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The protein encoded by NPC1L1 is a multi-pass membrane protein. Additionally we are shipping NPC1L1 Proteins (10) and NPC1L1 Kits (1) and many more products for this protein.
Showing 10 out of 45 products:
Human Polyclonal NPC1L1 Primary Antibody for WB - ABIN1881583
Teslovich, Musunuru, Smith, Edmondson, Stylianou, Koseki, Pirruccello, Ripatti, Chasman, Willer, Johansen, Fouchier, Isaacs, Peloso, Barbalic, Ricketts, Bis, Aulchenko, Thorleifsson, Feitosa et al.: Biological, clinical and population relevance of 95 loci for blood lipids. ... in Nature 2010
Show all 5 references for ABIN1881583
We therefore propose that cholesterol is absorbed by NPC1L1 acting as a membrane transporter and that NPC1L1 is internalized to an endosomal compartment to reduce the absorption of cholesterol.
NPC1L1 knockout protects against colitis-associated tumorigenesis.
demonstrate that Niemann-Pick C1-like 1 (NPC1L1) protein, a cholesterol transporter, plays a central role in intestinal VK uptake and modulates the anticoagulant effect of warfarin. In
NPC1L1 may suppress gluconeogenesis by inhibition of FoxO1 (show FOXO1 Antibodies) pathways.
DNA methylation (show HELLS Antibodies) in the promoter region of the NPC1L1 gene appears to be a major mechanism underlying differential expression of NPC1L1 along the length of the gastrointestinal tract.
cholesterol and tocopherol uptakes share common pathways in cell culture models, but display different in vivo absorption patterns associated with distinct contributions of SR-BI (show SCARB1 Antibodies) and NPC1L1
The clathrin adaptor Numb (show NUMB Antibodies) regulates intestinal cholesterol absorption through dynamic interaction with NPC1L1.
Glucose appears to directly modulate NPC1L1 expression via transcriptional mechanisms and the involvement of phosphatase-dependent pathways.
the mechanism of cholesterol sensing by NPC1L1 and proposes a mechanism for selective cholesterol absorption
Cdc42 (show CDC42 Antibodies) controls the cholesterol-regulated transport and localization of NPC1L1, and plays a role in cholesterol absorption.
These findings demonstrated a direct role of hepatic NPC1L1 in regulating biliary cholesterol excretion and hepatic/blood cholesterol levels, and unequivocally established hepatic NPC1L1 as a target of ezetimibe.
exposure to LDL-C-lowering genetic variants in or near NPC1L1 and other genes was associated with a higher risk of type 2 diabetes. These data provide insights into potential adverse effects of LDL-C-lowering therapy.
Detailed analysis of the role of NPC1L1 mutations in an exceptional responder to ezetimibe. The results point to a complex set of events in which the combined mutations were shown to affect cholesterol uptake in the presence of ezetimibe. Proteomic analysis suggests that the exceptional response may also lie in the nature of interactions with cytosolic proteins.
Study suggests that the G allele of the NPC1L1 polymorphism g1679C>G may be a positive marker of gallstone formation risk.
To study whether human NPC1L1 gene is regulated transcriptionally by LRH-1 (show NR5A2 Antibodies), we have analyzed evolutionary conserved regions (ECRs) in HepG2 cells.
No significant association between investigated NPC1L1 variants and risk of coronary atherosclerosis could be observed.
Results show that genetic variation in NPC1L1 is associated with a reduction in risk of IVD (show IVD Antibodies), with a corresponding reduction in LDL cholesterol, but with a concomitant increased risk of gallstone disease
The frequencies of NPC1L1 polymorphisms in Chinese Hans are comparable to Japanese population but totally different from Caucasians, African-Americans and Hispanic individuals
Lipid-lowering response to ezetimibe is not impacted by the NPC1L1 polymorphisms studied in Chilean hypercholesterolemic subjects.
NPC1L1-mediated cholesterol absorption is a major determinant of blood levels of apolipoprotein B (show APOB Antibodies)-containing atherogenic lipoproteins
The protein encoded by this gene is a multi-pass membrane protein. It contains a conserved N-terminal Niemann-Pick C1 (NPC1) domain and a putative sterol-sensing domain (SSD) which includes a YQRL motif functioning as a plasma membrane to trans-Golgi network transport signal in other proteins. This protein takes up free cholesterol into cells through vesicular endocytosis and plays a critical role in the absorption of intestinal cholesterol. It also has the ability to transport alpha-tocopherol (vitamin E). The drug ezetimibe targets this protein and inhibits the absorption of intestinal cholesterol and alpha-tocopherol. In addition, this protein may play a critical role in regulating lipid metabolism. Polymorphic variations in this gene are associated with plasma total cholesterol and low-density lipoprotein cholesterol (LDL-C) levels and coronary heart disease (CHD) risk. Alternatively spliced transcript variants encoding different isoforms have been found for this gene.
, NPC1 (Niemann-Pick disease, type C1, gene)-like 1
, Niemann-Pick C1-like protein 1
, Niemann-Pick C1-like 1 protein
, Niemann-Pick C1-like protein 1-like
, Niemann-Pick disease, type C1
, Niemann-Pick disease, type C1-like 1