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anti-Human ABCG1 Antikörper:
anti-Mouse (Murine) ABCG1 Antikörper:
anti-Rat (Rattus) ABCG1 Antikörper:
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Chinese Hamster Polyclonal ABCG1 Primary Antibody für ICC, IF - ABIN152900
Hu, Abe-Dohmae, Tsujita, Iwamoto, Ogikubo, Otsuka, Kumon, Yokoyama: Biogenesis of HDL by SAA is dependent on ABCA1 in the liver in vivo. in Journal of lipid research 2008
Show all 113 Pubmed References
Polyclonal ABCG1 Primary Antibody für IHC (fro), WB - ABIN540802
Tansley, Burgess, Bryan, Su, Hirsch-Reinshagen, Pearce, Chan, Wilkinson, Evans, Naus, McIsaac, Bromley, Song, Yang, Wang, DeMattos, Wellington: The cholesterol transporter ABCG1 modulates the subcellular distribution and proteolytic processing of beta-amyloid precursor protein. in Journal of lipid research 2007
Show all 5 Pubmed References
Human Polyclonal ABCG1 Primary Antibody für WB - ABIN3044094
Yan, Ding, Dong, Li, Wu: Sphingomyelin synthase overexpression increases cholesterol accumulation and decreases cholesterol secretion in liver cells. in Lipids in health and disease 2011
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Human Monoclonal ABCG1 Primary Antibody für IF, IHC - ABIN6135495
Qian, Ma, Wu, Yu, Lin, Ying, Wen, Gao: G004, a synthetic sulfonylurea compound, exerts anti-atherosclerosis effects by targeting SIRT1 in ApoE-/- mice. in Vascular pharmacology 2017
Human Polyclonal ABCG1 Primary Antibody für IHC, WB - ABIN5664740
He, Zhang, Pang, Yu, Xiong, Zhu, Chen: SIRT6 reduces macrophage foam cell formation by inducing autophagy and cholesterol efflux under ox-LDL condition. in The FEBS journal 2017
Human Polyclonal ABCG1 Primary Antibody für IF (p), IHC (p) - ABIN673719
Jia, Song, Yang, Ma, Li, Lu, Cao, Zhang, Zhu, Wang, Leng, Cao, Du, Xu: Effects of Tanshinone IIA on the modulation of miR‑33a and the SREBP‑2/Pcsk9 signaling pathway in hyperlipidemic rats. in Molecular medicine reports 2016
Human Polyclonal ABCG1 Primary Antibody für IHC (p), WB - ABIN4956605
OReilly, Kajani, Ralston, Lenighan, Roche, McGillicuddy: Nutritionally Derived Metabolic Cues Typical of the Obese Microenvironment Increase Cholesterol Efflux Capacity of Adipose Tissue Macrophages. in Molecular nutrition & food research 2019
Aortic endothelial cells transcytose high-density lipoproteins by mechanisms that involve either SR-BI or ABCG1 but not ABCA1.
Regulation of IL-32 in human primary liver cells, HepG2 and THP-1cells strongly influences the mRNA expression of ABCA1, ABCG1, LXRalpha and apoA1 and affects intracellular lipid concentrations.
membrane cholesterol distribution contributes to insulin homeostasis at production, packaging, and export levels through the actions of OSBP and ABCs G1 and A1.
Study found evidence that metabolic syndrome was associated with increased methylation on the cg06500161 locus in the ABCG1 gene.
HSP70 suppresses the expression of ABCA1 and ABCG1 through preventing Elk-1 from binding to the promoter of ABCA1 and ABCG1 in human THP-1-derived macrophages.
Downregulation of ABCG1 in macrophages promoted atherosclerotic lesions.
High ABCG1 expression is associated with glioma.
ABCG1 regulates pulmonary surfactant metabolism
Hepatic free cholesterol content was significantly increased in NASH as compared to non-NASH subjects, while ABCA1 and ABCG1 protein levels significantly decreased with NASH and fibrosis progression. The relative expression of miR-33a and miR-144 correlated inversely with ABCA1 but not with ABCG1 protein levels. miR-33a/144 and their target gene ABCA1 may contribute to the pathogenesis of NASH in morbidly obese subjects.
Understanding the relationship between cholesterol and inflammation in the lung, and the role that ABC transporters play in this may illuminate new pathways to target for the treatment of inflammatory lung diseases
Findings suggest that the ABCG1-mediated efflux of cholesterol, but not of 7-ketocholesterol, shows specificity for structural domains of apoA-I bound to reconstituted HDL. Although the mid region alone of apoA-I associated to rHDL can promote ABCG1-mediated cholesterol efflux, deletion of carboxyl-terminal region 185-243 from full-length apoA-I diminishes ABCG1-mediated cholesterol efflux.
ABCG1 regulates T cell differentiation into Tregs, highlighting a pathway by which cholesterol accumulation can influence T cell homeostasis in atherosclerosis
Data show that ELOVL7, SOCS3, ACSL4 and CLU were upregulated while PRKAR1A and ABCG1 were downregulated in the phlegm-dampness group.
ABCG1 and ABCG4 alter the distribution of gamma-secretase on the plasma membrane, leading to the decreased gamma-secretase activity and suppressed Abeta secretion
Both the full-length and the short isoforms of ABCG1 can dimerize with ABCG4, whereas the ABCG2 multidrug transporter is unable to form a heterodimer with ABCG4.
DNA methylation at the ABCG1 locus cg06500161 in blood DNA was associated with an increased risk for future type2 diabetes.
we have newly identified a haplotype-tagging SNP, rs225396, in ABCG1 to be associated with PCV and nAMD in Chinese and Japanese cohorts. This provides new evidence to support ABCG1 as a susceptibility gene for PCV and nAMD.
ABCG1 gene expression positively correlated with obesity indicators.
Our results indicated that genetic variants of ABCG1 may be predictors of survival of nonsmall-cell lung cancer patients
This review focuses on the role of ABC transporters A1 and G1 in the pathogenesis of atherosclerosis
Leu at position 550/562 in mABCG1/hABCG1 is critical for their plasma membrane localization but not for ABCG1-mediated cholesterol efflux.
ABCG1-overexpressing EPCs showed increased migration and tube formation and differentiation via the Lck/Yes-related novel protein tyrosine kinase /Akt/endothelial NO synthase pathway.
Stably expressed GFP-tagged ABCG1 closely mimics the distribution of endogenous ABCG1 in pancreatic insulin-secreting cells and accumulates in the trans-Golgi network (TGN), endosomal recycling compartment (ERC) and on the cell surface but not on insulin granules, early or late endosomes. Notably, ABCG1 is short-lived, and proteasomal and lysosomal inhibitors both decrease its degradation.
The TLR4 expression increased significantly in the arterial walls after receiving HFD treatment, while that of the co-localizing PPARgamma and ABCG1 markedly decreased. TLR4 deficiency reversed the HFD-induced attenuation of PPARgamma and ABCG1.
ABCG1 knockout mice exhibited an altered expression of multiple genes related to many aspects of atherosclerosis, which might affect the further studies to insight into the effect of ABCG1 on atherosclerosis with this animal model.
HSP70 promotes the progression of atherosclerosis in apoE-/- mice by suppressing the expression of ABCA1 and ABCG1 through the JNK/Elk-1 pathway.
TMP upregulated the protein stability of ABCA1 without affecting ABCG1. Accordingly, TMP regulated the expression of SR-A, CD36, ABCA1 and ABCG1 in aortas of ApoE-/- mice, which resembled the findings observed in macrophages.
Our data indicate that a combination of vildagliptin and pravastatin significantly induces the expression of LXR-ABCA1/ABCG1 cascade and improves cholesterol efflux (P > 0.05) in adipocytes. Our data may explain, at least in part, the improvement in HDL-C levels observed in patients receiving both medications
ABCG1 may play a protective role in early-stage atherosclerosis by reducing endothelial activation induced by oscillatory shear stress via suppressing the inflammatory response.
Endothelial cholesterol efflux pathways mediated by ABCA1 and ABCG1 are nonredundant and atheroprotective, reflecting preservation of endothelial NO synthase activity and suppression of endothelial inflammation, especially in regions of disturbed arterial blood flow.
ABCG1, irrespective of either a leucine or proline at position 550, is an intracellular protein that localizes to vesicles of the endosomal pathway where it functions to mobilize sterols away from the endoplasmic reticulum and out of the cell.
our study suggests that MEK1/2 inhibitors activate macrophage ABCG1 expression/RCT, and inhibit foam cell formation and lesion development by multiple mechanisms, supporting the concept that ERK1/2 inhibition is anti-atherogenic
miR-33 augments macrophage lipid rafts and enhances proinflammatory cytokine induction and NF-kappaB activation by LPS. This occurs through an ABCA1- and ABCG1-dependent mechanism and is reversible by interventions upon raft cholesterol and by ABC transporter-inducing liver X receptor agonists.
ABCG1 expression was down-regulated by TLR4, which induces inflammation and lipid accumulation in vascular smooth muscle cells via PPARgamma/LXRalpha signaling.
Visfatin upregulated CD36 and SRA expression and downregulated ABCA1 and ABCG1 expression, subsequently increased ox-LDL uptake and decreased cholesterol efflux, and finally promoted foam cell formation via the PI3K- and ERK-dependent pathways.
3beta,5alpha,6beta-cholestanetriol and 25-hydroxycholesterol are physiologic substrates for ABCG1
Our data suggest that GLP-1-based therapy modulate ABCA1/ABCG1 expression in adipocytes potentially through an LXR-alpha mediated process.
The absence of ABCG1 inhibits tumour growth through modulation of macrophage function within the tumour, and illustrates a link between cholesterol homeostasis and cancer.
The protein encoded by this gene is a member of the superfamily of ATP-binding cassette (ABC) transporters. ABC proteins transport various molecules across extra- and intra-cellular membranes. ABC genes are divided into seven distinct subfamilies (ABC1, MDR/TAP, MRP, ALD, OABP, GCN20, White). This protein is a member of the White subfamily. It is involved in macrophage cholesterol and phospholipids transport, and may regulate cellular lipid homeostasis in other cell types. Six alternative splice variants have been identified.
ATP-binding cassette sub-family G member 1
, ATP-binding cassette, sub-family G (WHITE), member 1
, ATP-binding cassette sub-family G member 1-like
, ABC transporter 8
, ATP-binding cassette transporter 8
, ATP-binding cassette transporter member 1 of subfamily G
, homolog of Drosophila white
, white protein homolog (ATP-binding cassette transporter 8)
, ATP-binding cassette 8
, ATP-binding cassette, subfamily G, member 1
, white protein homolog