Recombinant Mouse HMGCR protein (His tag) is a Mouse Fragment protein, in the 700 to 860 aa range, expressed in Escherichia coli, with >85% purity and suitable for SDS-PAGE.
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Application | Reactivity | Dilution info | Notes |
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Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
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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.
3-hydroxy-3-methylglutaryl-coenzyme A reductase, HMG-CoA reductase, Hmgcr
Recombinant Mouse HMGCR protein (His tag) is a Mouse Fragment protein, in the 700 to 860 aa range, expressed in Escherichia coli, with >85% purity and suitable for SDS-PAGE.
pH: 7.2 - 7.4
Constituents: Tris buffer, 50% Glycerol (glycerin, glycerine)
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.
Belongs to the HMG-CoA reductase family.
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.
HMG-CoA reductase also known as HMGCR plays an important role in cholesterol biosynthesis. This enzyme catalyzes the conversion of HMG-CoA (3-hydroxy-3-methyl-glutaryl-coenzyme A) to mevalonate a critical step in the isoprenoid synthesis pathway. HMGCR is a membrane-bound enzyme located primarily in the liver on the endoplasmic reticulum. The enzyme has a molecular mass of approximately 97 kDa. Due to its central role in cholesterol metabolism HMGCR has become a primary target for statins such as pravastatin and simvastatin.
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.
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.
HMGCR is strongly linked to cardiovascular diseases due to its influential role in cholesterol synthesis. Inhibitors like pravastatin and simvastatin effectively lower blood cholesterol levels and reduce the risk of coronary artery disease by targeting HMGCR. The Statins also have potential associations with muscular disorders because of shared pathways involving proteins such as SREBP (sterol regulatory element-binding proteins) which regulate the transcription of genes involved in lipid metabolism.
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(Tris-glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel of ab235715.
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