR-BI in rat H4IIE total cell lysates and plasma membrane proteins. Photo courtesy of product review by verified customer.](http://images.novusbio.com/fullsize/SR-BI-Antibody-Western-Blot-NB400-104-img0013.jpg)
![Immunohistochemistry: SR-BI Antibody [NB400-104] - Immunolocalization of SR-BI in adult mink testis using NB400-104. SR-BI labeling is visible at the surface and along the outline of the large vacuole. Photo courtesy of R.M. Pelletier, University of Montreal.](http://images.novusbio.com/fullsize/SR-BI-Antibody-Immunohistochemistry-NB400-104-img0011.jpg)
![Immunohistochemistry-Paraffin: SR-BI Antibody [NB400-104] - FFPE tissue section of mouse liver using SR-BI antibody (Lot 8310) at 1:300 dilution with HRP-DAB detection and hematoxylin counterstaining. The antibody generated a specific membrane signal of SR-BI protein in the murine hepatocytes.](http://images.novusbio.com/fullsize/SR-BI-Antibody-Immunohistochemistry-Paraffin-NB400-104-img0022.jpg)
![<b>Genetic Strategies Validation. </b>Western Blot: SR-BI Antibody [NB400-104] - HCV replication was increased by CD36. Silence of CD36 decreased HCV infection and replication (n = 3). Huh7.5 cells were transfected with 0.2 u g CD36-HA plasmid or with 150 pmol siRNA for CD36 (B) for 48 hrs, and then were washed and infected with HCV (150 IU/cell) for 2 hrs, followed by washing and continuously incubating. Intracellular HCV RNA and proteins were detected in 96 hrs, and the cytotoxicity of siRNAs was measured in 96-wells plate with a MTT assay in B. Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/srep21808) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/SR-BI-Antibody-Western-Blot-NB400-104-img0034.jpg)
![Immunohistochemistry-Paraffin: SR-BI Antibody [NB400-104] - Staining of human adrenal cortex.](http://images.novusbio.com/fullsize/SR-BI-Antibody-Immunohistochemistry-Paraffin-NB400-104-img0012.jpg)
![Immunocytochemistry/Immunofluorescence: SR-BI Antibody [NB400-104] - HeLa cells were fixed and permeabilized for 10 minutes using -20C MeOH. The cells were incubated with anti-SR-BI at 2 ug/ml overnight at 4C and detected with an anti-rabbit Dylight 488 (Green) at a 1:500 dilution. Alpha tubulin (DM1A) NB100-690 was used as a co-stain at a 1:1000 dilution and detected with an anti-mouse Dylight 550 (Red) at a 1:500 dilution. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 40X objective.](http://images.novusbio.com/fullsize/SR-BI-Antibody-Immunocytochemistry-Immunofluorescence-NB400-104-img0029.jpg)
![Immunohistochemistry-Paraffin: SR-BI Antibody [NB400-104] - FFPE tissue section of mouse liver using SR-BI antibody (Lot R-4) at 1:300 dilution with HRP-DAB detection and hematoxylin counterstaining. The antibody generated mainly a membranous signal of SR-BI protein in the murine hepatocytes.](http://images.novusbio.com/fullsize/SR-BI-Antibody-Immunohistochemistry-Paraffin-NB400-104-img0023.jpg)
![Flow Cytometry: SR-BI Antibody [NB400-104] - Analysis of Huh7 and HepG2 cells using SR-B1 antibody NB400-104. Courtesy of Bruno Sainz, Jr., PhD, University of Illinois at Chicago.](http://images.novusbio.com/fullsize/SR-BI-Antibody-Flow-Cytometry-NB400-104-img0004.jpg)
![Western Blot: SR-BI Antibody - BSA Free [NB400-104] - Effects of 13-HODE & LA in the presence & absence of PPAR alpha & PPAR gamma selective antagonists on molecular markers of cholesterol homeostasis in RAW264.7 macrophages. RAW264.7 cells were pre-treated without or with the PPAR alpha selective antagonist GW6471 or the PPAR gamma selective antagonist GW9662 & subsequently treated without (vehicle control) or with 2.5 μmol/L 13-HODE or 100 μmol/L LA for 24 h. Afterwards, cells were lysed & subsequently processed for western blotting as described in the materials & methods section. A, Representative immunoblots specific for ABCA1, ABCG1, SR-BI, LXR alpha , & beta -actin which was used for normalization are shown. B, Bars represent data from densitometric analysis & are means ± SD from three independent experiments (n = 3). Data are expressed as percentage of protein concentration of vehicle control cells. Results from statistical analysis are indicated: Significant effects are denoted with superscript letters. Bars marked without a common superscript letter significantly differ (P 2000) (g, h, i, respectively). Bar graph shows the mean percentage of positively stained cells. Error bars depict standard deviations. ****p 0.3) by one-way ANOVA. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29523748), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-104_rabbit-polyclonal-sr-bi-antibody-31020241618928.jpg)
![Western Blot: SR-BI Antibody - BSA Free [NB400-104] - Differentiation & characteristics of iHLCs. (a) Cell morphology & culture conditions at different stages of differentiation from iPSCs into iHLCs. Bright-field images were taken at the indicated time points (scale bar 100 µm). (b) Sequential expression & repression of transcription factors marking successful differentiation. Cells were immunostained with antibodies against Oct 3/4 (pluripotency marker), the endodermal transcription factor GATA-4, & the hepatic marker HNF4 alpha at day 0, 5, & 10 of differentiation (scale bars 20 µm). Shown are representative fluorescence & DIC images. (c) mRNA expression levels of different hepatocyte-specific factors in iHLCs, Huh7.5 cells, & primary human hepatocytes (PHHs) were analysed via qRT-PCR. Expression levels are displayed as fold over iPSCs normalised to GAPDH & 18S rRNA (mean ± SEM, n = 3–4, *p 0.9) by one-way ANOVA. §P < 0.02 by unpaired Student's t-test, relative to 0 h time point. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29523748), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-104_rabbit-polyclonal-sr-bi-antibody-31020241616010.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)
![Immunohistochemistry: CD36 Antibody [NB400-144] - Timp4-deficiency results in defective lipid digestion and absorption. (B) Immunostaining for CD36 in small intestine (proximal region) of chow-fed and HFD-fed WT and Timp4-/- mice. Western blot (C) and mRNA (D) for CD36 in enterocyte fraction of chow-fed and HFD-fed WT and Timp4-/- mice (collected from the proximal small intestine). Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/s41598-017-05951-4), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/CD36-SR-B3-Antibody-Immunohistochemistry-NB400-144-img0016.jpg "<b>Biological Strategies Validation and Orthogonal Strategies Validation.</b>Immunohistochemistry: CD36 Antibody [NB400-144] - Timp4-deficiency results in defective lipid digestion and absorption. (B) Immunostaining for CD36 in small intestine (proximal region) of chow-fed and HFD-fed WT and Timp4-/- mice. Western blot (C) and mRNA (D) for CD36 in enterocyte fraction of chow-fed and HFD-fed WT and Timp4-/- mice (collected from the proximal small intestine). Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/s41598-017-05951-4), licensed under a CC-BY license.")
![<b>Biological Strategies Validation and Orthogonal Strategies Validation.</b>Western Blot: CD36 Antibody [NB400-144] - Total protein from Human Skin and Adipose tissue, Mouse Adipose and Rat Adipose tissue was separated on a 12% gel by SDS-PAGE, transferred to PVDF membrane and blocked in 5% non-fat milk in TBST. The membrane was probed with 2.0 ug/ml anti-CD36 in 5% non-fat milk in TBST and detected with an anti-rabbit HRP secondary antibody using chemiluminescence.](http://images.novusbio.com/fullsize/CD36-SR-B3-Antibody-Western-Blot-NB400-144-img0009.jpg)
![Immunohistochemistry-Paraffin: CD36 Antibody [NB400-144] - Staining of CD36 in human adipocytes.](http://images.novusbio.com/fullsize/CD36-SR-B3-Antibody-Immunohistochemistry-Paraffin-NB400-144-img0005.jpg)
![Western Blot: CD36 Antibody [NB400-144] - Mouse primary muscle cell lysate. Western blot image submitted by a verified customer review.](http://images.novusbio.com/fullsize/CD36-SR-B3-Antibody-Western-Blot-NB400-144-img0011.jpg)
![Immunocytochemistry/Immunofluorescence: CD36 Antibody [NB400-144] - Bone marrrow derived mouse macrophages stained with CD36 antibody. ICC/IF image submitted by a verified customer review.](http://images.novusbio.com/fullsize/CD36-SR-B3-Antibody-Immunocytochemistry-Immunofluorescence-NB400-144-img0017.jpg)
![Western Blot: CD36 Antibody [NB400-144] - Detection of CD36 in human adipocyte extract (30 ug). Lane 1: 0.5 ug/ml NB 400-144; lane 2: 2 ug/ml NB 400-144. ECL: 3 second exposure.](http://images.novusbio.com/fullsize/CD36-SR-B3-Antibody-Western-Blot-NB400-144-img0004.jpg)
![Western Blot: Rabbit Polyclonal CD36 Antibody [NB400-144] - The western blot was conducted on avian (passerine) skeletal muscle tissue homogenate. 6ug of total protein was loaded and GAPDH was probed to ensure total protein loads were similar across samples. Rabbit polyclonal CD36 antibody (NB400-144) was used at 1:5000 dilution (diluted in 5% milk). CD36 and GAPDH were probed sequentially - not multiplexed. CD36 produced a band above 40kDa and GAPDH at 36kDa. Image from a verified customer review.](http://images.novusbio.com/fullsize/antibody/nb400-144_rabbit-polyclonal-cd36-antibody-western-blot-13202413439..png)
![Immunocytochemistry/ Immunofluorescence: CD36 Antibody - BSA Free [NB400-144] - Timp4-deficiency results in defective lipid digestion & absorption. Fecal triglyceride (TG) content (Ai) in chow- or HFD-fed WT & Timp4−/− mice. Fecal lipid analysis by thin layer chromatography in chow-fed (Aii) & HFD-fed (iii) WT & Timp4−/− mice. (B) Immunostaining for CD36 in small intestine (proximal region) of chow-fed & HFD-fed WT & Timp4−/− mice. Western blot (C) & mRNA (D) levels for CD36 in enterocyte fraction of chow-fed & HFD-fed WT & Timp4−/− mice (collected from the proximal small intestine). (E) Triglyceride levels in enterocytes collected from the proximal small intestine. Averaged data are presented as mean ± S.E.M & analyzed by ANOVA. * indicates significance (p < 0.05). Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/s41598-017-05951-4), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-144_rabbit-polyclonal-cd36-antibody-310202415293346.jpg)
![Western Blot: CD36 Antibody - BSA Free [NB400-144] - Timp4-deficiency results in defective lipid digestion & absorption. Fecal triglyceride (TG) content (Ai) in chow- or HFD-fed WT & Timp4−/− mice. Fecal lipid analysis by thin layer chromatography in chow-fed (Aii) & HFD-fed (iii) WT & Timp4−/− mice. (B) Immunostaining for CD36 in small intestine (proximal region) of chow-fed & HFD-fed WT & Timp4−/− mice. Western blot (C) & mRNA (D) levels for CD36 in enterocyte fraction of chow-fed & HFD-fed WT & Timp4−/− mice (collected from the proximal small intestine). (E) Triglyceride levels in enterocytes collected from the proximal small intestine. Averaged data are presented as mean ± S.E.M & analyzed by ANOVA. * indicates significance (p < 0.05). Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/s41598-017-05951-4), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-144_rabbit-polyclonal-cd36-antibody-31020241535667.jpg)
![Western Blot: CD36 Antibody - BSA Free [NB400-144] - MiR-29a inhibits the expression of fatty acid translocase CD36 by targeting 3’ untranslated region (UTR). (A) qPCR analysis of Cd36 in live tissue. (B) Representative immunoblotting bands & densitometric results of CD36 in liver tissue. (C) qPCR analysis of cd36 expression of HepG2 cells in vitro after 48h transfection of scramble sequence or miR-29a-mimic. Data obtained from six independent experiments. (D) Upper panel, sequence information, & mutual pairing status of CD36-3’UTR, mmu-miR29a, & CD36-3’UTR Mut. Note that red characters represent mismatching sites. HepG2 was first transfected with CD36-3’UTR or CD36-3’UTR mutant luciferase reporter construct then treated with control medium (ctrl), miRNA-scramble, or miR-29a mimic, & finally lysed to detect the luciferase signal. Data are expressed as mean ± SE. * p < 0.05, ** p < 0.01, & *** p < 0.001 between the indicated groups. WT, wild type mice. HFD, high-fat diet. miR-29a, mice harboring overexpression of miR-29a. mmu-miR29a, mouse-origin miR-29a. ctrl, control. Mut, mutant. UTR, untranslated region. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31652636), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-144_rabbit-polyclonal-cd36-antibody-310202416173544.jpg)
![Immunohistochemistry: CD36 Antibody - BSA Free [NB400-144] - Integrin beta 3 modulates SMC transdifferentiation. a–c Mice were fed a HFD for 6 or 16 weeks as indicated, & then transverse aortic root sections were stained. In a, b sections from ApoE(−/−), SMMHC-CreERT2, ROSA26R(mTmG/+) mice were stained for SMA, GFP (fate marker), nuclei (DAPI), & either integrin beta 3 (a) or CD36 (b). Dashed yellow lines separate cap from core (a, b) & core from media (b). n = 5. In c sections from ApoE(−/−) mice that were also wild type or null for Itgb3 were stained for SMMHC, CD68, & nuclei (DAPI). n = 3. Boxed regions (a, c) are shown as close-ups on right; in c CD68+SMMHC+ cells in the media (arrowheads) & plaque (arrows) of the Itgb3 null atherosclerotic aorta are indicated. Med, tunica media; Lu, lumen; Pl, plaque. Scale bars, 25 μm. d–h Aortic SMCs were isolated from ApoE(−/−) mice & then subjected to siRNA-mediated knockdown with si-Itgb3 vs. scrambled (Scr; d–f) or with si-Itgb3, si-Tlr4 vs. si-Itgb3 (g, h). Levels of indicated transcripts from qRT-PCR are relative to Gapdh & normalized to either Scr in d, f or to si-Itgb3 in g, h. For d, g, n = 4–5 in duplicate. In e silenced SMCs were cultured with DiI-conjugated ox-LDL for 10 h & stained with DAPI; n = 5. In f, h silenced SMCs were exposed to soluble cholesterol:methyl-beta -cyclodextrin complexes for 3 days, & then mRNA levels were assessed; n = 4–7 in duplicate. *, **, ***, ^, **** vs. control (Scr in d, f & si-Itgb3 in g, h), p < 0.05, p < 0.01, p < 0.005, p < 0.001, & p < 0.0005, respectively. NS, not significant. Student’s t-test was used, & error bars represent standard deviations. i Schematic of the effect of beta 3 reduction via TLR4 & CD36 in SMCs on transdifferentiation Image collected & cropped by CiteAb from the following publication (//www.nature.com/articles/s41467-018-04447-7), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-144_rabbit-polyclonal-cd36-antibody-310202416161810.jpg)
![Western Blot: CD36 Antibody - BSA Free [NB400-144] - The increase in CD36 levels caused by lipids in Sirt3-deficient hepatocytes is mediated by Nrf2. VLDLR mRNA abundance (a) & protein levels of VLDLR & NQO1, an Nrf-2-target gene, (b) were assessed in Huh-7 cells incubated with fatty acid free-BSA or BSA-palmitate (0.3 mM) & exposed to either vehicle or the Sirt3 inhibitor AAPBO (100 μM) for 16 h. a, p < 0.05 vs. CT. b, p < 0.05 vs. CT cells incubated with palmitate. c, p < 0.05 vs. CT cells treated with AAPBO. c, fatty acid uptake in Huh-7 cells incubated with fatty acid free-BSA or BSA-palmitate (0.3 mM) & exposed to either vehicle or the Sirt3 inhibitor AAPBO (100 μM) for 16 h was measured by the uptake of BODIPY-C16. a, p < 0.05 vs. CT. b, p < 0.05 vs. CT cells incubated with palmitate. c, p < 0.05 vs. CT cells treated with AAPBO. mRNA abundance (d) & protein levels of VLDLR (e) in Huh-7 cells transfected with control (CT) or SIRT3 siRNA & incubated in the presence or absence 0.3 mM palmitate (Pal) for 24 h. Protein levels of CD36 (f), NQO1 (g) & PPAR gamma (h) in Huh-7 cells transfected with control (CT) or SIRT3 siRNA & incubated in the presence or absence 0.3 mM palmitate (Pal) or the Nrf2 inhibitor ML385 (10 μM) for 24 h. a, p < 0.05 vs. CT siRNA cells. b, p < 0.05 vs. CT siRNA cells incubated with palmitate. c, p < 0.05 vs. SIRT3 siRNA cells. d, p < 0.05 vs. CT siRNA cells incubated with palmitate & ML385 Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32912335), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-144_rabbit-polyclonal-cd36-antibody-31020241616372.jpg)
![Western Blot: CD36 Antibody - BSA Free [NB400-144] - The increase in CD36 levels caused by lipids in Sirt3-deficient hepatocytes is mediated by Nrf2. VLDLR mRNA abundance (a) & protein levels of VLDLR & NQO1, an Nrf-2-target gene, (b) were assessed in Huh-7 cells incubated with fatty acid free-BSA or BSA-palmitate (0.3 mM) & exposed to either vehicle or the Sirt3 inhibitor AAPBO (100 μM) for 16 h. a, p < 0.05 vs. CT. b, p < 0.05 vs. CT cells incubated with palmitate. c, p < 0.05 vs. CT cells treated with AAPBO. c, fatty acid uptake in Huh-7 cells incubated with fatty acid free-BSA or BSA-palmitate (0.3 mM) & exposed to either vehicle or the Sirt3 inhibitor AAPBO (100 μM) for 16 h was measured by the uptake of BODIPY-C16. a, p < 0.05 vs. CT. b, p < 0.05 vs. CT cells incubated with palmitate. c, p < 0.05 vs. CT cells treated with AAPBO. mRNA abundance (d) & protein levels of VLDLR (e) in Huh-7 cells transfected with control (CT) or SIRT3 siRNA & incubated in the presence or absence 0.3 mM palmitate (Pal) for 24 h. Protein levels of CD36 (f), NQO1 (g) & PPAR gamma (h) in Huh-7 cells transfected with control (CT) or SIRT3 siRNA & incubated in the presence or absence 0.3 mM palmitate (Pal) or the Nrf2 inhibitor ML385 (10 μM) for 24 h. a, p < 0.05 vs. CT siRNA cells. b, p < 0.05 vs. CT siRNA cells incubated with palmitate. c, p < 0.05 vs. SIRT3 siRNA cells. d, p < 0.05 vs. CT siRNA cells incubated with palmitate & ML385 Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32912335), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-144_rabbit-polyclonal-cd36-antibody-31020241617350.jpg)
![Immunocytochemistry/ Immunofluorescence: SR-BI Antibody [NB400-101] - Immunofluorescent analysis of SR-BI localization in aorta of Tie2-Scarb1 x Scarb1-KO and Scarb1-KO mice. Mouse aorta sections were stained for SR-BI (a and d, red). In several EC stained for SR-B1 red color was present on both apical and basolateral sides. There is no red signal in aorta from Scarb1-KO mice. Image collected and cropped by CiteAb from the following publication (//www.hindawi.com/journals/bmri/2015/607120/) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/SR-BI-Antibody-Knockout-Validated-NB400-101-img0018.jpg "<b>Genetic Strategies Validation. </b>Immunocytochemistry/ Immunofluorescence: SR-BI Antibody [NB400-101] - Immunofluorescent analysis of SR-BI localization in aorta of Tie2-Scarb1 x Scarb1-KO and Scarb1-KO mice. Mouse aorta sections were stained for SR-BI (a and d, red). In several EC stained for SR-B1 red color was present on both apical and basolateral sides. There is no red signal in aorta from Scarb1-KO mice. Image collected and cropped by CiteAb from the following publication (//www.hindawi.com/journals/bmri/2015/607120/) licensed under a CC-BY license.")
![<b>Genetic Strategies Validation. </b>Simple Western: SR-BI Antibody [NB400-101] - Lane view shows a specific band for SR-BI in 0.5 mg/ml of HeLa lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system.](http://images.novusbio.com/fullsize/SR-BI-Antibody-Simple-Western-NB400-101-img0007.jpg)
![<b>Genetic Strategies Validation. </b>Immunohistochemistry: SR-BI Antibody [NB400-101] - Immunofluorescent analysis of SR-BI localization in liver of normal, Tie2-Scarb1 x Scarb1-KO, and Scarb1-KO mice. Liver sections from normal (b) and Tie2-Scarb1 x Scarb1-KO mice (c) were stained for SR-BI (red) and cytokeratin 8-18 (green).Merge image for normal mouse (b) demonstrates strong presence of SR-BI in hepatocytes (b, yellow signal) and absence of detectable level of SR-BI protein in liver of Tie2-Scarb1 x Scarb1-KO mice (c). In Scarb1-KO mice there was no detectable level of SR-BI protein (d, staining for SR-BI). Blue = DAPI. Image collected and cropped by CiteAb from the following publication (//www.hindawi.com/journals/bmri/2015/607120/) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/SR-BI-Antibody-Knockout-Validated-NB400-101-img0011.jpg)
![Western Blot: SR-BI Antibody [NB400-101] - Detection of SR-BI in mouse liver lysate (20 ug) using NB 400-101. ECL detection 5 seconds.](http://images.novusbio.com/fullsize/SR-BI-Antibody-Western-Blot-NB400-101-img0005.jpg)
![Flow (Intracellular): SR-BI Antibody [NB400-101] - An intracellular stain was performed on HeLa cells with NB400-101AF647 (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeablized with 0.1% saponin. Cells were incubated in an antibody dilution of 2.5 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to Alexa Fluor 647.](http://images.novusbio.com/fullsize/SR-BI-Antibody-Flow-Intracellular-NB400-101-img0010.jpg)
![<b>Genetic Strategies Validation. </b>Western Blot: SR-BI Antibody [NB400-101] - Western blot and Coomassie stain of membrane fractions isolated from livers of normal C57Bl/6N (lane 1), Scarb1-KO (lane 2), and LIV11-SCARB1 x Scarb1-KO (lane 3) mice. 20 ug of membrane protein was loaded into each lane. (a)Western blot (anti-SR-BI antibody). (b) Coomassie stain (loading control for Western blot) encompassing the same MW region as SR-BI. Aliquots from the same tube were loaded for the Western blot and for the Coomassie-stained gel, which shows comparable loading between the three samples. Image collected and cropped by CiteAb from the following publication (//www.hindawi.com/journals/bmri/2015/607120/) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/SR-BI-Antibody-Knockout-Validated-NB400-101-img0014.jpg)
![Immunocytochemistry/Immunofluorescence: SR-BI Antibody [NB400-101] - HeLa cells were fixed and permeabilized for 10 minutes using -20C MeOH. The cells were incubated with anti-SR-BI at 2 ug/ml overnight at 4C and detected with an anti-rabbit DyLight 488 (Green) at a 1:500 dilution. Alpha tubulin (DM1A) NB100-690 was used as a co-stain at a 1:1000 dilution and detected with an anti-mouse DyLight 550 (Red) at a 1:500 dilution. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 40X objective.](http://images.novusbio.com/fullsize/SR-BI-Antibody-Immunocytochemistry-Immunofluorescence-NB400-101-img0009.jpg)
![Immunohistochemistry-Paraffin: SR-BI Antibody [NB400-101] - SR-B1 was detected in immersion fixed paraffin-embedded sections of human liver using rabbit anti-human antibody (Catalog # NB400-101) at 1:300 dilution overnight at 4C. Tissue was stained using the VisuCyte anti-rabbit HRP polymer detection reagent (Catalog # VC003) with DAB chromogen (brown) and counterstained with hematoxylin (blue). Images may not be copied, printed or otherwise disseminated without express written permission of Novus Biologicals a Bio-techne brand.](http://images.novusbio.com/fullsize/SR-BI-Antibody-Immunohistochemistry-Paraffin-NB400-101-img0008.jpg)
![Western Blot: SR-BI Antibody [NB400-101] - Western blot analysis of ABCA1 and SR-B1 proteins from WT and Osbpl8KO mouse liver. The blots were probed with anti-beta-actin as a loading control. Densitometric quantification of the Western blot data is shown on the right. The results were normalized against beta-actin. The data represents mean +/- s.e.m. (n=4). Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0058856), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/SR-BI-Antibody-Western-Blot-NB400-101-img0019.jpg)
![Immunocytochemistry/ Immunofluorescence: SR-BI Antibody - BSA Free [NB400-101] - SR-BI distribution in polarized EC SVEC4-10 cells. SR-BI localization is presented in (a) as x-y image & orthogonal (x-z & y-z) views. (b) & (c) represent rendering of SR-BI staining (red) throughout the cells. Nuclei: blue. In (b) & (c) basolateral surface is on the top & the bottom, respectively. These results demonstrate the presence of SR-BI on both the apical & the basolateral sides of EC. The size of scale bar on (a) is 5 μm & on (b) & (c) 10 μm. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26504816), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-101_rabbit-polyclonal-sr-bi-antibody-31020241534391.jpg)
![Immunocytochemistry/ Immunofluorescence: SR-BI Antibody - BSA Free [NB400-101] - Immunofluorescent analysis of SR-BI localization in aorta of Tie2-Scarb1 × Scarb1-KO & Scarb1-KO mice. Mouse aorta sections were stained for SR-BI (a & d, red) & CD31 (b & e, green). Colocalization of SR-BI & CD31 was presented on (c) & (f). Blue = DAPI. (a, b, & c) Immunohistological analysis of SR-BI localization in aortic sections of Tie2-Scarb1 × Scarb1-KO mice. Colocalization of SR-BI & CD31 was found in aortic endothelial cells. In several EC stained for SR-B1 red color was present on both apical & basolateral sides (a). (d, e, & f) Immunohistological analysis of SR-BI localization in aortic sections of Scarb1-KO mice. There is no red signal in aorta from Scarb1-KO mice. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26504816), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-101_rabbit-polyclonal-sr-bi-antibody-31020241517529.jpg)
![Immunocytochemistry/ Immunofluorescence: SR-BI Antibody - BSA Free [NB400-101] - Immunofluorescent analysis of SR-BI localization in liver of normal, Tie2-Scarb1 × Scarb1-KO, & Scarb1-KO mice. Liver sections from normal (a, b) & Tie2-Scarb1 × Scarb1-KO mice (c) were stained for SR-BI (red) & cytokeratin 8–18 (green). Merge image for normal mouse (b) demonstrates strong presence of SR-BI in hepatocytes (b, yellow signal) & absence of detectable level of SR-BI protein in liver of Tie2-Scarb1 × Scarb1-KO mice (c). In Scarb1-KO mice there was no detectable level of SR-BI protein (d, staining for SR-BI). Blue = DAPI. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26504816), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-101_rabbit-polyclonal-sr-bi-antibody-310202415392517.jpg)
![Immunocytochemistry/ Immunofluorescence: SR-BI Antibody - BSA Free [NB400-101] - Immunofluorescent analysis of SR-BI localization in liver of normal, Tie2-Scarb1 × Scarb1-KO, & Scarb1-KO mice. Liver sections from normal (a, b) & Tie2-Scarb1 × Scarb1-KO mice (c) were stained for SR-BI (red) & cytokeratin 8–18 (green). Merge image for normal mouse (b) demonstrates strong presence of SR-BI in hepatocytes (b, yellow signal) & absence of detectable level of SR-BI protein in liver of Tie2-Scarb1 × Scarb1-KO mice (c). In Scarb1-KO mice there was no detectable level of SR-BI protein (d, staining for SR-BI). Blue = DAPI. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26504816), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-101_rabbit-polyclonal-sr-bi-antibody-310202415384155.jpg)
![Immunocytochemistry/ Immunofluorescence: SR-BI Antibody - BSA Free [NB400-101] - Immunofluorescent analysis of SR-BI localization in aorta of Tie2-Scarb1 × Scarb1-KO & Scarb1-KO mice. Mouse aorta sections were stained for SR-BI (a & d, red) & CD31 (b & e, green). Colocalization of SR-BI & CD31 was presented on (c) & (f). Blue = DAPI. (a, b, & c) Immunohistological analysis of SR-BI localization in aortic sections of Tie2-Scarb1 × Scarb1-KO mice. Colocalization of SR-BI & CD31 was found in aortic endothelial cells. In several EC stained for SR-B1 red color was present on both apical & basolateral sides (a). (d, e, & f) Immunohistological analysis of SR-BI localization in aortic sections of Scarb1-KO mice. There is no red signal in aorta from Scarb1-KO mice. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26504816), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-101_rabbit-polyclonal-sr-bi-antibody-310202415171323.jpg)
![Immunocytochemistry/ Immunofluorescence: SR-BI Antibody - BSA Free [NB400-101] - Immunofluorescent analysis of SR-BI localization in aorta of Tie2-Scarb1 × Scarb1-KO & Scarb1-KO mice. Mouse aorta sections were stained for SR-BI (a & d, red) & CD31 (b & e, green). Colocalization of SR-BI & CD31 was presented on (c) & (f). Blue = DAPI. (a, b, & c) Immunohistological analysis of SR-BI localization in aortic sections of Tie2-Scarb1 × Scarb1-KO mice. Colocalization of SR-BI & CD31 was found in aortic endothelial cells. In several EC stained for SR-B1 red color was present on both apical & basolateral sides (a). (d, e, & f) Immunohistological analysis of SR-BI localization in aortic sections of Scarb1-KO mice. There is no red signal in aorta from Scarb1-KO mice. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26504816), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-101_rabbit-polyclonal-sr-bi-antibody-310202415395943.jpg)
![Immunocytochemistry/ Immunofluorescence: SR-BI Antibody - BSA Free [NB400-101] - Immunofluorescent analysis of SR-BI localization in aorta of Tie2-Scarb1 × Scarb1-KO & Scarb1-KO mice. Mouse aorta sections were stained for SR-BI (a & d, red) & CD31 (b & e, green). Colocalization of SR-BI & CD31 was presented on (c) & (f). Blue = DAPI. (a, b, & c) Immunohistological analysis of SR-BI localization in aortic sections of Tie2-Scarb1 × Scarb1-KO mice. Colocalization of SR-BI & CD31 was found in aortic endothelial cells. In several EC stained for SR-B1 red color was present on both apical & basolateral sides (a). (d, e, & f) Immunohistological analysis of SR-BI localization in aortic sections of Scarb1-KO mice. There is no red signal in aorta from Scarb1-KO mice. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26504816), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-101_rabbit-polyclonal-sr-bi-antibody-310202415175263.jpg)
![Immunocytochemistry/ Immunofluorescence: SR-BI Antibody - BSA Free [NB400-101] - Immunofluorescent analysis of SR-BI localization in liver of normal, Tie2-Scarb1 × Scarb1-KO, & Scarb1-KO mice. Liver sections from normal (a, b) & Tie2-Scarb1 × Scarb1-KO mice (c) were stained for SR-BI (red) & cytokeratin 8–18 (green). Merge image for normal mouse (b) demonstrates strong presence of SR-BI in hepatocytes (b, yellow signal) & absence of detectable level of SR-BI protein in liver of Tie2-Scarb1 × Scarb1-KO mice (c). In Scarb1-KO mice there was no detectable level of SR-BI protein (d, staining for SR-BI). Blue = DAPI. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26504816), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-101_rabbit-polyclonal-sr-bi-antibody-310202415384121.jpg)
![Immunocytochemistry/ Immunofluorescence: SR-BI Antibody - BSA Free [NB400-101] - SR-BI distribution in polarized EC SVEC4-10 cells. SR-BI localization is presented in (a) as x-y image & orthogonal (x-z & y-z) views. (b) & (c) represent rendering of SR-BI staining (red) throughout the cells. Nuclei: blue. In (b) & (c) basolateral surface is on the top & the bottom, respectively. These results demonstrate the presence of SR-BI on both the apical & the basolateral sides of EC. The size of scale bar on (a) is 5 μm & on (b) & (c) 10 μm. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26504816), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-101_rabbit-polyclonal-sr-bi-antibody-31020241535669.jpg)
![Western Blot: SR-BI Antibody - BSA Free [NB400-101] - Western blot & Coomassie stain of membrane fractions isolated from livers of normal C57Bl/6N (lane 1), Scarb1-KO (lane 2), & LIV11-SCARB1 × Scarb1-KO (lane 3) mice. 20 μg of membrane protein was loaded into each lane. (a) Western blot (anti-SR-BI antibody). (b) Coomassie stain (loading control for Western blot) encompassing the same MW region as SR-BI. Aliquots from the same tube were loaded for the Western blot & for the Coomassie-stained gel, which shows comparable loading between the three samples. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26504816), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-101_rabbit-polyclonal-sr-bi-antibody-31020241539732.jpg)
![Immunocytochemistry/ Immunofluorescence: SR-BI Antibody - BSA Free [NB400-101] - SR-BI distribution in polarized EC SVEC4-10 cells. SR-BI localization is presented in (a) as x-y image & orthogonal (x-z & y-z) views. (b) & (c) represent rendering of SR-BI staining (red) throughout the cells. Nuclei: blue. In (b) & (c) basolateral surface is on the top & the bottom, respectively. These results demonstrate the presence of SR-BI on both the apical & the basolateral sides of EC. The size of scale bar on (a) is 5 μm & on (b) & (c) 10 μm. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26504816), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-101_rabbit-polyclonal-sr-bi-antibody-310202415304249.jpg)
![Immunocytochemistry/ Immunofluorescence: SR-BI Antibody - BSA Free [NB400-101] - Immunofluorescent analysis of SR-BI localization in liver of normal, Tie2-Scarb1 × Scarb1-KO, & Scarb1-KO mice. Liver sections from normal (a, b) & Tie2-Scarb1 × Scarb1-KO mice (c) were stained for SR-BI (red) & cytokeratin 8–18 (green). Merge image for normal mouse (b) demonstrates strong presence of SR-BI in hepatocytes (b, yellow signal) & absence of detectable level of SR-BI protein in liver of Tie2-Scarb1 × Scarb1-KO mice (c). In Scarb1-KO mice there was no detectable level of SR-BI protein (d, staining for SR-BI). Blue = DAPI. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26504816), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-101_rabbit-polyclonal-sr-bi-antibody-310202415384113.jpg)
![Western Blot: SR-BI Antibody - BSA Free [NB400-101] - Liver mRNA & protein expression analysis of chow-fed Osbpl8KO mice.A: qPCR analysis of the quantity of the mRNAs identified at the bottom in chow-fed KO females (open bars) & males (closed bars). The mRNAs were quantified using ribosomal protein 36B4 message as a housekeeping reference. The data are expressed relative to quantity in littermate WT animals of the same gender, & represent mean ± s.e.m. (n = 6; *p<0.05, **p<0.01, T-test). B: Western blot analysis of ABCA1 & SR-B1 proteins in WT & KO mouse liver. The blots were probed with anti-beta -actin as a loading control. Densitometric quantification of the Western blot data is shown on the right. The results were normalized against beta -actin. The data represents mean ± s.e.m. (n = 4). Image collected & cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0058856), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-101_rabbit-polyclonal-sr-bi-antibody-3102024153435.jpg)
![Western Blot: SR-BI Antibody - BSA Free [NB400-101] - Western blot & Coomassie stain of membrane fractions isolated from livers of normal C57Bl/6N (lane 1), Scarb1-KO (lane 2), & LIV11-SCARB1 × Scarb1-KO (lane 3) mice. 20 μg of membrane protein was loaded into each lane. (a) Western blot (anti-SR-BI antibody). (b) Coomassie stain (loading control for Western blot) encompassing the same MW region as SR-BI. Aliquots from the same tube were loaded for the Western blot & for the Coomassie-stained gel, which shows comparable loading between the three samples. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26504816), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-101_rabbit-polyclonal-sr-bi-antibody-3102024153971.jpg)
![Immunocytochemistry/ Immunofluorescence: SR-BI Antibody - BSA Free [NB400-101] - SR-BI distribution in polarized EC SVEC4-10 cells. SR-BI localization is presented in (a) as x-y image & orthogonal (x-z & y-z) views. (b) & (c) represent rendering of SR-BI staining (red) throughout the cells. Nuclei: blue. In (b) & (c) basolateral surface is on the top & the bottom, respectively. These results demonstrate the presence of SR-BI on both the apical & the basolateral sides of EC. The size of scale bar on (a) is 5 μm & on (b) & (c) 10 μm. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26504816), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-101_rabbit-polyclonal-sr-bi-antibody-31020241536378.jpg)
![Immunocytochemistry/ Immunofluorescence: SR-BI Antibody - BSA Free [NB400-101] - Immunofluorescent analysis of SR-BI localization in aorta of Tie2-Scarb1 × Scarb1-KO & Scarb1-KO mice. Mouse aorta sections were stained for SR-BI (a & d, red) & CD31 (b & e, green). Colocalization of SR-BI & CD31 was presented on (c) & (f). Blue = DAPI. (a, b, & c) Immunohistological analysis of SR-BI localization in aortic sections of Tie2-Scarb1 × Scarb1-KO mice. Colocalization of SR-BI & CD31 was found in aortic endothelial cells. In several EC stained for SR-B1 red color was present on both apical & basolateral sides (a). (d, e, & f) Immunohistological analysis of SR-BI localization in aortic sections of Scarb1-KO mice. There is no red signal in aorta from Scarb1-KO mice. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26504816), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-101_rabbit-polyclonal-sr-bi-antibody-310202415284531.jpg)
![Immunocytochemistry/ Immunofluorescence: SR-BI Antibody - BSA Free [NB400-101] - Immunofluorescent analysis of SR-BI localization in liver of normal, Tie2-Scarb1 × Scarb1-KO, & Scarb1-KO mice. Liver sections from normal (a, b) & Tie2-Scarb1 × Scarb1-KO mice (c) were stained for SR-BI (red) & cytokeratin 8–18 (green). Merge image for normal mouse (b) demonstrates strong presence of SR-BI in hepatocytes (b, yellow signal) & absence of detectable level of SR-BI protein in liver of Tie2-Scarb1 × Scarb1-KO mice (c). In Scarb1-KO mice there was no detectable level of SR-BI protein (d, staining for SR-BI). Blue = DAPI. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/26504816), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-101_rabbit-polyclonal-sr-bi-antibody-31020241537193.jpg)
![Western Blot: SR-BI Antibody [NB400-113] - Detection of SR-BI (80kDa) in mouse testis lysate total protein using NB400-113.](http://images.novusbio.com/fullsize/SR-BI-Antibody-Western-Blot-NB400-113-img0009.jpg "Western Blot: SR-BI Antibody [NB400-113] - Detection of SR-BI (80kDa) in mouse testis lysate total protein using NB400-113.")
![Immunocytochemistry/Immunofluorescence: SR-BI Antibody [NB400-113] - Antibody was tested in HeLa cells with DyLight 488 (green). Nuclei and alpha-tubulin were counterstained with DAPI (blue) and DyLight 550 (red).](http://images.novusbio.com/fullsize/SR-BI-Antibody-Immunocytochemistry-Immunofluorescence-NB400-113-img0006.jpg)
![Immunohistochemistry-Paraffin: SR-BI Antibody [NB400-113] - Analysis of a FFPE section of human adrenal gland tissue using 1:100 dilution of SR-BI antibody. The staining was developed using HRP-DAB based detection method and the nuclei of the cells were counterstained with hematoxylin. This antibody generated a specific staining of SR-BI/SCARB1 in the glandular cells. The staining was membrane-cytoplasmic in the zona glomerulosa cells while the signal was primarily localized to the membranes of the cells in the zona fasciculata and zona reticularis layers of the adrenal cortex.](http://images.novusbio.com/fullsize/SR-BI-Antibody-Immunohistochemistry-Paraffin-NB400-113-img0008.jpg)
![Immunohistochemistry-Paraffin: SR-BI Antibody [NB400-113] - Analysis of a FFPE section of human adrenal gland tissue using 1:100 dilution of SR-BI antibody. The staining was developed using HRP-DAB based detection method and the nuclei of the cells were counterstained using hematoxylin. The representative section shows SR-BI/SCARB1 positivity in the glandular cells and the staining was mainly localized to the membranes of the cells.](http://images.novusbio.com/fullsize/SR-BI-Antibody-Immunohistochemistry-Paraffin-NB400-113-img0007.jpg)
![Western Blot: SR-BI Antibody [NB400-113] - Cell surface expression of SR-BI in renal carcinoma cells. Western blot analysis of SR-BI in total cell lysates (left) and on the cell surface (right) in 786-O and 786-O-VHL cells. The Western blots were probed with anti-SR-BI (82 kDa), anti-TBP (40 kDa, used as a control for intracellular protein expression), and anti-Na+/K+-ATPase (110 kDa, used as a control for cell surface protein expression). Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30173145/) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/nb400-113_rabbit-polyclonal-sr-bi-antibody-2552023151494.jpg)
![Immunohistochemistry-Paraffin: LIMPII/SR-B2 Antibody [NB400-129] - Comparison of LIMP2-positive organelles in young (A) and aged (C) rat urothelium. LIMP2-positive structures (green) shown in umbrella cells (delineated by dashed yellow line). Rhodamine phalloidin (red), which labels the cortical actin cytoskeleton, was used to show cell borders. Umbrella cells show an apparent, age-related increase in LIMP2 staining (white arrows). Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0198817), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/LIMPII-SR-B2-Antibody-Immunohistochemistry-Paraffin-NB400-129-img0009.jpg "Immunohistochemistry-Paraffin: LIMPII/SR-B2 Antibody [NB400-129] - Comparison of LIMP2-positive organelles in young (A) and aged (C) rat urothelium. LIMP2-positive structures (green) shown in umbrella cells (delineated by dashed yellow line). Rhodamine phalloidin (red), which labels the cortical actin cytoskeleton, was used to show cell borders. Umbrella cells show an apparent, age-related increase in LIMP2 staining (white arrows). Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0198817), licensed under a CC-BY license.")
![Western Blot: LIMPII/SR-B2 Antibody [NB400-129] - Detection of LIMP II (~85 kDa) in Lane 1: Rat cardiac fibroblasts (RCF), 3T3 mouse fibroblasts (2), canine lung lysate (3), RCF treated with angiotensin II (4), and H2O2 (5), HEPG2 human liver lysate (6).](http://images.novusbio.com/fullsize/LIMPII-SR-B2-Antibody-Western-Blot-NB400-129-img0004.jpg)
![Simple Western: LIMPII/SR-B2 Antibody [NB400-129] - CHAPS-solublized SVG-A (human astrocyte cells) and B103 (rat neuroblastoma cells) cell lyates, at the indicated concentrations, were probed with a 1:25 dilution of antibody. Image from verified customer review.](http://images.novusbio.com/fullsize/LIMPII-SR-B2-Antibody-Simple-Western-NB400-129-img0008.jpg)
![Immunohistochemistry-Paraffin: LIMPII/SR-B2 Antibody [NB400-129] - Lysotracker Red accumulates in endolysosomes.Immunofluorescence of young (A) and aged (C) urothelium incubated with Lysotracker Red (red) and co-stained with antibodies to LIMP2 (green structures) and phalloidin (blue), which labels the cortical actin cytoskeleton. Large, Lysotracker Red-positive endolysosomes are marked with white arrows. Underlying intermediate (IC) and basal cells (BC) show non-specific cytoplasmic Lysotracker Red staining that did not appear in umbrella cells (UC). Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0198817), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/LIMPII-SR-B2-Antibody-Immunohistochemistry-Paraffin-NB400-129-img0010.jpg)
![Immunocytochemistry/Immunofluorescence: LIMPII/SR-B2 Antibody [NB400-129] - Detection of LIMPII/lpg85 (Green) in Hela cells using NB400-129. Nuclei (Blue) are counterstained using Hoechst 33258.](http://images.novusbio.com/fullsize/LIMPII-SR-B2-Antibody-Immunocytochemistry-Immunofluorescence-NB400-129-img0007.jpg)
![Immunohistochemistry: LIMPII/SR-B2 Antibody [NB400-129] - Substitution V135A enhances PSGL1 usage by mouse-adapted EV-A71. LIMPII/SR-B2 (SCARB2) and PSGL1 in various organs tissues assessed by means of immunohistochemistry. SCARB2 protein expression in CNS, intestine, pancreas, liver and lung. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31339457/) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/LIMPII-SR-B2 Antibody-Immunohistochemistry-NB400-129-img0011.jpg)
![Immunohistochemistry: LIMPII/SR-B2 Antibody [NB400-129] - Staining of LIMP II in rat infarctzone tissue with a DAB detection system.](http://images.novusbio.com/fullsize/LIMPII-SR-B2-Antibody-Immunohistochemistry-NB400-129-img0005.jpg)
![Immunocytochemistry/ Immunofluorescence: LIMPII/SR-B2 Antibody [NB400-129] - Comparison of LIMP2-positive organelles in young (A), adult (B), & aged (C) rat urothelium. LIMP2-positive structures (green) shown in umbrella cells (delineated by dashed yellow line). Rhodamine phalloidin (red), which labels the cortical actin cytoskeleton, was used to show cell borders. Umbrella cells show an apparent, age-related increase in LIMP2 staining (white arrows). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29883476), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-129_rabbit-polyclonal-limpii-sr-b2-antibody-31020241530421.jpg)
![Immunocytochemistry/ Immunofluorescence: LIMPII/SR-B2 Antibody [NB400-129] - Lysotracker Red accumulates in endolysosomes.Immunofluorescence of young (A), adult (B), & aged (C) urothelium incubated with Lysotracker Red (red) & co-stained with antibodies to LIMP2 (green structures) & phalloidin (blue), which labels the cortical actin cytoskeleton. Large, Lysotracker Red-positive endolysosomes are marked with white arrows. Underlying intermediate (IC) & basal cells (BC) show non-specific cytoplasmic Lysotracker Red staining that did not appear in umbrella cells (UC). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29883476), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-129_rabbit-polyclonal-limpii-sr-b2-antibody-310202415334943.jpg)
![Immunocytochemistry/ Immunofluorescence: LIMPII/SR-B2 Antibody [NB400-129] - Comparison of LIMP2-positive organelles in young (A), adult (B), & aged (C) rat urothelium. LIMP2-positive structures (green) shown in umbrella cells (delineated by dashed yellow line). Rhodamine phalloidin (red), which labels the cortical actin cytoskeleton, was used to show cell borders. Umbrella cells show an apparent, age-related increase in LIMP2 staining (white arrows). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29883476), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-129_rabbit-polyclonal-limpii-sr-b2-antibody-31020241534378.jpg)
![Immunocytochemistry/ Immunofluorescence: LIMPII/SR-B2 Antibody [NB400-129] - Comparison of LIMP2-positive organelles in young (A), adult (B), & aged (C) rat urothelium. LIMP2-positive structures (green) shown in umbrella cells (delineated by dashed yellow line). Rhodamine phalloidin (red), which labels the cortical actin cytoskeleton, was used to show cell borders. Umbrella cells show an apparent, age-related increase in LIMP2 staining (white arrows). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29883476), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-129_rabbit-polyclonal-limpii-sr-b2-antibody-310202415304272.jpg)
![Immunocytochemistry/ Immunofluorescence: LIMPII/SR-B2 Antibody [NB400-129] - Lysotracker Red accumulates in endolysosomes.Immunofluorescence of young (A), adult (B), & aged (C) urothelium incubated with Lysotracker Red (red) & co-stained with antibodies to LIMP2 (green structures) & phalloidin (blue), which labels the cortical actin cytoskeleton. Large, Lysotracker Red-positive endolysosomes are marked with white arrows. Underlying intermediate (IC) & basal cells (BC) show non-specific cytoplasmic Lysotracker Red staining that did not appear in umbrella cells (UC). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29883476), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-129_rabbit-polyclonal-limpii-sr-b2-antibody-310202415291970.jpg)
![Immunocytochemistry/ Immunofluorescence: LIMPII/SR-B2 Antibody [NB400-129] - Lysotracker Red accumulates in endolysosomes.Immunofluorescence of young (A), adult (B), & aged (C) urothelium incubated with Lysotracker Red (red) & co-stained with antibodies to LIMP2 (green structures) & phalloidin (blue), which labels the cortical actin cytoskeleton. Large, Lysotracker Red-positive endolysosomes are marked with white arrows. Underlying intermediate (IC) & basal cells (BC) show non-specific cytoplasmic Lysotracker Red staining that did not appear in umbrella cells (UC). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29883476), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-129_rabbit-polyclonal-limpii-sr-b2-antibody-310202415284535.jpg)
![Western Blot: LDL R Antibody (C7) [NBP1-78159] - Total protein from human HeLa and HepG2 cells was separated on a 7.5% gel by SDS-PAGE, transferred to PVDF membrane and blocked in 5% non-fat milk in TBST. The membrane was probed with 0.5 ug/mL anti-LDL receptor in 1% non-fat milk in TBST and detected with an anti-mouse HRP secondary antibody using chemiluminescence.](http://images.novusbio.com/fullsize/LDL-R-Antibody-C7-Western-Blot-NBP1-78159-img0008.jpg "Western Blot: LDL R Antibody (C7) [NBP1-78159] - Total protein from human HeLa and HepG2 cells was separated on a 7.5% gel by SDS-PAGE, transferred to PVDF membrane and blocked in 5% non-fat milk in TBST. The membrane was probed with 0.5 ug/mL anti-LDL receptor in 1% non-fat milk in TBST and detected with an anti-mouse HRP secondary antibody using chemiluminescence.")
![Immunocytochemistry/Immunofluorescence: LDLR Antibody (C7) [NBP1-78159] - Immunocytochemistry of LA-6 and intact MPEFs (used as positive control) using anti-LDLR antibody. The parental MPEFs reactive to the secondary antibody (fluorescein-labeled anti-mouse IgG) alone are designated as negative control. All cells were counterstained with DAPI upon reaction with the secondary antibody. Bar = 30 um. Image collected and cropped by CiteAb from the following publication (www.mdpi.com/1422-0067/18/12/2610) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/LDLR-Antibody-C7-Immunocytochemistry-Immunofluorescence-NBP1-78159-img0010.jpg)
![Immunohistochemistry: LDL R Antibody (C7) [NBP1-78159] - Analysis of an FFPE tissue section of human liver using LDL Receptor antibody (clone C7) with HRP-DAB based detection and hematoxylin counterstaining.](http://images.novusbio.com/fullsize/LDL-R-Antibody-C7-Immunohistochemistry-NBP1-78159-img0006.jpg)
![Immunocytochemistry/Immunofluorescence: LDL R Antibody (C7) [NBP1-78159] - Antibody was tested in HepG2 cells with FITC (green). Nuclei were counterstained with DAPI (blue).](http://images.novusbio.com/fullsize/LDL-R-Antibody-C7-Immunocytochemistry-Immunofluorescence-NBP1-78159-img0005.jpg)
![Immunocytochemistry/Immunofluorescence: LDL R Antibody (C7) [NBP1-78159] - Image from a customer review on porcine intestinal epithelial cells IPEC-J2.](http://images.novusbio.com/fullsize/LDL-R-Antibody-C7-Immunocytochemistry-Immunofluorescence-NBP1-78159-img0007.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)
![Western Blot: LDLR Antibody [NBP1-06709] - 8-weeks-old male Ces1 -/- Ldlr -/- (DKO) mice and control littermates Ces1 +/+ Ldlr -/- (Ldlr -/-) mice were fed a Western diet for 16 weeks (n = 8). Hepatic Ces1/Ces1g and LDLR protein levels were determined. Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/s41598-017-18232-x) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/LDLR-Antibody-Knockout-Validated-NBP1-06709-img0009.jpg "<b>Genetic Strategies Validation. </b>Western Blot: LDLR Antibody [NBP1-06709] - 8-weeks-old male Ces1 -/- Ldlr -/- (DKO) mice and control littermates Ces1 +/+ Ldlr -/- (Ldlr -/-) mice were fed a Western diet for 16 weeks (n = 8). Hepatic Ces1/Ces1g and LDLR protein levels were determined. Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/s41598-017-18232-x) licensed under a CC-BY license.")
![<b>Genetic Strategies Validation. </b>Immunocytochemistry/Immunofluorescence: LDLR Antibody [NBP1-06709] - HepG2 cells were fixed for 10 minutes using 4% paraformaldehyde for 10 minutes and permeabilized in 0.05% Triton X-100 in PBS for 5 minutes. The cells were incubated with anti-LDLR at 1 ug/ml overnight at 4C and detected with an anti-rabbit Dylight 488 (Green) at a 1:1000 dilution. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 40X objective.](http://images.novusbio.com/fullsize/LDLR-Antibody-Immunocytochemistry-Immunofluorescence-NBP1-06709-img0008.jpg)
![Simple Western: LDLR Antibody [NBP1-06709] - LDL R Antibody [NBP1-06709] - Simple Western lane view shows a specific band for LDL R in 0.05 mg/ml of HepG2 lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system.](http://images.novusbio.com/fullsize/LDL-R-Antibody-Simple-Western-NBP1-06709-img0004.jpg)
![Western Blot: LDLR Antibody [NBP1-06709] - LDL R Antibody [NBP1-06709] - Western Blot on HepG2 whole cell lysate.](http://images.novusbio.com/fullsize/LDL-R-Antibody-Western-Blot-NBP1-06709-img0002.jpg)
![Immunohistochemistry-Paraffin: LDL R Antibody [NBP1-06709] - LDL Receptor was detected in immersion fixed paraffin-embedded sections of human liver cancer using rabbit anti-human antibody (Catalog # NBP1-06709) at 1:3000 dilution overnight at 4C. Tissue was stained using the VisuCyte anti-rabbit HRP polymer detection reagent (Catalog # VC003) with DAB chromogen (brown) and counterstained with hematoxylin (blue).Images may not be copied, printed or otherwise disseminated without express written permission of Novus Biologicals a bio-techne brand.](http://images.novusbio.com/fullsize/LDL-R-Antibody-Immunohistochemistry-Paraffin-NBP1-06709-img0007.jpg)
![Immunocytochemistry/Immunofluorescence: LDL R Antibody [NBP1-06709] - LDL receptor antibody was tested in HepG2 cells with Dylight 488 (green). Nuclei and alpha-tubulin were counterstained with DAPI (blue) and Dylight 550 (red).](http://images.novusbio.com/fullsize/LDL-R-Antibody-Immunocytochemistry-Immunofluorescence-NBP1-06709-img0003.jpg)
![Western Blot: Rabbit Polyclonal LDLR Antibody [NBP1-06709] - Analysis of LDLR in bovine and canine corpus luetum. Image for a verified customer review.](http://images.novusbio.com/fullsize/antibody/nbp1-06709_rabbit-polyclonal-ldlr-antibody-western-blot-283202515254..jpg)
![Immunohistochemistry: CD36 Antibody [NB400-145] - CD36 ligand disrupts TLR2-CD36 interaction modulated TLR2 heterodimer-signaling. (A) Confocal imaging of central retina cryosection stained with CD11b (white), CD36 (red), TLR2 (green), and DAPI (blue) from blue light-challenged WT mice. Scale bar = 25 um. (B) High magnification (3X) shows subretinal CD11b-positive cells (white) with the co-localisation of CD36 (red) and TLR2 (green). Scale bar = 5 um. Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/s41598-019-49472-8), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/CD36-Antibody-Immunohistochemistry-NB400-145-img0009.jpg "Immunohistochemistry: CD36 Antibody [NB400-145] - CD36 ligand disrupts TLR2-CD36 interaction modulated TLR2 heterodimer-signaling. (A) Confocal imaging of central retina cryosection stained with CD11b (white), CD36 (red), TLR2 (green), and DAPI (blue) from blue light-challenged WT mice. Scale bar = 25 um. (B) High magnification (3X) shows subretinal CD11b-positive cells (white) with the co-localisation of CD36 (red) and TLR2 (green). Scale bar = 5 um. Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/s41598-019-49472-8), licensed under a CC-BY license.")
![Simple Western: CD36 Antibody [NB400-145] - Image shows a specific band for CD36 in human adipose lysate. This experiment was performed under reducing conditions using the 12-230 kDa separation system.](http://images.novusbio.com/fullsize/CD36-Antibody-Simple-Western-NB400-145-img0007.jpg)
![Western Blot: CD36 Antibody [NB400-145] - Detection of CD36 in human adipocyte extract (30 ug). Lane 1: 0.5 ug/ml NB 400-145; lane 2: 2 ug/ml NB 400-145. ECL: 3 second exposure.](http://images.novusbio.com/fullsize/CD36-Antibody-Western-Blot-NB400-145-img0006.jpg)
![Western Blot: CD36 Antibody - BSA Free [NB400-145] - CD36 ligand disrupts TLR2-CD36 interaction modulated TLR2 heterodimer-signaling. (A) Confocal imaging of central retina cryosection stained with CD11b (white), CD36 (red), TLR2 (green), & DAPI (blue) from blue light-challenged WT mice. Scale bar = 25 μm. (B) High magnification (3X) shows subretinal CD11b-positive cells (white) with the co-localisation of CD36 (red) & TLR2 (green). Scale bar = 5 μm. (C-F) Peritoneal MPs were stimulated with 300 ng/ml R-FSL1 in the presence of 10−7 M MPE-001 or vehicle. (C) MPE-001 disrupted the interaction between CD36 labeled with Cy5 (red) & TLR2 labeled with Cy3 (green) as assessed by FRET after 5 min stimulation with R-FSL1. (D) Percentage of energy transfer measured using LSM-700 confocal microscope (Zeiss). Data in B,C are representative of 3-4 independent experiments. (E) Phosphorylated & total Western blot density bands of IRAK4, IKK alpha beta & P65-NF kappa B, JNK & P38 in peritoneal MPs from CD36+/+ & CD36−/− mice stimulated with R-FSL1. (F) Quantification of P65-NF kappa B following stimulation of CD36+/+ & CD36−/− peritoneal MPs with R-FSL1 using ELISA-based assay. Data in C-F are representative of 3 independent experiments (n = 3/group). In (D,F) one-way ANOVA test with Newman-Keuls post-test for multiple comparison was performed. *P < 0.05, **P < 0.01 & ***P < 0.001 vs R-FSL1. Data are shown as mean ± S.E.M. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31501473), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-145_rabbit-polyclonal-cd36-antibody-31020241618930.jpg)
![Immunocytochemistry/ Immunofluorescence: CD36 Antibody - BSA Free [NB400-145] - CD36 ligand disrupts TLR2-CD36 interaction modulated TLR2 heterodimer-signaling. (A) Confocal imaging of central retina cryosection stained with CD11b (white), CD36 (red), TLR2 (green), & DAPI (blue) from blue light-challenged WT mice. Scale bar = 25 μm. (B) High magnification (3X) shows subretinal CD11b-positive cells (white) with the co-localisation of CD36 (red) & TLR2 (green). Scale bar = 5 μm. (C-F) Peritoneal MPs were stimulated with 300 ng/ml R-FSL1 in the presence of 10−7 M MPE-001 or vehicle. (C) MPE-001 disrupted the interaction between CD36 labeled with Cy5 (red) & TLR2 labeled with Cy3 (green) as assessed by FRET after 5 min stimulation with R-FSL1. (D) Percentage of energy transfer measured using LSM-700 confocal microscope (Zeiss). Data in B,C are representative of 3-4 independent experiments. (E) Phosphorylated & total Western blot density bands of IRAK4, IKK alpha beta & P65-NF kappa B, JNK & P38 in peritoneal MPs from CD36+/+ & CD36−/− mice stimulated with R-FSL1. (F) Quantification of P65-NF kappa B following stimulation of CD36+/+ & CD36−/− peritoneal MPs with R-FSL1 using ELISA-based assay. Data in C-F are representative of 3 independent experiments (n = 3/group). In (D,F) one-way ANOVA test with Newman-Keuls post-test for multiple comparison was performed. *P < 0.05, **P < 0.01 & ***P < 0.001 vs R-FSL1. Data are shown as mean ± S.E.M. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31501473), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-145_rabbit-polyclonal-cd36-antibody-31020241616182.jpg)
![Immunocytochemistry/ Immunofluorescence: CD36 Antibody - BSA Free [NB400-145] - CD36 ligand disrupts TLR2-CD36 interaction modulated TLR2 heterodimer-signaling. (A) Confocal imaging of central retina cryosection stained with CD11b (white), CD36 (red), TLR2 (green), & DAPI (blue) from blue light-challenged WT mice. Scale bar = 25 μm. (B) High magnification (3X) shows subretinal CD11b-positive cells (white) with the co-localisation of CD36 (red) & TLR2 (green). Scale bar = 5 μm. (C-F) Peritoneal MPs were stimulated with 300 ng/ml R-FSL1 in the presence of 10−7 M MPE-001 or vehicle. (C) MPE-001 disrupted the interaction between CD36 labeled with Cy5 (red) & TLR2 labeled with Cy3 (green) as assessed by FRET after 5 min stimulation with R-FSL1. (D) Percentage of energy transfer measured using LSM-700 confocal microscope (Zeiss). Data in B,C are representative of 3-4 independent experiments. (E) Phosphorylated & total Western blot density bands of IRAK4, IKK alpha beta & P65-NF kappa B, JNK & P38 in peritoneal MPs from CD36+/+ & CD36−/− mice stimulated with R-FSL1. (F) Quantification of P65-NF kappa B following stimulation of CD36+/+ & CD36−/− peritoneal MPs with R-FSL1 using ELISA-based assay. Data in C-F are representative of 3 independent experiments (n = 3/group). In (D,F) one-way ANOVA test with Newman-Keuls post-test for multiple comparison was performed. *P < 0.05, **P < 0.01 & ***P < 0.001 vs R-FSL1. Data are shown as mean ± S.E.M. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31501473), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-145_rabbit-polyclonal-cd36-antibody-31020241618949.jpg)
![Immunocytochemistry/ Immunofluorescence: CD36 Antibody - BSA Free [NB400-145] - CD36 ligand disrupts TLR2-CD36 interaction modulated TLR2 heterodimer-signaling. (A) Confocal imaging of central retina cryosection stained with CD11b (white), CD36 (red), TLR2 (green), & DAPI (blue) from blue light-challenged WT mice. Scale bar = 25 μm. (B) High magnification (3X) shows subretinal CD11b-positive cells (white) with the co-localisation of CD36 (red) & TLR2 (green). Scale bar = 5 μm. (C-F) Peritoneal MPs were stimulated with 300 ng/ml R-FSL1 in the presence of 10−7 M MPE-001 or vehicle. (C) MPE-001 disrupted the interaction between CD36 labeled with Cy5 (red) & TLR2 labeled with Cy3 (green) as assessed by FRET after 5 min stimulation with R-FSL1. (D) Percentage of energy transfer measured using LSM-700 confocal microscope (Zeiss). Data in B,C are representative of 3-4 independent experiments. (E) Phosphorylated & total Western blot density bands of IRAK4, IKK alpha beta & P65-NF kappa B, JNK & P38 in peritoneal MPs from CD36+/+ & CD36−/− mice stimulated with R-FSL1. (F) Quantification of P65-NF kappa B following stimulation of CD36+/+ & CD36−/− peritoneal MPs with R-FSL1 using ELISA-based assay. Data in C-F are representative of 3 independent experiments (n = 3/group). In (D,F) one-way ANOVA test with Newman-Keuls post-test for multiple comparison was performed. *P < 0.05, **P < 0.01 & ***P < 0.001 vs R-FSL1. Data are shown as mean ± S.E.M. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31501473), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-145_rabbit-polyclonal-cd36-antibody-310202416173513.jpg)
![Western Blot: Niemann-Pick type C1 Like-1 Antibody [NB400-127] - Detection of NPC1L1 protein in lysate of human small intestine tissue using Niemann-Pick type C1 Like-1 antibody at 2ug/ml concentration.](http://images.novusbio.com/fullsize/Niemann-Pick-type-C1-Like-1-Antibody-Western-Blot-NB400-127-img0007.jpg "Western Blot: Niemann-Pick type C1 Like-1 Antibody [NB400-127] - Detection of NPC1L1 protein in lysate of human small intestine tissue using Niemann-Pick type C1 Like-1 antibody at 2ug/ml concentration.")
![Immunocytochemistry/Immunofluorescence: Niemann-Pick type C1 Like-1 Antibody [NB400-127] - HepG2 cells were fixed in 4% paraformaldehyde for 10 min and permeabilized in 0.05% Triton X-100 in PBS for 5 minutes. The cells were incubated with anti-Niemann-Pick type C1 Like-1 Antibody (NB400-127) at 2 ug/ml overnight at 4C and detected with an anti-rabbit Dylight 488 (Green) at a 1:500 dilution for 60 minutes. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 100X objective and digitally deconvolved.](http://images.novusbio.com/fullsize/Niemann-Pick-type-C1-Like-1-Antibody-Immunocytochemistry-Immunofluorescence-NB400-127-img0008.jpg)
![Immunohistochemistry-Paraffin: Niemann-Pick type C1 Like-1 Antibody [NB400-127] - Analysis of a FFPE tissue section of mouse small intestine using 1:200 dilution of NPC1L1 antibody (NB400-127). The staining was developed using HRP labeled anti-rabbit secondary antibody and DAB reagent, and nuclei of cells were counter-stained with hematoxylin.](http://images.novusbio.com/fullsize/Niemann-Pick-type-C1-Like-1-Antibody-Immunohistochemistry-Paraffin-NB400-127-img0009.jpg)