| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB400-105SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB400-132SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB400-148SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB110-60531SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB400-128SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB400-127SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB100-2068SS | |||
| Azide and BSA Free | NBP2-80554 | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB400-164SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NB100-2216SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NBP1-78162SS | |||
| Azide and BSA Free | NBP2-81010 | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NBP1-31123SS | |||
| Formulation | Catalog # | Availability | Price | |
|---|---|---|---|---|
| BSA Free | NBP1-49529SS | |||
![Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - (A) Upregulation of ABCA1 & ABCG1 & (B) enhancement of cholesterol efflux by purple Perilla frutescens extracts (PPE) in 50 μg/ml Cu2+-oxidized low-density lipoproteins (LDL)-exposed J774A.1 murine macrophages. (A) For the measurement of ABCA1 & ABCG1 expression, total cell lysates were subjected to western blot analysis with a primary antibody against ABCA1 or ABCG1. beta -actin was used as an internal control. Bar graphs (means ± SEM, n=3) represent quantitative densitometric results of the upper bands. (B) Cholesterol efflux was expressed as the percentage of fluorescence in the medium relative to the total fluorescence. Bar graphs denoted without a common letter indicate significant difference, P<0.05. Image collected & cropped by CiteAb from the following publication (//www.spandidos-publications.com/10.3892/ijmm.2015.2101), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-105_rabbit-polyclonal-abca1-antibody-310202415382446.jpg)
![Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - 6‐Dihydroparadol increases A) ABCA1 & B) ABCG1, but not C) SR‐BI protein levels in cholesterol‐loaded THP‐1‐derived macrophages. THP‐1 cells were differentiated as described in Figure 2, & then loaded with unlabeled cholesterol for 24 h. Cells were treated with increasing concentrations of 6‐dihydroparadol (1–30 μm) for another 24 h. The protein levels of ABCA1, ABCG1, & SR‐B1 were detected by Western blot analysis. The control was treated with solvent vehicle (0.1% DMSO). As a positive control, TO901317 (5 μm, 24 h) was used. The bar graphs represent mean ± SD from three independent experiments. *p < 0.05, **p < 0.01, & ***p < 0.001 versus control (determined by Student's t‐test or ANOVA with Bonferroni's post hoc test). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29802792), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-105_rabbit-polyclonal-abca1-antibody-310202415384115.jpg)
![Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - Akt inhibition suppresses mTORC1 activity.BHK-ABCA1 cells were induced overnight with mifepristone (10 nM) & then incubated with DEBC, LY294002 or rapamycin at indicated concentrations for 2 h. Cells were then lysed & analyzed for ABCA1 & phosphorylated S6K by Western blotting. Actin was also blotted as loading control. Image collected & cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0113789), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-105_rabbit-polyclonal-abca1-antibody-31020241538240.jpg)
![Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - Reversal of hepatic steatosis by reduction of SREBP-1 levels.(a) Western blotting analysis of SREBP-1 & ABCA1 levels in livers of miR-33+/+Srebf1+/+, miR-33+/+Srebf1+/−, miR-33−/−Srebf1+/+ & miR-33−/−Srebf1+/− mice. Representative western blot images are shown (n=4). Image collected & cropped by CiteAb from following publication (//pubmed.ncbi.nlm.nih.gov/24300912), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-105_rabbit-polyclonal-abca1-antibody-310202415291985.jpg)
![Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - 6‐Dihydroparadol increases A) ABCA1 & B) ABCG1 protein stability. THP‐1 cells were differentiated as described in Figure 2. Then cells were loaded with unlabeled cholesterol & treated with 6‐dihydroparadol (10 μm), or solvent vehicle (0.1% DMSO, control) for 24 h. Cells were lysed at different time points (0, 1, 2, 3, 4, & 6 h) after treatment with the protein synthesis inhibitor cycloheximide (CHX, 100 μm). The protein levels of both ABCA1 & ABCG1 were detected by Western blot analysis. The data points represent mean ± SD from three independent experiments. *p < 0.05 & **p < 0.01 versus control at the same time point (determined by Student's t‐test). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29802792), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-105_rabbit-polyclonal-abca1-antibody-310202415394516.jpg)
![Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - Ligand activation of LXR inhibits LPS-induced MAP kinase activation through Abca1 induction.(A–D) Bone marrow-derived macrophages from Lxr alpha −/−Lxr beta −/− & control wild-type mice (A, B), or bone marrow-derived macrophages from myeloid-specific Abca1−/− & control wild-type mice (C, D) were pretreated with GW3965 (1 µM) overnight, followed by stimulation with LPS (10 ng/ml) for 20 min or 1 hr. Whole cell lysates were harvested & protein expression was analyzed by immunoblotting with the indicated antibodies (A, C). Protein expression was quantified by Image Quant TL7.0 (B, D). N = 4–6 per group. *p < 0.05, **p < 0.01, NS, not significant. Error bars represent means ± SEM.DOI://dx.doi.org/10.7554/eLife.08009.012 Image collected & cropped by CiteAb from the following publication (//elifesciences.org/articles/08009), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-105_rabbit-polyclonal-abca1-antibody-310202415392521.jpg)
![Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - 6‐Dihydroparadol increases A) ABCA1 & B) ABCG1, but not C) SR‐BI protein levels in cholesterol‐loaded THP‐1‐derived macrophages. THP‐1 cells were differentiated as described in Figure 2, & then loaded with unlabeled cholesterol for 24 h. Cells were treated with increasing concentrations of 6‐dihydroparadol (1–30 μm) for another 24 h. The protein levels of ABCA1, ABCG1, & SR‐B1 were detected by Western blot analysis. The control was treated with solvent vehicle (0.1% DMSO). As a positive control, TO901317 (5 μm, 24 h) was used. The bar graphs represent mean ± SD from three independent experiments. *p < 0.05, **p < 0.01, & ***p < 0.001 versus control (determined by Student's t‐test or ANOVA with Bonferroni's post hoc test). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29802792), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-105_rabbit-polyclonal-abca1-antibody-310202415392590.jpg)
![Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - Western Blotting for ABCA1, as detailed in Supplementary Protocol #5 (Additional file 1). Caco-2 cells cultivated on filter inserts were treated for 48 h with bexarotene (RXR agonist, 5 μM), T0901317 (LXR agonist, 10 μM), GW3965 (LXR agonist, 10 μM) or the vehicle control (DMSO 0.1%). Protein expression was then determined by western blot analysis. Results were normalized for interexperimental variance & then set in relation to the vehicle control. Bar graphs represent mean ± SD from three independent experiments. A representative blot is shown - the bands stem from the same membrane & the vertical line indicates excised irrelevant bands. ns not significant, *P < 0.05, **P < 0.01 versus solvent vehicle (determined by paired t-test) Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32308567), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-105_rabbit-polyclonal-abca1-antibody-310202415284512.jpg)
![Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - Ligand activation of LXR inhibits LPS-induced MAP kinase activation through Abca1 induction.(A–D) Bone marrow-derived macrophages from Lxr alpha −/−Lxr beta −/− & control wild-type mice (A, B), or bone marrow-derived macrophages from myeloid-specific Abca1−/− & control wild-type mice (C, D) were pretreated with GW3965 (1 µM) overnight, followed by stimulation with LPS (10 ng/ml) for 20 min or 1 hr. Whole cell lysates were harvested & protein expression was analyzed by immunoblotting with the indicated antibodies (A, C). Protein expression was quantified by Image Quant TL7.0 (B, D). N = 4–6 per group. *p < 0.05, **p < 0.01, NS, not significant. Error bars represent means ± SEM.DOI://dx.doi.org/10.7554/eLife.08009.012 Image collected & cropped by CiteAb from the following publication (//elifesciences.org/articles/08009), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-105_rabbit-polyclonal-abca1-antibody-310202415384110.jpg)
![Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - Ligand activation of LXR inhibits LPS-induced MAP kinase activation through Abca1 induction.(A–D) Bone marrow-derived macrophages from Lxr alpha −/−Lxr beta −/− & control wild-type mice (A, B), or bone marrow-derived macrophages from myeloid-specific Abca1−/− & control wild-type mice (C, D) were pretreated with GW3965 (1 µM) overnight, followed by stimulation with LPS (10 ng/ml) for 20 min or 1 hr. Whole cell lysates were harvested & protein expression was analyzed by immunoblotting with the indicated antibodies (A, C). Protein expression was quantified by Image Quant TL7.0 (B, D). N = 4–6 per group. *p < 0.05, **p < 0.01, NS, not significant. Error bars represent means ± SEM.DOI://dx.doi.org/10.7554/eLife.08009.012 Image collected & cropped by CiteAb from the following publication (//elifesciences.org/articles/08009), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-105_rabbit-polyclonal-abca1-antibody-31020241534346.jpg)
![Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - Expression of ABCA1 & CROT in livers & RIP140 in macrophages is elevated in miR-33−/−Apoe−/− mice compared with miR-33+/+Apoe−/− mice. A, Quantitative real-time PCR analysis of Abca1, Crot, Cpt1a, & Prkaa1in livers from miR-33+/+Apoe−/− & miR-33−/−Apoe−/− mice. Values from miR-33+/+Apoe−/− mice were set at 100%. Values are mean±SE (n=9 to 11each); **P<0.01. B, Western analysis of ABCA1, CROT, CPT1a, & AMPK alpha in livers from miR-33+/+Apoe−/− & miR-33−/−Apoe−/− mice. beta -actin was used as a loading control. C, Densitometry of ABCA1, CROT, CPT1a, & AMPK alpha in livers from miR-33+/+Apoe−/− & miR-33−/−Apoe−/− mice. Values from miR-33+/+Apoe−/− mice were set at 100%. Values are mean±SE (n=4 each); *P<0.05. D, Total cholesterol, free cholesterol, cholesterol ester, & triglyceride levels in livers of miR-33+/+Apoe−/− & miR-33−/−Apoe−/− mice. Values are mean±SE (n=9 to 11 each). E, HE staining of livers of miR-33+/+Apoe−/− & miR-33−/−Apoe−/− mice at age 20 weeks fed NC. Scale bar: 100 μm. F, Quantitative real-time PCR analysis of Nrip1 (RIP140) in peritoneal macrophages from miR-33+/+Apoe−/− & miR-33−/−Apoe−/− mice. Values from miR-33+/+Apoe−/− mice were set at 100%. Values are mean±SE (n=7 each). G, Western analysis of NRIP1 (RIP140) in peritoneal macrophages from miR-33+/+Apoe−/− & miR-33−/−Apoe−/− mice. GAPDH was used as a loading control. H, Densitometry of NRIP1 (RIP140) in peritoneal macrophages from miR-33+/+Apoe−/− & miR-33−/−Apoe−/− mice. Values from miR-33+/+Apoe−/− mice were set at 100%. Values are mean±SE (n=4 each); *P<0.05. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/23316322), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-105_rabbit-polyclonal-abca1-antibody-31020241616095.jpg)
![Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - Basal ABCA1 expression & function in patient-derived iRPEs. (A) Representation of patient-derived iPSC lines & genotypes harboring polymorphisms in ABCA1 that are associated with decreased or increased risk for AMD development. (B) Relative expression of ABCA1 mRNA in patient-derived iRPEs under basal conditions normalized to RPL28 & decreased risk group. (C) Western blot analysis of ABCA1 levels in patient-derived iRPEs under basal conditions. Actin was detected as loading control. ABCA1 expression was quantified & normalized to actin. (D,E) Relative expression of ABCG1 (D) & NR1H3 (E) mRNA in patient-derived iRPEs under basal conditions normalized to RPL28 & decreased risk group. (F) Cholesterol efflux in patient-derived iRPEs after direct cell labeling & in the presence of ApoAI. (G) Cholesterol efflux in patient-derived iRPEs after phagocytosis of BODIPY-cholesterol-loaded POSs & in the presence of ApoAI. (H) Quantification of phagocytosed POSs per nuclei in patient-derived iRPEs. Values shown are means ± SD (n = 3). * p < 0.05; *** p < 0.001. Unpaired Student’s t-test. (I) Representative fluorescence microscopy images of phagocytosed FITC-labeled POSs (green) & staining for ZO-1 (red) & DAPI (blue) of increased risk cell line IPS19-00096. Scale bar = 100 μm. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35328615), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-105_rabbit-polyclonal-abca1-antibody-310202416171459.jpg)
![Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - A–C) Effects of 6‐dihydroparadol & specific proteasomal, lysosomal, & calpain inhibitors on the ABCA1 protein levels. THP‐1 cells were differentiated as described in Figure 2, & then loaded with unlabeled cholesterol for 24 h. Cells were treated with or without 6‐dihydroparadol (6‐DP, 30 μm) for 24 h & incubated for another 3 h with or without the proteasome inhibitor lactacystin (10 μm), the lysosomal inhibitor chloroquine (100 μm), or the calpain inhibitor calpeptin (30 μg mL−1). The ABCA1 protein levels were detected by Western blot analysis. The bar graphs represent mean ± SD from three independent experiments. *p < 0.05, **p < 0.01, & ***p < 0.001 versus control; n.s., not significant versus control (determined by Student's t‐test or ANOVA with Bonferroni's post hoc test). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29802792), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-105_rabbit-polyclonal-abca1-antibody-310202416165615.jpg)
![Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - Suppressive effects of Ucn1 on foam cell formation & related protein expression in human monocyte-derived macrophages.Human monocytes were incubated for 7 days with RPMI-1640 supplemented with 10% human serum & the indicated concentrations of Ucn1, followed by a 19 h-incubation with 50 µg/ml oxLDL in the presence of 0.1 mmol/l [3H]oleate. Intracellular CE accumulation was determined from the radioactivity of cholesterol-[3H]oleate. Otherwise, before the addition of oxLDL, cells were harvested & subjected to immunoblotting analyses for CD36, ACAT1, or ABCA1. beta -Actin served as a loading control. Data are expressed as means ± SEM from 4–6 independent experiments with monocytes from 4–6 different donors. Baseline (1 fold) = 8.4±2.2 nmol/mg cell protein. *P<0.05, †P<0.001 vs. 0 nmol/l of Ucn1. Image collected & cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0110866), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-105_rabbit-polyclonal-abca1-antibody-310202416182616.jpg)
![Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - Effect of evodiamine on ABCA1 transcription & the degradation rate of ABCA1 protein. (a) Differentiated THP-1 macrophages were incubated with 10 μM evodiamine or 10 μM pioglitazone as positive control for 24 h. Total RNA was extracted & ABCA1 mRNA expression levels were quantified by qRT-PCR. (b) 293 T cells were transfected with a luciferase reporter construct driven by the human ABCA1 promoter as described in the Materials & Methods section. After transfection, cells were treated with 10 μM Evodiamine or 1 μM T0901317 as positive control for 24 h. (c) Differentiated THP-1 macrophages were incubated for 24 h with (black circle) or without (Veh; white circle) evodiamine (10 μM) & lysed after addition of cycloheximide (CHX; 140 μM) at different time points (0, 10, 20, 40 min). Western blot analysis shows the decline of ABCA1 protein level with cycloheximide in the presence & absence of evodiamine. All data are means ± S.D. (n = 3) vs. solvent vehicle control (DMSO), *p < 0.05, **p < 0.01, n.s. no significance (ANOVA/Bonferroni). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30038271), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-105_rabbit-polyclonal-abca1-antibody-310202416173512.jpg)
![Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - miR-33 deficiency improved cholesterol efflux in macrophages. A, Quantitative real-time PCR analysis of Abca1 & Abcg1 in macrophages from miR-33+/+Apoe−/− & miR-33−/−Apoe−/− mice. Values from miR-33+/+Apoe−/− were set at 100%. Values are mean±SE (n=7 each); ***P<0.001. B, Western blotting analysis of ABCA1 & ABCG1 in thioglycollate-elicited peritoneal macrophages from miR-33+/+Apoe−/− & miR-33−/−Apoe−/− mice. GAPDH was used as a loading control. C, Cholesterol efflux from thioglycollate-elicited peritoneal macrophages in the presence or absence of apoA-I (5 or 10 μg/mL). Values are mean±SE (n=6 each); **P<0.01. D, Cholesterol efflux from thioglycollate-elicited peritoneal macrophages in the presence or absence of HDL-C (50 or 100 μg/mL). Values are mean±SE (n=6 each); **P<0.01. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/23316322), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-105_rabbit-polyclonal-abca1-antibody-31020241616047.jpg)
![Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - A–C) Effects of 6‐dihydroparadol & specific proteasomal, lysosomal, & calpain inhibitors on the ABCA1 protein levels. THP‐1 cells were differentiated as described in Figure 2, & then loaded with unlabeled cholesterol for 24 h. Cells were treated with or without 6‐dihydroparadol (6‐DP, 30 μm) for 24 h & incubated for another 3 h with or without the proteasome inhibitor lactacystin (10 μm), the lysosomal inhibitor chloroquine (100 μm), or the calpain inhibitor calpeptin (30 μg mL−1). The ABCA1 protein levels were detected by Western blot analysis. The bar graphs represent mean ± SD from three independent experiments. *p < 0.05, **p < 0.01, & ***p < 0.001 versus control; n.s., not significant versus control (determined by Student's t‐test or ANOVA with Bonferroni's post hoc test). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29802792), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-105_rabbit-polyclonal-abca1-antibody-310202416165626.jpg)
![Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - Srebf1 is a miR-33 target gene.(a) Relative changes in lipid metabolism-related genes in the livers of miR-33−/− mice compared with miR-33+/+ mice fed NC at 16 weeks of age. (n=5–8 each,*P<0.05 in Student’s t-test). (b) Conservation of miR-33 target regions in the 3′UTR of Srebf1. Underlined sequences are the potential binding site of miR-33 seed sequences. * indicates the conservation among spieces. (c) 3′UTR reporter assay used to verify the target. Luciferase reporter activity of human & mouse SREBP-1 gene 3′UTR constructs in 293T cells overexpressing miR-control (miR-Con) & miR-33 (n=4 each, *P<0.05 & ***P<0.001 in Student’s t-test). (d) miR-33 dose-dependent changes in luciferase reporter activity of mouse Srebf1 3′UTR construct in 293T cells. miR-Con & miR-146a is used as a negative control (n=4 each, *P<0.05 & ***P<0.001 in one-way analysis of valiance test). (e) Luciferase reporter activity of the WT or mutant Srebf1 3′UTR at the potential miR-33 binding site in 293T cells (n=4 each, **P<0.01 in Student’s t-test). (f,g) Luciferase reporter activity of SRE-promoter (f) or FAS-promoter (g) in 293T cells. 293T cells were co-transfected with mouse Srebf1 with the full-length 3′UTR or without the 3′UTR, along with expression plasmids for miR-negative control, or miR-33. Values are the mean±s.e. (n=4 each, **P<0.01 versus miR-Con. ***P<0.001 versus miR-Con in one-way analysis of valiance test). (h) Western blotting analysis of SREBP-1, ABCA1, & IRS-2 in miR-33 transduced HepG2 cells & primary hepatocytes & hepatocytes prepared from miR-33+/+ & miR-33−/− mice. Representative western blot images are shown (n=4). Values are the means±s.e.m. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/24300912), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-105_rabbit-polyclonal-abca1-antibody-310202416165627.jpg)
![Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - (A) Chemical structure, (B) cytotoxicity of alpha -asarone, (C) enhancement of cholesterol efflux by alpha -asarone, (D & E) upregulation of ABCA1 & ABCG1 by alpha -asarone & beta -asarone, & (F) elevation of retinoid X receptor (RXR) alpha transcription. J774A.1 murine macrophages were exposed to 50 μg/ml oxidized low-density lipoprotein (LDL) & treated with 1–10 μM purple Perilla frutescens extracts (PPE)-alpha -asarone & 5–10 μM beta -asarone. (B) MTT assay was performed for the measurement of alpha -asarone toxicity. Graph data represent 1 of 4 independent experiments with multiple estimations. Values are expressed as the percentage cell survival relative to the untreated control cells (cell viability, 100%). (C) Cholesterol efflux was expressed as the percentage fluorescence in the medium relative to total fluorescence. (D & E) For the measurement of ABCA1 & ABCG1 expression, total cell lysates were subjected to western blot analysis with a primary antibody against ABCG1 or ABCG1. beta -actin was used as an internal control. Bar graphs (means ± SEM, n=3) represent quantitative densitometric results of the upper bands. Bar graphs denoted without a common letter indicate significant difference, P<0.05. (F) RXR alpha mRNA expression was measured by RT-PCR. GAPDH was used as a housekeeping gene for the co-amplification with RXR alpha . Image collected & cropped by CiteAb from the following publication (//www.spandidos-publications.com/10.3892/ijmm.2015.2101), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-105_rabbit-polyclonal-abca1-antibody-310202416161846.jpg)
![Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - Bilirubin significantly decreases expression of ATP‐binding cassette transporter A1 (ABCA1) protein in THP‐1 macrophages treated with LXR agonist (TO901317) to upregulate ABCA1 protein. THP‐1 cells were differentiated for 72 hours with 200 nmol/L phorbol‐12‐myristate‐13‐acetate & then loaded with unlabeled cholesterol for another 24 hours. Cells were treated with TO901317 (5 μmol/L) or solvent vehicle (0.1% dimethyl sulfoxide [DMSO]) for 24 hours. Afterward, cells were treated with bilirubin (17.1 μmol/L) or solvent vehicle (0.1% DMSO) for 16 hours. The protein levels of ABCA1 were detected by western blot analysis. The bar graphs present mean±SD from 3 independent experiments. ***P<0.001 vs control (determined by ANOVA with Bonferroni post hoc test). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28455345), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-105_rabbit-polyclonal-abca1-antibody-310202416175272.jpg)
![Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - Induction of cholesterol efflux attenuates the enhancement in HIV-1infectivity in NPCD55 cells. (A) Normal & NPCD55 cells were treated with 5 μM TO-901317 at 24 h post-infection & cultured for 72 h in the presence of the compound. At 96 h post-infection the cells were harvested & ABCA1, Gag, & beta -actin expression was detected by Western blotting analysis. All samples were loaded on the same gel. (B) AmplexRed assay was performed to measure free cholesterol content of untreated (filled) & TO-901317-treated (slashed) cells. Cholesterol content was normalized to protein concentration. (C) AmplexRed assay was performed to measure virion-associated cholesterol from purified virus produced in untreated (filled) & TO-901317-treated (slashed) infected cells. Virion-associated cholesterol content was normalized to p24 concentration. (D) TZM-bl reporter assay was performed to measure virus infectivity when cholesterol efflux was induced via TO-901317 stimulation. The ρ values were calculated by performing student T-test (*denotes < 0.05). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/22273177), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-105_rabbit-polyclonal-abca1-antibody-31020241617529.jpg)
![Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - Effects of apabetalone on ABCA1 expression & carboplatin response in ovarian cancer cells. (A) Apabetalone treatment reduced expression of ABCA1 in OVCAR-5 & OVCAR-5 CBPR cell lines. Cells were treated for 72 h with control medium (DMSO) or apabetalone (80 µM). Protein extracts from OVCAR-5 (~30 µg) were electrophoresed & immunoblotted with rabbit polyclonal ABCA1 antibody (1/1000, NB400-105, Novus Biological) & beta -actin (1/2000, Abcam) was used as a loading control. (B) Quantification of Western blot. OVCAR-5 (C), CaOV3 (D), OVCAR-5 CBPR (E) & CaOV3 CBPR (F) cell survival following treatment with carboplatin (CBP) alone (0-200 µM, black line) & in combination with apabetalone (Apa, 80 µM, purple line). (G) Carboplatin IC50 for OVCAR-5 & OVCAR-5 CBPR cells ± apabetalone. Data are mean ± SEM from three independent experiments. *P < 0.05, Student’s t-test. (H) Carboplatin IC50 for CaOV3 & CaOV3 CBPR cells ± apabetalone. Data are mean ± SEM from three independent experiments. P < 0.05, Student’s t-test. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35582032), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-105_rabbit-polyclonal-abca1-antibody-310202416161826.jpg)
![Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - Expression of ATP‐binding cassette transporter A1 (ABCA1) protein in THP‐1 macrophages treated with bilirubin & in peripheral blood mononuclear cells (PBMCs) from Gilbert syndrome (GS) patients. A, Bilirubin suppresses the expression of ABCA1 protein in THP‐1‐derived macrophages time‐dependently. THP‐1 cells were differentiated as described in Figure 1 & then loaded with unlabeled cholesterol for another 24 hours. Cells were treated with bilirubin (17.1 μmol/L) for 4, 8, 16, & 24 hours. The protein levels of ABCA1 were detected by western blotting. Control was treated with solvent vehicle (0.1% dimethyl sulfoxide). The bar graph presents mean±SD from 3 independent experiments. B, Expression of ABCA1 protein is decreased in PBMCs from participants with high bilirubin blood levels (GS) compared with healthy controls. The protein levels of ABCA1 were detected by western blotting. The bar graph presents mean±SEM (n=28 per group). *P<0.05, **P<0.01 & ***P<0.001 vs control. ns indicates not significant (determined by Student t test). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/28455345), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-105_rabbit-polyclonal-abca1-antibody-31020241616374.jpg)
![Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - (A) Time course response of ABCA1 induction by pioglitazone, & (B) enhancement of ABCA1 & (C) peroxisome proliferator-activated receptor gamma (PPAR gamma ) by purple Perilla frutescens extracts (PPE). J774A.1 murine macrophages were incubated with 10 μM pioglitazone & 50 μg/ml oxidized low-density lipoprotein (LDL) in the absence or presence of 1–10 μg/ml PPE. For the measurement of expression of (A & B) ABCA1 & (C) PPAR gamma , total cell lysates were subjected to western blot analysis with a primary antibody against ABCA1 or PPAR gamma . beta -actin was used as an internal control. Bar graphs (means ± SEM, n=3) represent quantitative densitometric results of the upper bands. Bar graphs denoted without a common letter indicate significant difference, P<0.05. Image collected & cropped by CiteAb from the following publication (//www.spandidos-publications.com/10.3892/ijmm.2015.2101), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-105_rabbit-polyclonal-abca1-antibody-3102024161896.jpg)
![Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - LXR agonist-stimulated ABCA1 expression & function in patient-derived iRPEs. Patient-derived iRPE lines were stimulated for 16 h with LXR agonist & are relative to unstimulated cells shown in Figure 2. (A) Expression of ABCA1 mRNA normalized to RPL28 & relative to unstimulated cells shown in Figure 2B. (B) Western blot analysis of ABCA1 protein levels. Actin was detected as loading control. ABCA1 expression was quantified & normalized to actin. (C) Cholesterol efflux assay after direct cell labeling & in the presence of ApoAI. (D) Cholesterol efflux assay after phagocytosis of BODIPY-cholesterol-loaded POSs & in the presence of ApoAI. Data are relative to unstimulated cells shown in Figure 2F,G, respectively. Data are presented as means ± SD (n = 3). Unpaired Student’s t-test. * p < 0.05. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35328615), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-105_rabbit-polyclonal-abca1-antibody-310202416171457.jpg)
![Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - Akt inhibition by LY294002 or Akt1/2 also enhances cholesterol efflux to apoA-I from ABCA1-expressing BHK cells.A) BHK cells were induced as in Fig. 1 & then incubated with LY294002 (200 µM) for 2 h. Cells were then lysed & analysed for ABCA1, phosphorylated Akt (p-Akt) & total Akt by Western-blotting. Hsp70 was also blotted as loading control. B & C) BHK cells were labeled with [3H] cholesterol & induced with 10 nM mifepristone overnight. Cholesterol efflux was measured after 2 h incubation with BSA (1 mg/ml) or BSA plus apoA-I (5 µg/ml). Some of cells were also incubated with indicated doses of LY294002 (B) or Akt1/2 (C), in addition to apoA-I, during 2 h efflux period. Results are presented as the average of triplicate wells with standard deviation & representative of more than three independent experiments. *** P<0.0001, **P<0.001 & *P<0.05 vs apoA-I only. Image collected & cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0113789), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-105_rabbit-polyclonal-abca1-antibody-310202416163770.jpg)
![Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - Generation, differentiation & analysis of ABCA1-deficient iRPEs. (A) Immunofluorescence staining for ZO-1 (red) in 4-week cultured iRPEs. Nuclei were stained with DAPI (blue). Scale bar = 100 μm. (B) Bright-field microscopy of iRPEs. (C) Ct values of RPE marker genes BEST1, OTX2, RLBP1 & RPE65 in iRPEs & parental iPSCs obtained by qPCR. Values shown are means ± SD (n = 3). Unpaired Student’s t-test. **** p < 0.0001. (D) Sequence alignment of parts of exon 14 (top) & exon 46 (bottom) of ABCA1-deficient iRPE cell clones & parental line. (E) Western blot of ABCA1 protein levels in ABCA1-deficient iRPE cell lines & parental cell line after 16 h of stimulation with 1 μM LXR agonist. Actin was detected as loading control. (F) Relative expression of ABCA1 mRNA in ABCA1-deficient iRPE cell lines & parental cell line normalized to ACTB. Values shown are means ± SD (n = 3). One-way ANOVA with Tukey’s post hoc test. **** p < 0.0001. (G) Relative expression of ABCG1 mRNA in ABCA1-deficient iRPE cell lines & parental cell line normalized to ACTB. Values shown are means ± SD (n = 3). One-way ANOVA with Tukey’s post hoc test. ** p < 0.01; *** p < 0.001. (H) Cholesterol efflux assay in iRPEs in the presence of ApoAI and/or LXR agonist (LXR ag). Values shown are means ± SD (n = 3). Two-way ANOVA with Bonferroni post hoc test vs. DMSO + BSA control. **** p < 0.0001. (I) Bright-field (BF) microscopy & Nile Red fluorescence microscopy (overview & close-up view marked with white squares) of 4-week cultured ABCA1-deficient iRPE cell lines & parental cell line. Relative fluorescence was quantified & is shown as mean ± SD (n = 8). One-way ANOVA with Tukey’s post hoc test. * p < 0.05, **** p < 0.0001. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35328615), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-105_rabbit-polyclonal-abca1-antibody-310202416173523.jpg)
![Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - Akt inhibition enhances cholesterol efflux to apoA-I from wt MEFs, but not from TSC2-/- MEFs where mTORC1 is constitutively activated.A) Mouse embryonic fibroblasts (MEFs), wt & TSC2-/-, were induced overnight with T0901317 (10 µM). Cell lysates were collected for Western blotting for phosphorylated S6K & total S6K. B) wt & TSC2-/- MEFs were incubated with or without T0901317 (10 µM) overnight. Some of cells were then incubated with apoA-I (10 µg/ml) or apoA-I plus DEBC (25 µM) for 2 h. The expression of ABCA1, phosphorylated Akt, total Akt & loading control hsp70 were analyzed by Western blotting. C) wt & TSC2-/- were labeled with [3H] cholesterol for 1 day & then incubated with or without T0901317 (10 µM) overnight. Some of cells were then incubated with apoA-I (10 µg/ml) or apoA-I plus DEBC (25 µM) for 2 h to analyze cholesterol efflux. Data presented as the average of triplicate wells with standard deviation & representative of at least three independent experiments. *** P<0.0001 vs apoA-I only. Image collected & cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0113789), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-105_rabbit-polyclonal-abca1-antibody-310202416163724.jpg)
![Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - Akt inhibition by DEBC enhances cholesterol efflux to apoA-I specifically from ABCA1-expressing BHK cells.A) BHK-ABCA1 cells were induced with mifepristone (10 nM) overnight & then incubated with indicated doses of DEBC for 2 h. Cells were then lysed & Western-blotted for ABCA1, phosphorylated Akt (p-Akt) & total Akt. Hsp70 was also blotted as loading control. B) BHK-ABCA1 cells were labeled with [3H] cholesterol & induced overnight as above. After 2 h incubation with BSA (1 mg/ml) or BSA plus apoA-I (5 µg/ml), cholesterol efflux was measured as described in the Methods section. Some of the cells were also incubated with indicated doses of DEBC, in addition to apoA-I, during 2 h efflux period. C) BHK-ABCA1 & BHK-A937V cells were induced with mifepristone (10 nM) overnight. 2 h Cholesterol efflux was measured as above either with or without DEBC (25 µM). Results are presented as the average of triplicate wells with standard deviation & representative of more than three independent experiments. *** P<0.0001 & **P<0.001 vs apoA-I only. Image collected & cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0113789), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-105_rabbit-polyclonal-abca1-antibody-310202416175212.jpg)
![Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - LXRs control expression of genes involved in cholesterol homeostasis & fatty acid synthesis in MPECs.(A) qPCR analysis of Abca1, Abcg1 & Idol levels in WT (+/+) & Lxr alpha beta −/− (lxr−/−) MPECs after DMSO (vehicle) or T0901317 stimulation (B) Effect of 9-cis retinoic acid and/or T0901317 stimulation on Abca1 accumulation levels in WT (+/+) & Lxr alpha beta −/− (lxr−/−) MPECs (C) qPCR analysis of Srebp1, Acc, & Fas levels in WT (+/+) & Lxr alpha beta −/− (lxr−/−) MPECs after DMSO (vehicle) or T0901317 stimulation. (qPCR analysis results from 4 independant experiments & was normalized using 36b4 gene). *p<0.05, **p<0.01, ***p<0.001 in Student’s t test. Error bars represent mean ± SEM. (D) Western blot analysis was performed on WT (+/+) or Lxr alpha beta −/− MPECs using Srebp1c, Abca1 & beta -Actin antibodies. (E) Oil-Red O staining (ORO) & Normarski/Dapi of WT (+/+) & Lxr alpha beta −/− MPECs, or WT MEFs, treated for 48h with DMSO (vehicle) or T0901317 (1 µM). Head arrows indicate lipid droplets. Scale bars 100 µm. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/23554947), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-105_rabbit-polyclonal-abca1-antibody-31020241616059.jpg)
![Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - (A) Time course response of ABCA1 induction by pioglitazone, & (B) enhancement of ABCA1 & (C) peroxisome proliferator-activated receptor gamma (PPAR gamma ) by purple Perilla frutescens extracts (PPE). J774A.1 murine macrophages were incubated with 10 μM pioglitazone & 50 μg/ml oxidized low-density lipoprotein (LDL) in the absence or presence of 1–10 μg/ml PPE. For the measurement of expression of (A & B) ABCA1 & (C) PPAR gamma , total cell lysates were subjected to western blot analysis with a primary antibody against ABCA1 or PPAR gamma . beta -actin was used as an internal control. Bar graphs (means ± SEM, n=3) represent quantitative densitometric results of the upper bands. Bar graphs denoted without a common letter indicate significant difference, P<0.05. Image collected & cropped by CiteAb from the following publication (//www.spandidos-publications.com/10.3892/ijmm.2015.2101), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-105_rabbit-polyclonal-abca1-antibody-310202416171495.jpg)
![Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - Anti-ApoA-1 IgGs upregulate ABCA1. ABCA1 was increased after 16 & 24 h of anti-ApoA-1 IgG exposure to HMDM at the mRNA level as revealed by RT-PCR (a) as well as at the protein level after 24 h anti-apoA-1 IgG stimulation, as revealed by Western blot analysis (b). In panel a, data are expressed as fold change expression of the mean ± SD of ABCA1 calculated by delta delta CT method of six independent experiments (n = 6) & values were normalized to untreated condition. p-values were calculated using the Student’s t-test: * p < 0.05, ** p < 0.01, **** p < 0.0001. (b) One of four representative Western blots is shown. Data are the mean ± SD of band intensity volume/actin intensity volume of four independent experiments (n = 4). p-values were calculated using the Student’s t-test: * p = 0.02, ** p = 0.005. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31766415), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-105_rabbit-polyclonal-abca1-antibody-31020241616076.jpg)
![Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - A–C) Effects of 6‐dihydroparadol & specific proteasomal, lysosomal, & calpain inhibitors on the ABCA1 protein levels. THP‐1 cells were differentiated as described in Figure 2, & then loaded with unlabeled cholesterol for 24 h. Cells were treated with or without 6‐dihydroparadol (6‐DP, 30 μm) for 24 h & incubated for another 3 h with or without the proteasome inhibitor lactacystin (10 μm), the lysosomal inhibitor chloroquine (100 μm), or the calpain inhibitor calpeptin (30 μg mL−1). The ABCA1 protein levels were detected by Western blot analysis. The bar graphs represent mean ± SD from three independent experiments. *p < 0.05, **p < 0.01, & ***p < 0.001 versus control; n.s., not significant versus control (determined by Student's t‐test or ANOVA with Bonferroni's post hoc test). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29802792), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-105_rabbit-polyclonal-abca1-antibody-31020241618917.jpg)
![Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - ABCA1 protein expression is upregulated in ovarian cancer cells with acquired carboplatin resistance. ABCA1 expression in OVCAR-5 (A) & CaOV3 (C) & carboplatin resistant OVCAR-5 CBPR (B) & CaOV3 CBPR (D) by immunocytochemistry using rabbit polyclonal ABCA1 antibody (1/100, NB400-105, Novus Biological). (E) OVCAR-5 cells with Rabbit IgG & (F) CaOV3 cells with Rabbit IgG. (G) Protein extracts from OVCAR-5 (~30 µg) & CaOV3 cell lines (~60 µg) were electrophoresed & immunoblotted with rabbit polyclonal ABCA1 antibody (1/1000, NB400-105, Novus Biological), & beta -actin (1/2000, Abcam) was used as a loading control. A major band was detected at ~250 kDa, which is the predicted size for ABCA1. (H) Quantitation of ABCA1 Western blots. Data are from 2-4 independent experiments. Statistical significance was determined using the Student’s t-test, *P < 0.05. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35582032), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-105_rabbit-polyclonal-abca1-antibody-310202416171478.jpg)
![Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - Evodiamine enhances apo A1-mediated ChE from THP-1 macrophages & increases ABCA1 protein level. (a) Differentiated THP-1 cells were loaded with [3H]-cholesterol together with the indicated treatments for 24 h. On the next day, the cells were washed twice with PBS & incubated with the same compounds [solvent vehicle control (Veh; ≤0.1% DMSO), evodiamine (1–20 μM), & the PPAR gamma agonist pioglitazone (10 μM) as positive control] with or without 10 µg/mL apo A1. Extracellular as well as intracellular radioactivities were quantified with scintillation counter. Differentiated THP-1-derived macrophages were treated with solvent vehicle control (Veh; ≤0.1% DMSO), evodiamine (10 μM), & the PPAR gamma agonist pioglitazone (10 μM) as positive control. After 24 h incubation, the cells were lysed & 20 μg protein was resolved via SDS-PAGE. Immunodetection was performed with antibodies against the indicated proteins, ABCA1 (b), ABCG1 (c), & SR-B1 (d), & visualized by chemiluminescence detection. All experiments were performed at least three times & data are presented as means ± S.D. vs. solvent vehicle control, *p < 0.05, **p < 0.01, ***p < 0.001, n.s. no significance (ANOVA/Bonferroni). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30038271), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-105_rabbit-polyclonal-abca1-antibody-310202416161816.jpg)
![Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - A–C) Effects of 6‐dihydroparadol & specific proteasomal, lysosomal, & calpain inhibitors on the ABCA1 protein levels. THP‐1 cells were differentiated as described in Figure 2, & then loaded with unlabeled cholesterol for 24 h. Cells were treated with or without 6‐dihydroparadol (6‐DP, 30 μm) for 24 h & incubated for another 3 h with or without the proteasome inhibitor lactacystin (10 μm), the lysosomal inhibitor chloroquine (100 μm), or the calpain inhibitor calpeptin (30 μg mL−1). The ABCA1 protein levels were detected by Western blot analysis. The bar graphs represent mean ± SD from three independent experiments. *p < 0.05, **p < 0.01, & ***p < 0.001 versus control; n.s., not significant versus control (determined by Student's t‐test or ANOVA with Bonferroni's post hoc test). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29802792), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-105_rabbit-polyclonal-abca1-antibody-310202416161840.jpg)
![Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - Functional miR-33 responsive elements in the 3′UTR of ATP8B1 & ABCB11A,B. Conserved sequences in the 3′UTR of ATP8B1 & ABCB11 are partially complementary to miR-33. The element in human ATP8B1 is located 1877–1897 nt after the stop codon. The element in ABCB11 overlaps the stop codon in primates, while rodents show a conserved sequence 732–751 nt after the stop codon.C,D. Luciferase assays in HEK293 cells using the whole 3′UTR of human or murine ATP8B1 & ABCB11, or a single copy of the responsive elements (RE) identified above, or mutant responsive elements (RE*; where AATGCA was mutated to GGGTTG to prevent complementarity to the seed sequence of the miRNA), co-transfected with (closed bars) or without (open bars) a vector to overexpress miR-33. In grey, data from empty (negative control) & R33 (positive control containing a 100% match to miR-33) reporter vectors.E,F. Relative mRNA expression of canalicular transporters in primary murine hepatocytes (n = 4 dishes/condition) & human HuH-7 hepatoma cells (n = 3 dishes/condition) transduced 48 h with empty or miR-33 adenovirus.G. Relative protein levels in HuH7 cells transduced with empty or miR-33 adenovirus. Some cells were incubated for 16 h in the presence of FXR:RXR agonists (2 µmol/L GW4064 : 1 µmol/L 9-cis-retinoic acid) to induce ABCB11. Asterisk indicates a non-specific band. Data shown as mean ± SD; **p < 0.01. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/22767443), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-105_rabbit-polyclonal-abca1-antibody-31020241616034.jpg)
![Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - (A) Chemical structure, (B) cytotoxicity of alpha -asarone, (C) enhancement of cholesterol efflux by alpha -asarone, (D & E) upregulation of ABCA1 & ABCG1 by alpha -asarone & beta -asarone, & (F) elevation of retinoid X receptor (RXR) alpha transcription. J774A.1 murine macrophages were exposed to 50 μg/ml oxidized low-density lipoprotein (LDL) & treated with 1–10 μM purple Perilla frutescens extracts (PPE)-alpha -asarone & 5–10 μM beta -asarone. (B) MTT assay was performed for the measurement of alpha -asarone toxicity. Graph data represent 1 of 4 independent experiments with multiple estimations. Values are expressed as the percentage cell survival relative to the untreated control cells (cell viability, 100%). (C) Cholesterol efflux was expressed as the percentage fluorescence in the medium relative to total fluorescence. (D & E) For the measurement of ABCA1 & ABCG1 expression, total cell lysates were subjected to western blot analysis with a primary antibody against ABCG1 or ABCG1. beta -actin was used as an internal control. Bar graphs (means ± SEM, n=3) represent quantitative densitometric results of the upper bands. Bar graphs denoted without a common letter indicate significant difference, P<0.05. (F) RXR alpha mRNA expression was measured by RT-PCR. GAPDH was used as a housekeeping gene for the co-amplification with RXR alpha . Image collected & cropped by CiteAb from the following publication (//www.spandidos-publications.com/10.3892/ijmm.2015.2101), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-105_rabbit-polyclonal-abca1-antibody-310202416175262.jpg)
![Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - Gas6 treatment enhances expression of LXR alpha & LXR beta & their target genes in BMDM.Mouse BMDM were stimulated with 400 ng/ml Gas6, 1 μM T0901317, 10 ng/ml interferon (IFN)-gamma , 10 ng/ml IL-4, or 100 ng/ml LPS for 4 h (a,b) or 400 ng/ml Gas6 for the indicated times (c–g). (a,b,e) The amounts of the LXR alpha , LXR beta , ABCA1, ABCG1, ApoE, AIM, Arg2, VEGF, YM1, & Arg1 mRNAs were analyzed by real-time PCR & normalized to that of Hprt mRNA. (c,d,f,g) The relative abundances of LXR alpha , LXR beta , ABCA1, ABCG1, ApoE, Aim, Arg2, & VEGF proteins were determined by Western blotting analysis. The relative densitometric intensity was determined for each band & normalized to beta -actin. Data in all bar graphs are means ± SEM of three independent experiments. *P < 0.05 compared with control. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/27406916), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-105_rabbit-polyclonal-abca1-antibody-310202416175244.jpg)
![Western Blot: ABCA1 Antibody - BSA Free [NB400-105] - (A) Time course response of ABCA1 induction by TO-091317 & (B) upregulation of ABCA1 by purple Perilla frutescens extracts (PPE), & (C) enhancement of liver X receptor (LXR) alpha induction by PPE. J774A.1 murine macrophages were cultured with 1 μM TO-091317 or 50 μg/ml Cu2+-oxidized low-density lipoprotein (LDL) in the absence or presence of 1–10 μg/ml PPE. For the measurement of expression of (A & B) ABCA1 & (C) LXR alpha , total cell lysates were subjected to western blot analysis with a primary antibody against ABCA1 or LXR alpha . beta -actin was used as an internal control. Bar graphs (means ± SEM, n=3) represent quantitative densitometric results of the upper bands. Bar graphs denoted without a common letter indicate significant difference, P<0.05. Image collected & cropped by CiteAb from the following publication (//www.spandidos-publications.com/10.3892/ijmm.2015.2101), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-105_rabbit-polyclonal-abca1-antibody-31020241616565.jpg)
![Western Blot: ABCG1 Antibody - BSA Free [NB400-132] - ABCG-1 protein level in control and glycolaldehyde-treated macrophages. J774 macrophages were overloaded with oxidized LDL (50 ug/mL de DMEM) for 48 h. In the last 5h, cells were incubated with 0.25 mM glycolaldehyde (GAD; black bars) and 1 uM LXR agonist (T0901317). Control cells (C; gray bars) were incubated with T0901317 alone. Cells were scrapped into TBS containing protease inhibitors. Equal amounts of cell protein were applied into a 6% polyacrylamide electrophoresis gel and immunoblot was performed utilizing anti ABCG-1 antibody. Data (arbitrary units; n = 4) were corrected per beta-actin. Image collected and cropped by CiteAb from the following publication (//lipidworld.biomedcentral.com/articles/10.1186/1476-511X-10-172), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/ABCG1-Antibody---BSA-Free-Western-Blot-NB400-132-img0016.jpg "Western Blot: ABCG1 Antibody - BSA Free [NB400-132] - ABCG-1 protein level in control and glycolaldehyde-treated macrophages. J774 macrophages were overloaded with oxidized LDL (50 ug/mL de DMEM) for 48 h. In the last 5h, cells were incubated with 0.25 mM glycolaldehyde (GAD; black bars) and 1 uM LXR agonist (T0901317). Control cells (C; gray bars) were incubated with T0901317 alone. Cells were scrapped into TBS containing protease inhibitors. Equal amounts of cell protein were applied into a 6% polyacrylamide electrophoresis gel and immunoblot was performed utilizing anti ABCG-1 antibody. Data (arbitrary units; n = 4) were corrected per beta-actin. Image collected and cropped by CiteAb from the following publication (//lipidworld.biomedcentral.com/articles/10.1186/1476-511X-10-172), licensed under a CC-BY license.")
![Immunohistochemistry-Paraffin: ABCG1 Antibody - BSA Free [NB400-132] - Staining of human lung, alveolar macrophages.](http://images.novusbio.com/fullsize/ABCG1-Antibody---BSA-Free-Immunohistochemistry-Paraffin-NB400-132-img0013.jpg)
![Flow (Intracellular): ABCG1 Antibody - BSA Free [NB400-132] - RAW 246.7 cells were either untreated (A) or serum starved for 24 hours, and then treated with 1uM TO9 for 24 hours (B). An intracellular stain was performed with NB400-132 (blue) and a matched isotype control NB810-56910 (orange). Cells were fixed with 4% paraformaldehyde, following fixation, cells were permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 5 ug/mL for 30 minutes at room temperature, followed by Goat Anti-Rabbit Dylight 550-conjugated antibody.](http://images.novusbio.com/fullsize/ABCG1-Antibody-BSA-Free-Flow-Intracellular-NB400-132-img0012.jpg)
![<b>Biological Strategies Validation. </b>Western Blot: ABCG1 Antibody - BSA Free [NB400-132] - Cells were pretreated with 5 uM F12511 or 5 uM MG132 for 30 min and then exposed to 5 or 50 uM 24S-OHC for 6 h. Whole-cell lysates were immunoblotted with antibodies specific for ABCG1 or beta-actin. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/31285856/) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/ABCG1 Antibody - BSA Free-Western Blot-NB400-132-img0017.jpg)
![Western Blot: ABCG1 Antibody - BSA Free [NB400-132] - Detection of ABCG1 in J774 mouse macrophages. Image provided by Dr. Angeliki Chroni of the National Centre for Scientific Research Demokritos.](http://images.novusbio.com/fullsize/ABCG1-Antibody---BSA-Free-Western-Blot-NB400-132-img0005.jpg)
![Western Blot: ABCG1 Antibody - BSA Free [NB400-132] - Raw 264.7 (A), and Raw 264.7 + 10uM T09 18 hr (B) cell lysate using ABCG1 antibody at 2 ug/mL.](http://images.novusbio.com/fullsize/ABCG1-Antibody---BSA-Free-Western-Blot-NB400-132-img0009.jpg)
![Western Blot: ABCG1 Antibody - BSA Free [NB400-132] - Detection of ABCG1 in mouse peritoneal macrophages. Lane 1: untreated mouse peritoneal macrophages, Lane 2: 22-(R)-hydrocholesterol treated macrophages, Lane 3: T0901713 treated macrophages, Lane 4: T091713 treated macrophages.](http://images.novusbio.com/fullsize/ABCG1-Antibody---BSA-Free-Western-Blot-NB400-132-img0004.jpg)
![Western Blot: ABCG1 Antibody - BSA Free [NB400-132] - SAA has little impact on the impairment in biliary and fecal excretion of macrophage-derived 3H-cholesterol during endotoxemia. WT and SAAKO mice were injected subcutaneously with PBS or 0.8 ug/g LPS as indicated, followed 4 hr later by intraperitoneal injection of 3H-cholesterol-labeled J774 macrophages. ABCG1 in liver lysates (40 ug protein) was identified by immunoblotting and quantified by densitometry. Results from each of the 3 experiments (n = 4-5 per group per experiment) were expressed relative to PBS-injected WT mice after normalization to beta-actin. A representative western blot is shown. Image collected and cropped by CiteAb from the following publication (//www.hindawi.com/journals/jl/2013/283486/), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/ABCG1-Antibody---BSA-Free-Western-Blot-NB400-132-img0014.jpg)
![Western Blot: ABCG1 Antibody - BSA Free [NB400-132] - 6‐Dihydroparadol increases A) ABCA1 & B) ABCG1 protein stability. THP‐1 cells were differentiated as described in Figure 2. Then cells were loaded with unlabeled cholesterol & treated with 6‐dihydroparadol (10 μm), or solvent vehicle (0.1% DMSO, control) for 24 h. Cells were lysed at different time points (0, 1, 2, 3, 4, & 6 h) after treatment with the protein synthesis inhibitor cycloheximide (CHX, 100 μm). The protein levels of both ABCA1 & ABCG1 were detected by Western blot analysis. The data points represent mean ± SD from three independent experiments. *p < 0.05 & **p < 0.01 versus control at the same time point (determined by Student's t‐test). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/29802792), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-132_rabbit-polyclonal-abcg1-antibody-310202415291917.jpg)
![Western Blot: ABCG1 Antibody - BSA Free [NB400-132] - Evodiamine enhances apo A1-mediated ChE from THP-1 macrophages & increases ABCA1 protein level. (a) Differentiated THP-1 cells were loaded with [3H]-cholesterol together with the indicated treatments for 24 h. On the next day, the cells were washed twice with PBS & incubated with the same compounds [solvent vehicle control (Veh; ≤0.1% DMSO), evodiamine (1–20 μM), & the PPAR gamma agonist pioglitazone (10 μM) as positive control] with or without 10 µg/mL apo A1. Extracellular as well as intracellular radioactivities were quantified with scintillation counter. Differentiated THP-1-derived macrophages were treated with solvent vehicle control (Veh; ≤0.1% DMSO), evodiamine (10 μM), & the PPAR gamma agonist pioglitazone (10 μM) as positive control. After 24 h incubation, the cells were lysed & 20 μg protein was resolved via SDS-PAGE. Immunodetection was performed with antibodies against the indicated proteins, ABCA1 (b), ABCG1 (c), & SR-B1 (d), & visualized by chemiluminescence detection. All experiments were performed at least three times & data are presented as means ± S.D. vs. solvent vehicle control, *p < 0.05, **p < 0.01, ***p < 0.001, n.s. no significance (ANOVA/Bonferroni). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/30038271), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-132_rabbit-polyclonal-abcg1-antibody-31020241618932.jpg)
![Western Blot: Niemann-Pick C1 Antibody - BSA Free [NB400-148] - NPC proteins in mouse lungs. Western blot of wild type (W) littermates, NPC1 (Mut) or NPC2 (Mut) mutant mouse lungs using anti-NPC1 or -NPC2 antibody. beta-actin used as a loading control. 30 ug protein/lane. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0067084), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/Niemann-Pick-C1-Antibody---BSA-Free-Western-Blot-NB400-148-img0015.jpg "Western Blot: Niemann-Pick C1 Antibody - BSA Free [NB400-148] - NPC proteins in mouse lungs. Western blot of wild type (W) littermates, NPC1 (Mut) or NPC2 (Mut) mutant mouse lungs using anti-NPC1 or -NPC2 antibody. beta-actin used as a loading control. 30 ug protein/lane. Image collected and cropped by CiteAb from the following publication (//dx.plos.org/10.1371/journal.pone.0067084), licensed under a CC-BY license.")
![Immunocytochemistry/Immunofluorescence: Niemann-Pick C1 Antibody - BSA Free [NB400-148] - NPC1 antibody was tested in HeLa cells with DyLight 488 (green). Nuclei were counterstained with DAPI (blue).](http://images.novusbio.com/fullsize/Niemann-Pick-C1-Antibody---BSA-Free-Immunocytochemistry-Immunofluorescence-NB400-148-img0010.jpg)
![Immunohistochemistry-Paraffin: Niemann-Pick C1 Antibody - BSA Free [NB400-148] - Staining of human brain, cortex, neurons and astrocytes.](http://images.novusbio.com/fullsize/Niemann-Pick-C1-Antibody---BSA-Free-Immunohistochemistry-Paraffin-NB400-148-img0011.jpg)
![Western Blot: Niemann-Pick C1 Antibody - BSA Free [NB400-148] - Protein expression analysis of normal and NPC-deficient cells after HIV-1 infection. Cells were uninfected or infected with VSVG-HIV-1 and harvested 96 h post-infection. NPC2, NPC1, and beta-actin protein expression was detected via Western blotting in uninfected and infected cells. Gag expression was also detected in the infected cells. Image collected and cropped by CiteAb from the following publication (//virologyj.biomedcentral.com/articles/10.1186/1743-422X-9-31), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/Niemann-Pick-C1-Antibody---BSA-Free-Western-Blot-NB400-148-img0016.jpg)
![<b>Biological Strategies Validation. </b>Immunocytochemistry/Immunofluorescence: Niemann-Pick C1 Antibody - BSA Free [NB400-148] - Immunocytochemical staining with corresponding colocalization analysis of ALIX (green) and NPC-1 (red) in fibroblasts exposed to LLOMe for 15 min. Nuclei are stained with DAPI (blue) and merged images show colocalization in yellow (n = 5). Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32409651/) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/Niemann-Pick C1 Antibody - BSA Free-Immunocytochemistry-Immunofluorescence-NB400-148-img0017.jpg)
![<b>Genetic Strategies Validation. </b>Western Blot: Niemann-Pick C1 Antibody - BSA Free [NB400-148] - Western blot shows lysates of HeLa human cervical epithelial carcinoma parental cell line and NPC1 knockout (KO) HeLa cell line. PVDF membrane was probed with 1:1000 of Rabbit Anti-Human NPC1 Polyclonal Antibody (Catalog # NB400-148) followed by HRP-conjugated Anti-Rabbit IgG Secondary Antibody (Catalog #HAF008). Specific band was detected for NPC1 at approximately 240-260 kDa (as indicated) in the parental HeLa cell line, but is not detectable in the knockout HeLa cell line. This experiment was conducted under reducing conditions.](http://images.novusbio.com/fullsize/Niemann-Pick-C1-Antibody---BSA-Free-Knockout-Validated-NB400-148-img0014.jpg)
![<b>Genetic Strategies Validation. </b>Western Blot: Niemann-Pick C1 Antibody - BSA Free [NB400-148] - HeLa lysate, BHK lysate, A431 lysate tested at 1:1000. Image from verified customer review.](http://images.novusbio.com/fullsize/Niemann-Pick-C1-Antibody---BSA-Free-Knockdown-Validated-NB400-148-img0012.jpg)
![Immunocytochemistry/ Immunofluorescence: Niemann-Pick C1 Antibody - BSA Free [NB400-148] - ESCRT complex recruited to LLOMe-damaged lysosomes promotes cell survival.Human fibroblasts were exposed to 1 mM LLOMe & when indicated, the cell permeable calcium chelator BAPTA-AM (1 µM) was added 10 min prior to LLOMe exposure. Immunocytochemical staining with corresponding colocalization analysis of a CHMP4B (green) & LAMP2 (red), b ALIX (green) & NPC-1 (red), & c CHMP4B (green) & LAMP2 (red) in fibroblasts exposed to LLOMe for 15 min. Nuclei are stained with DAPI (blue) & merged images show colocalization in yellow (n = 5). d Caspase-3 like activity in cells exposed to LLOMe for 8 h (n = 3). e Quantification of apoptotic & necrotic cells using Annexin V/PI staining in fibroblasts exposed to LLOMe for 6 h (n = 3). f Immunoblot of LAMP2 in digitonin-extracted cytosolic fractions from cells exposed to LLOMe for 2 h (n = 8) with corresponding quantitative analysis. *p < 0.05, **p < 0.01 & ***p < 0.001 compared to control (a–b) or LLOMe only (c–f). Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32409651), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-148_rabbit-polyclonal-niemann-pick-c1-antibody-310202416165630.jpg)
![Western Blot: Niemann-Pick C1 Antibody - BSA Free [NB400-148] - Expression of proteins involved in extracellular lipid uptake & intracellular cholesterol trafficking following JQ1 (0.4 µM) administration to HepG2 cells for 48 hours. (A) Representative Western blot (left panel) & densitometric analysis (right panel) of SR-B1. n = 6 independent experiments. (B) Immunofluorescence analysis of SR-B1 (green). Nuclei were counterstained with DAPI. n = 3 different experiments. Scale bar: 50 µm. (C) Representative Western blot (left panel) & densitometric analysis (right panel) of LDLr. n = 5 independent experiments. (D) LDLr immunofluorescence (green). Nuclei were counterstained with DAPI. n = 3 different experiments. (E–F) Representative Western blots & densitometric analysis of NPC1 & TMEM97. Tubulin was chosen as loading control. n = 6 independent experiments. Data represent means ± SD. Statistical analysis was performed by using unpaired Student’s t test. ** p < 0.01; *** p < 0.001. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/32075110), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-148_rabbit-polyclonal-niemann-pick-c1-antibody-310202416163786.jpg)
![Western Blot: Niemann-Pick C1 Antibody - BSA Free [NB400-148] - Effects of p75NTR modulation by LM11A-31 on cholesterol metabolism & secretion. (A–D) Representative Western blot & densitometric analysis of HMGCR, ABCA1, NPC1, & ApoE in U373 cells treated with vehicle (Ctrl) & LM11A-31 (0.1 µM) for 48 h. n = 4 different experiments. Vinculin served as a housekeeping protein to normalize protein loading. (E) Quantification of ApoE amount (µg/mL) by ELISA assay in culture medium from vehicle- & LM11A-31-treated U373 cells. n = 3 different experiments. (F) Cholesterol quantification (total cholesterol, free cholesterol, & cholesteryl esters) in the culture medium of U373 cells treated with vehicle (Ctrl) & LM11A-31 (0.1 µM) for 48 h. n = 3 different experiments. Data represent means ± SD. Statistical analysis was carried out by using unpaired Student’s t test. *** p < 0.001. Image collected & cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/35563230), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-148_rabbit-polyclonal-niemann-pick-c1-antibody-31020241616058.jpg)
![Immunohistochemistry-Paraffin: Apolipoprotein E/ApoE Antibody (WUE-4) [NB110-60531] - ApoE was detected in immersion fixed paraffin-embedded sections of human liver using anti-human mouse monoclonal antibody (Catalog # NB110-60531) at 1:200 dilution overnight at 4C. Tissue was stained using the VisuCyte anti-mouse HRP polymer detection reagent (Catalog # VC001) 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/Apolipoprotein-E-ApoE-Antibody-WUE-4-Immunohistochemistry-Paraffin-NB110-60531-img0011.jpg "Immunohistochemistry-Paraffin: Apolipoprotein E/ApoE Antibody (WUE-4) [NB110-60531] - ApoE was detected in immersion fixed paraffin-embedded sections of human liver using anti-human mouse monoclonal antibody (Catalog # NB110-60531) at 1:200 dilution overnight at 4C. Tissue was stained using the VisuCyte anti-mouse HRP polymer detection reagent (Catalog # VC001) 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.")
![Western Blot: Apolipoprotein E/ApoE Antibody (WUE-4) [NB110-60531] - ApoE Antibody (WUE-4) [NB110-60531] - Detection of ApoE in human tissue lysate using NB110-60531. Lane 1: liver Lane 2: brain](http://images.novusbio.com/fullsize/Apolipoprotein-E-ApoE-Antibody-WUE-4-Western-Blot-NB110-60531-img0013.jpg)
![Flow Cytometry: Apolipoprotein E/ApoE Antibody (WUE-4) [NB110-60531] - ApoE Antibody (WUE-4) [NB110-60531] - Intracellular flow cytometric staining of 1 x 10^6 CHO (A) and HEK-293 (B) cells using ApoE antibody (dark blue). Isotype control shown in orange. An antibody concentration of 1 ug/1x10^6 cells was used.](http://images.novusbio.com/fullsize/Apolipoprotein-E-ApoE-Antibody-WUE-4-Flow-Cytometry-NB110-60531-img0014.jpg)
![Western Blot: Apolipoprotein E/ApoE Antibody (WUE-4) [NB110-60531] - 50 ug protein per lane for liver lysate and 0.5 ul of plasma at 9% SDS. Samples are loaded onto the gel as the following order: human liver lysate, mouse liver lysate, rat liver lysate, human plasma, and mouse plasma. Image from confirmed customer review.](http://images.novusbio.com/fullsize/Apolipoprotein-E-ApoE-Antibody-WUE-4-Western-Blot-NB110-60531-img0005.jpg)
![Immunocytochemistry/Immunofluorescence: Apolipoprotein E/ApoE Antibody (WUE-4) [NB110-60531] - HepG2 cells were fixed for 10 minutes using 10% formalin and then permeabilized for 5 minutes using 1X TBS + 0.5% Triton X-100. The cells were incubated with anti-ApoE (WUE-4) [NB110-60531] at a 1:200 dilution overnight at 4C and detected with an anti-mouse DyLight 488 (Green) at a 1:500 dilution. Actin was detected with Phalloidin 568 (Red) at a 1:200 dilution. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 40X objective.](http://images.novusbio.com/fullsize/Apolipoprotein-E-ApoE-Antibody-WUE-4-Immunocytochemistry-Immunofluorescence-NB110-60531-img0010.jpg)
![Flow Cytometry: Apolipoprotein E/ApoE Antibody (WUE-4) [NB110-60531] - Analysis of apoB-positivity in blood plasma and PLT concentrate-derived EXOs. FCM detection of the indicated markers in EXOs conjugated onto latex beads. The EXOs were isolated from fasting PFP or PLT concentrate by differential UC and gravity size filtration (gray histograms: blocked beads incubated with antibody, empty histograms: EXO sample). Image collected and cropped by CiteAb from the following publication (//www.nature.com/articles/srep24316), licensed under a CC-BY license.](http://images.novusbio.com/fullsize/Apolipoprotein-E-ApoE-Antibody-WUE-4-Flow-Cytometry-NB110-60531-img0020.jpg)
![Flow (Intracellular): Apolipoprotein E/ApoE Antibody (WUE-4) [NB110-60531] - An intracellular stain was performed on HepG2 cells with NB110-60531AF700 (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 5 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to Alexa Fluor 700.](http://images.novusbio.com/fullsize/Apolipoprotein-E-ApoE-Antibody-WUE-4-Flow-Intracellular-NB110-60531-img0012.jpg)
![Flow Cytometry: Apolipoprotein E/ApoE Antibody (WUE-4) [NB110-60531] - An intracellular stain was performed on HepG2 cells with NB110-60531PE (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 5 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to Phycoerythrin.](http://images.novusbio.com/fullsize/Apolipoprotein-E-ApoE-Antibody-WUE-4-Flow-Cytometry-NB110-60531-img0015.jpg)
![Flow Cytometry: Apolipoprotein E/ApoE Antibody (WUE-4) [NB110-60531] - An intracellular stain was performed on HepG2 cells with Apolipoprotein E/ApoE Antibody NB110-60531 [WUE-4] (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 1.0 ug/mL for 30 minutes at room temperature, followed by Mouse IgG (H+L) Cross-Adsorbed Secondary Antibody, Dylight 488.](http://images.novusbio.com/fullsize/Apolipoprotein-E-ApoE-Antibody-WUE-4-Flow-Cytometry-NB110-60531-img0016.jpg)
![Flow Cytometry: Apolipoprotein E/ApoE Antibody (WUE-4) [NB110-60531] - An intracellular stain was performed on SK-MEL-28 cells with alpha-Synuclein [2A7] Antibody NB110-60531AF488 (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 5 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to Alexa Fluor 488.](http://images.novusbio.com/fullsize/Apolipoprotein-E-ApoE-Antibody-WUE-4-Flow-Cytometry-NB110-60531-img0017.jpg)
![Flow Cytometry: Apolipoprotein E/ApoE Antibody (WUE-4) [NB110-60531] - An intracellular stain was performed on SK-MEL-28 cells with Apolipoprotein E/ApoE Antibody [WUE-4] NB110-60531F (blue) and a matched isotype control (orange). Cells were fixed with 4% PFA and then permeabilized with 0.1% saponin. Cells were incubated in an antibody dilution of 10 ug/mL for 30 minutes at room temperature. Both antibodies were conjugated to FITC.](http://images.novusbio.com/fullsize/Apolipoprotein-E-ApoE-Antibody-WUE-4-Flow-Cytometry-NB110-60531-img0018.jpg)
![Flow Cytometry: Apolipoprotein E/ApoE Antibody (WUE-4) [NB110-60531] - An intracellular stain was performed on SK-MEL-28 cells with Apolipoprotein E/ApoE [WUE-4] Antibody NB110-60531PE (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 Phycoerythrin.](http://images.novusbio.com/fullsize/Apolipoprotein-E-ApoE-Antibody-WUE-4-Flow-Cytometry-NB110-60531-img0019.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: 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)
![Western Blot: ABCA1 Antibody (HJ1) [NB100-2068] - Detection of ABCA1 in wildtype liver tissue (in RIPA) Lane 1: KO mouse liver tissue. Lane 2: WT mouse liver tissue.](http://images.novusbio.com/fullsize/ABCA1-Antibody-HJ1-Western-Blot-NB100-2068-img0012.jpg "<b>Genetic Strategies Validation. </b>Western Blot: ABCA1 Antibody (HJ1) [NB100-2068] - Detection of ABCA1 in wildtype liver tissue (in RIPA) Lane 1: KO mouse liver tissue. Lane 2: WT mouse liver tissue.")
![<b>Genetic Strategies Validation. </b>Immunohistochemistry: ABCA1 Antibody (HJ1) [NB100-2068] - Analysis of ABCA1 in human renal cancer using DAB with hematoxylin counterstain.](http://images.novusbio.com/fullsize/ABCA1-Antibody-HJ1-Immunohistochemistry-NB100-2068-img0006.jpg)
![Flow Cytometry: ABCA1 Antibody (HJ1) [NB100-2068] - Staining of 1 x 10^6 CHO (A) and HEK-293 (B) cells using ABCA1 antibody (dark blue). Isotype control shown in orange. An antibody concentration of 1 ug/1x10^6 cells was used.](http://images.novusbio.com/fullsize/ABCA1-Antibody-HJ1-Flow-Cytometry-NB100-2068-img0010.jpg)
![Western Blot: ABCA1 Antibody (3A1.891.3) [NB400-164] - Western blot analysis of lipid transporters in macrophages treated with or without oxLDL using antibodies against ABCA1 (NB400-164), SR-B1 (NB400-104), and CD36 (NB400-144) . Lrp1Y63F impairs Abca1-mediated cholesterol efflux and increases lipid accumulation in macrophages. Image collected and cropped by CiteAb from the following publication (//elifesciences.org/articles/29292) licensed under a CC-BY license.](http://images.novusbio.com/fullsize/ABCA1-Antibody-3A1-891-3-Western-Blot-NB400-164-img0008.jpg "<b>Biological Strategies Validation. </b>Western Blot: ABCA1 Antibody (3A1.891.3) [NB400-164] - Western blot analysis of lipid transporters in macrophages treated with or without oxLDL using antibodies against ABCA1 (NB400-164), SR-B1 (NB400-104), and CD36 (NB400-144) . Lrp1Y63F impairs Abca1-mediated cholesterol efflux and increases lipid accumulation in macrophages. Image collected and cropped by CiteAb from the following publication (//elifesciences.org/articles/29292) licensed under a CC-BY license.")
![<b>Biological Strategies Validation. </b>Immunohistochemistry-Paraffin: ABCA1 Antibody (3A1.891.3) [NB400-164] - Analysis of FFPE mouse liver using ABCA1 antibody at 1:500 on a Bond Rx autostainer (Leica Biosystems). The assay involved 20 minutes of heat induced antigen retrieval (HIER) using 10mM sodium citrate buffer (pH 6.0) and endogenous peroxidase quenching with peroxide block. The sections were incubated with primary antibody for 30 minutes and Bond Polymer Refine Detection (Leica Biosystems) with DAB was used for signal development followed by counterstaining with hematoxylin. Whole slide scanning and capturing of representative images was performed using Aperio AT2 (Leica Biosystems). Plasma membrane staining was observed. Staining was performed by Histowiz.](http://images.novusbio.com/fullsize/ABCA1-Antibody-3A1-891-3-Immunohistochemistry-Paraffin-NB400-164-img0007.jpg)
![Western Blot: ABCA1 Antibody (3A1.891.3) [NB400-164] - Detection of ABCA1 using NB400-164 at various dilutions in ABCA1 transfected HeLa lysates.](http://images.novusbio.com/fullsize/ABCA1-Antibody-3A1-891-3-Western-Blot-NB400-164-img0004.jpg)
![<b>Biological Strategies Validation. </b>Western Blot: ABCA1 Antibody (3A1.891.3) [NB400-164] - Analysis of ABCA1 in (A) T09 treated RAW 264.7 cells and (B) untreated RAW 264.7 cells.](http://images.novusbio.com/fullsize/ABCA1-Antibody-3A1-891-3-Western-Blot-NB400-164-img0006.jpg)
![Western Blot: ABCA1 Antibody (3A1.891.3) [NB400-164] - Lrp1Y63F mutation downregulates hepatic Abca1 levels.(A) Western blot analysis of Abca1 expression in the liver from Lrp1Y63F;Ldlr−/− & Ldlr−/− mice fed with HCHF diet for 16 weeks (n = 5, each group). (B) Western blot analysis of Abca1 expression in the liver from 16 week HCHF-fed Lrp1Y63F;Ldlr−/− & Ldlr−/− mice after BMT (n = 5, each group). All data are mean ±SEM. **p<0.01. Image collected & cropped by CiteAb from the following publication (//elifesciences.org/articles/29292), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-164_rat-monoclonal-abca1-antibody-3a1-891-3-31020241535616.jpg)
![Western Blot: ABCA1 Antibody (3A1.891.3) [NB400-164] - Lrp1Y63F mutation has no effect on atherogenic signaling pathways & morphological phenotype in SMCs.(A) Left: representative images of H&E stained descending thoracic aortas (scale bar = 50 μm). Right: aortic wall thickness & cell number were quantified for the indicated genotypes. Data are expressed mean ±SEM; n = 3 per group & genotype. (B) HCHF diet in Lrp1Y63F;Ldlr−/− mice has no effect on PDGF & TGF beta -mediated signaling in the aorta. Proteins were extracted from whole aorta in Lrp1Y63F;Ldlr−/− & Ldlr−/− mice fed with indicated diets. Expression of proteins involved in PDGF signaling pathways was determined by Western blot analysis. (C) Lrp1Y63F mutation did not affect atherogenic signaling pathways mediated by PDGF in vitro. Primary SMCs from WT & Lrp1Y63F mice were incubated with or without 10 ng/ml PDGF-BB for 10 min. Expression of proteins involved in PDGF signaling were determined by Western blot analysis. (D) Lrp1Y63F mutation did not alter SMC functions in vitro. Primary cultured SMCs from WT & Lrp1Y63F mice were incubated with or without 10 ng/ml PDGF-BB under indicated conditions, then cell migration (left) & proliferation (right) were determined. Values from three independent experiments are expressed as mean ±SEM. *p<0.05. Image collected & cropped by CiteAb from the following publication (//elifesciences.org/articles/29292), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-164_rat-monoclonal-abca1-antibody-3a1-891-3-310202416175236.jpg)
![Western Blot: ABCA1 Antibody (3A1.891.3) [NB400-164] - Lrp1Y63F impairs Abca1 induction through inhibiting the PPAR gamma /LXR pathway.(A) Real-time PCR analysis of Abca1, Abca7, Pparg, Nr1h3 & Nr2h2 expression in macrophages treated with or without ox-LDL. (B–E) Isolated peritoneal macrophages from Lrp1Y63F;Ldlr−/− & Ldlr−/− were pre-incubated for 1 hr with (B) T0070907 (PPAR gamma antagonist, 10 μM), (C) Rosiglitizone (PPAR gamma agonist) at indicated concentrations in μM, (D) T0901317 (nonspecific LXR agonist) at indicated concentrations in μM, (E) LXR623 (LXR beta full agonist & LXR alpha partial agonist) at indicated concentrations in μM, followed by the treatment with or without oxLDL for an additional 24 hr. Abca1 expression was assessed by immunoblot analysis (left). Protein expression was quantified & analyzed (right). Data are mean ±SEM from three independent experiments. *p<0.05; **p<0.01. Image collected & cropped by CiteAb from the following publication (//elifesciences.org/articles/29292), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-164_rat-monoclonal-abca1-antibody-3a1-891-3-310202416154639.jpg)
![Western Blot: ABCA1 Antibody (3A1.891.3) [NB400-164] - Lrp1Y63F mutation has no effect on atherogenic signaling pathways & morphological phenotype in SMCs.(A) Left: representative images of H&E stained descending thoracic aortas (scale bar = 50 μm). Right: aortic wall thickness & cell number were quantified for the indicated genotypes. Data are expressed mean ±SEM; n = 3 per group & genotype. (B) HCHF diet in Lrp1Y63F;Ldlr−/− mice has no effect on PDGF & TGF beta -mediated signaling in the aorta. Proteins were extracted from whole aorta in Lrp1Y63F;Ldlr−/− & Ldlr−/− mice fed with indicated diets. Expression of proteins involved in PDGF signaling pathways was determined by Western blot analysis. (C) Lrp1Y63F mutation did not affect atherogenic signaling pathways mediated by PDGF in vitro. Primary SMCs from WT & Lrp1Y63F mice were incubated with or without 10 ng/ml PDGF-BB for 10 min. Expression of proteins involved in PDGF signaling were determined by Western blot analysis. (D) Lrp1Y63F mutation did not alter SMC functions in vitro. Primary cultured SMCs from WT & Lrp1Y63F mice were incubated with or without 10 ng/ml PDGF-BB under indicated conditions, then cell migration (left) & proliferation (right) were determined. Values from three independent experiments are expressed as mean ±SEM. *p<0.05. Image collected & cropped by CiteAb from the following publication (//elifesciences.org/articles/29292), licensed under a CC-BY license. Not internally tested by Novus Biologicals.](http://images.novusbio.com/fullsize/nb400-164_rat-monoclonal-abca1-antibody-3a1-891-3-31020241616063.jpg)
![Western Blot: Apolipoprotein E R2/ApoE R2 Antibody [NB100-2216] - Analysis of ApoER2 on mouse brain membrane.](http://images.novusbio.com/fullsize/Apolipoprotein-E-R2-ApoE-R2-Antibody-Western-Blot-NB100-2216-img0005.jpg "Western Blot: Apolipoprotein E R2/ApoE R2 Antibody [NB100-2216] - Analysis of ApoER2 on mouse brain membrane.")
![Immunocytochemistry/Immunofluorescence: Apolipoprotein E R2/ApoE R2 Antibody [NB100-2216] - Antibody was tested in Neuro-2a cells with Dylight 488 (green). Nuclei and alpha-tubulin were counterstained with DAPI (blue) and Dylight 550 (red).](http://images.novusbio.com/fullsize/Apolipoprotein-E-R2-ApoE-R2-Antibody-Immunocytochemistry-Immunofluorescence-NB100-2216-img0006.jpg)
![Western Blot: VLDLR Antibody (6A6) [NBP1-78162] - MCF-7 cells were exposed to 20% or 1% O2 for 48 hours, whole cell lysates were loaded with 50 ug/lane. 10% SDS-PAGE. VLDLR Antibody (NBP1-78162) antibody at 1:1000, 4C, overnight. WB image submitted by a verifed customer review.](http://images.novusbio.com/fullsize/VLDLR-Antibody-6A6-Western-Blot-NBP1-78162-img0010.jpg "Western Blot: VLDLR Antibody (6A6) [NBP1-78162] - MCF-7 cells were exposed to 20% or 1% O2 for 48 hours, whole cell lysates were loaded with 50 ug/lane. 10% SDS-PAGE. VLDLR Antibody (NBP1-78162) antibody at 1:1000, 4C, overnight. WB image submitted by a verifed customer review.")
![Immunocytochemistry/Immunofluorescence: VLDLR Antibody (6A6) [NBP1-78162] - VLDL R Antibody (6A6) [NBP1-78162] - VLDL Receptor antibody was tested in HeLa cells with FITC (green). Nuclei and actin were counterstained with DAPI (blue) and Phalloidin (red).](http://images.novusbio.com/fullsize/VLDL-R-Antibody-6A6-Immunocytochemistry-Immunofluorescence-NBP1-78162-img0006.jpg)
![Immunohistochemistry: VLDL R Antibody (6A6) [NBP1-78162] - Analysis of VLDL Receptor in mouse kidney.](http://images.novusbio.com/fullsize/VLDL-R-Antibody-6A6-Immunohistochemistry-NBP1-78162-img0007.jpg)
![Western Blot: VLDL R Antibody (6A6) [NBP1-78162] - Analysis of VLDL Receptor expression in mouse kidney.](http://images.novusbio.com/fullsize/VLDL-R-Antibody-6A6-Western-Blot-NBP1-78162-img0008.jpg)
![Western Blot: Apolipoprotein E/ApoE Antibody [NBP1-31123] - A. 30 ug HepG2 whole cell lysate/extract 12% SDS-PAGE Apolipoprotein E antibody [C2C3], C-term dilution: 1:1000 The HRP-conjugated anti-rabbit IgG antibody was used to detect the primary antibody.](http://images.novusbio.com/fullsize/Apolipoprotein-E-ApoE-Antibody-Western-Blot-NBP1-31123-img0032.jpg "Western Blot: Apolipoprotein E/ApoE Antibody [NBP1-31123] - A. 30 ug HepG2 whole cell lysate/extract 12% SDS-PAGE Apolipoprotein E antibody [C2C3], C-term dilution: 1:1000 The HRP-conjugated anti-rabbit IgG antibody was used to detect the primary antibody.")
![Immunocytochemistry/Immunofluorescence: Apolipoprotein E/ApoE Antibody [NBP1-31123] - HepG2 cells were fixed in 4% paraformaldehyde at RT for 15 min. Green: Apolipoprotein E stained by Apolipoprotein E antibody [C2C3], C-term diluted at 1:500. Blue: Hoechst 33342 staining](http://images.novusbio.com/fullsize/Apolipoprotein-E-ApoE-Antibody-Immunocytochemistry-Immunofluorescence-NBP1-31123-img0033.jpg)
![Immunohistochemistry-Paraffin: Apolipoprotein E/ApoE Antibody [NBP1-31123] - Apolipoprotein E antibody [C2C3], C-term detects secreted Apolipoprotein E protein by immunohistochemical analysis.Sample: Paraffin-embedded human ovarian cancer.Apolipoprotein E stained by Apolipoprotein E antibody [C2C3], C-term (NBP1-31123).Antigen Retrieval: Citrate buffer, pH 6.0, 15 min](http://images.novusbio.com/fullsize/Apolipoprotein-E-ApoE-Antibody-Immunohistochemistry-Paraffin-NBP1-31123-img0036.jpg)
![Western Blot: Apolipoprotein E/ApoE Antibody [NBP1-31123] - HepG2 whole cell lysate/extract A : 30 ug whole cell lysate/extract of Apolipoprotein E protein expressing HepG2 cells B : Control with 3ug of pre-immune rabbit IgG C : Immunoprecipitation of Apolipoprotein E by 3 ug of Apolipoprotein E antibody [C2C3], C-term 10% SDS-PAGE The immunoprecipitated Apolipoprotein E protein was detected by Apolipoprotein E antibody [C2C3], C-term diluted at 1 : 1000. Easy Blot anti-rabbit IgG (HRP) was used as a secondary reagent.](http://images.novusbio.com/fullsize/Apolipoprotein-E-ApoE-Antibody-Western-Blot-NBP1-31123-img0006.jpg)
![Western Blot: Apolipoprotein E/ApoE Antibody [NBP1-31123] - Human tissue extract (30 ug) was separated by 10% SDS-PAGE, and the membrane was blotted with Apolipoprotein E antibody [C2C3], C-term diluted at 1:5000.](http://images.novusbio.com/fullsize/Apolipoprotein-E-ApoE-Antibody-Western-Blot-NBP1-31123-img0007.jpg)
![Western Blot: Apolipoprotein E/ApoE Antibody [NBP1-31123] - Sample (2. 5 ug of whole cell lysate) A: Conditional medium from human primary preadipocyte B: Conditional medium from differentiated human primary preadipocyte 12% SDS PAGE, antibody diluted at 1:2000.](http://images.novusbio.com/fullsize/Apolipoprotein-E-ApoE-Antibody-Western-Blot-NBP1-31123-img0029.jpg)
![Immunocytochemistry/Immunofluorescence: Apolipoprotein E/ApoE Antibody [NBP1-31123] - Apolipoprotein E antibody [C2C3], C-term detects Apolipoprotein E protein at cytoplasm by analysis. Sample: THP-1 cells were fixed in ice-cold MeOH for 5 min. Green: Apolipoprotein E protein stained by Apolipoprotein E antibody [C2C3], C-term diluted at 1:500. Blue: Hoechst 33342 staining.](http://images.novusbio.com/fullsize/Apolipoprotein-E-ApoE-Antibody-Immunocytochemistry-Immunofluorescence-NBP1-31123-img0008.jpg)
![Immunohistochemistry-Paraffin: Apolipoprotein E/ApoE Antibody [NBP1-31123] - Human hepatoma. Apolipoprotein E antibody [C2C3], C-term dilution: 1:500. Antigen Retrieval: Trilogy™ (EDTA based, pH 8.0) buffer, 15min](http://images.novusbio.com/fullsize/Apolipoprotein-E-ApoE-Antibody-Immunohistochemistry-Paraffin-NBP1-31123-img0026.jpg)
![ELISA: Apolipoprotein E/ApoE Antibody [NBP1-31123] - Sandwich ELISA detection of recombinant full-length Apolipoprotein E protein using as capture antibody at concentration of 5 ug/mL and a mouse monoclonal anti-Apolipoprotein E antibody as detection antibody at concentration of 1 ug/mL. Mouse IgG antibody (HRP) (NBP2-19382) was diluted at 1:10000 and used to detect the primary antibody.](http://images.novusbio.com/fullsize/Apolipoprotein-E-ApoE-Antibody-ELISA-NBP1-31123-img0035.jpg)
![Western Blot: ApoE4 Antibody (4E4) [NBP1-49529] - Analysis of ApoE4 expression in concentrated supernatants of CHO cells secreting human ApoE2, ApoE3 or ApoE4 using NBP1-49529. Image courtesy of Dr. Marko Roblek from the Medical University of Vienna.](http://images.novusbio.com/fullsize/ApoE4-Antibody-4E4-Western-Blot-NBP1-49529-img0004.jpg "Western Blot: ApoE4 Antibody (4E4) [NBP1-49529] - Analysis of ApoE4 expression in concentrated supernatants of CHO cells secreting human ApoE2, ApoE3 or ApoE4 using NBP1-49529. Image courtesy of Dr. Marko Roblek from the Medical University of Vienna.")
![Immunocytochemistry/Immunofluorescence: ApoE4 Antibody (4E4) [NBP1-49529] - HepG2 cells were fixed for 10 minutes using 10% formalin and then permeabilized for 5 minutes using 1X TBS + 0.5% Triton X-100. The cells were incubated with anti-ApoE4 (4E4) at 5 ug/ml overnight at 4C and detected with an anti-mouse DyLight 488 (Green) at a 1:500 dilution. Actin was detected with Phalloidin 568 (Red) at a 1:200 dilution. Nuclei were counterstained with DAPI (Blue). Cells were imaged using a 40X objective.](http://images.novusbio.com/fullsize/ApoE4-Antibody-4E4-Immunocytochemistry-Immunofluorescence-NBP1-49529-img0005.jpg)