HMG-CoA Reductase (human recombinant)

HMG-CoA reductase (HMGR) is a highly regulated enzyme found on the endoplasmic reticulum (ER) membrane. It is bound to the ER membrane by a multi-pass 339 amino acid N-terminal transmembrane domain while the carboxy terminal catalytic region projects into the cytosol. HMGR is controlled by feedback regulation from sterols and non-sterol metabolites derived from mevalonate. Binding of cholesterol derived from internalized LDL receptors suppresses HMGR. The enzyme is responsible for catalyzing the rate-limiting step in cholesterol biosynthesis. Mevalonate, which is converted to isopentenyl pyrophosphate, is the building block for cholesterol and non-sterol isoprenoids. The four-electron reduction of HMG-CoA catalyzed by HMGR to form mevalonate is the committed step in the biosynthesis of sterols and isoprenoids. Potent inhibitors of HMGR, collectively called statins, are effective in lowering mortality due to hypercholesterolemia by lowering serum cholesterol levels.Synonyms: 3-hydroxy-3-methylglutaryl-Coenzyme A Reductase, HMGCR, HMGR. Purity: >85% estimated by SDS-PAGE. Source: recombinant N-terminal GST-tagged protein expressed in E. coli. Amino Acids: 426-888 (N-terminal truncation). MW: 76.5 kDa. Formulation: (Request formulation change), 50 mM Tris, pH 8.0, with 300 mM sodium chloride and 20% glycerol. UniProt Accession #: P04035.