Recombinant Mouse HMGCR protein (His tag)
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Recombinant Mouse HMGCR protein (His tag) is a Mouse Fragment protein, in the 700 to 860 aa range, expressed in Escherichia coli, with >85%, suitable for SDS-PAGE.
View Alternative Names
3-hydroxy-3-methylglutaryl-coenzyme A reductase, HMG-CoA reductase, Hmgcr
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant Mouse HMGCR protein (His tag) (AB235715)
(Tris-glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel of ab235715.
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
HMGCR reduces HMG-CoA to mevalonate an important precursor for several important biomolecules including cholesterol. It exists as part of a complex regulatory system impacted by intracellular cholesterol levels. The activity of HMGCR is tightly controlled through feedback inhibition and post-translational modifications. The enzyme interacts with other proteins in the endoplasmic reticulum as part of the cholesterol homeostatic mechanism in cells expressing it including hepatocytes.
Pathways
HMGCR is an essential component of the mevalonate pathway which is important for the synthesis of sterols and non-sterol isoprenoids. This pathway also intersects with the biosynthesis of ubiquinone and dolichol. The regulation of cholesterol synthesis involves the coordinated activity of HMG-CoA reductase and LDL receptor proteins. Their interplay ensures a balanced cholesterol level and integrates with the response to cellular demands and dietary intake.
Specifications
Form
Liquid
General info
Function
Catalyzes the conversion of (3S)-hydroxy-3-methylglutaryl-CoA (HMG-CoA) to mevalonic acid, the rate-limiting step in the synthesis of cholesterol and other isoprenoids, thus plays a critical role in cellular cholesterol homeostasis.
Sequence similarities
Belongs to the HMG-CoA reductase family.
Post-translational modifications
Undergoes sterol-mediated ubiquitination and ER-associated degradation (ERAD). Accumulation of sterols in the endoplasmic reticulum (ER) membrane, triggers binding of the reductase to the ER membrane protein INSIG1 or INSIG2. The INSIG1 binding leads to the recruitment of the ubiquitin ligase, AMFR/gp78, RNF139 or RNF145, initiating ubiquitination of the reductase. The ubiquitinated reductase is then extracted from the ER membrane and delivered to cytosolic 26S proteosomes by a mechanism probably mediated by the ATPase Valosin-containing protein VCP/p97. The INSIG2-binding leads to the recruitment of the ubiquitin ligase RNF139, initiating ubiquitination of the reductase. Lys-248 is the main site of ubiquitination. Ubiquitination is enhanced by the presence of a geranylgeranylated protein.. N-glycosylated. Deglycosylated by NGLY1 on release from the endoplasmic reticulum (ER) in a sterol-mediated manner.. Phosphorylated. Phosphorylation at Ser-871 reduces the catalytic activity.
Subcellular localisation
Peroxisome membrane
Target data
Product promise
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