Active, pure human recombinant enzyme
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HMG-CoA Reductase (human recombinant)

Item No. 14944

Technical Information
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
50 mM Tris, pH 8.0, with 300 mM sodium chloride and 20% glycerol
UniProt Accession №
P04035
Shipping & Storage Information
Storage
-80°C
Shipping
Dry ice in continental US; may vary elsewhere
Certificates of Analysis & Batch Specific Data

Provide batch numbers separated by commas to download or request available product inserts, QC sheets, certificates of analysis, data packs, and GC-MS data.

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    Product Description

    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.1,2 HMGR is controlled by feedback regulation from sterols and non-sterol metabolites derived from mevalonate.2,3,4 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.5 Potent inhibitors of HMGR, collectively called statins, are effective in lowering mortality due to hypercholesterolemia by lowering serum cholesterol levels.6

    WARNING This product is not for human or veterinary use.

    References & Product Citations
    Product Description References

    1. Istvan, E.S., Palnitkar, M., Buchanan, S.K., et alCrystal structure of the catalytic portion of human HMG-CoA reductase: Insights into regulation of activity and catalysis. EMBO J. 19(5), 819-830 (2000).

    2. Luskey, K.L., and Stevens, B. Human 3-hydroxy-3-methylglutaryl coenzyme A reductase. Conserved domains responsible for catalytic activity and sterol-regulated degradation. The Journal of Biological Chemisty 260(18), 10271-10277 (1985).

    3. Brown, M.S., and Goldstein, J.L. Multivalent feedback regulation of HMG CoA reductase, a control mechanism coordinating isoprenoid synthesis and cell growth. J. Lipid Res. 21(5), 505-517 (1980).

    4. Sever, N., Yang, T., Brown, M.S., et alAccelerated degradation of HMG CoA reductase mediated by binding of insig-1 to its sterol-sensing domain. Mol. Cell 11(1), 25-33 (2003).

    5. Istvan, E.S., and Deisenhofer, J. Structural mechanism for statin inhibition of HMG-CoA reductase. Science 292(5519), 1160-1164 (2001).

    6. Brown, W.V. Safety of statins. Curr. Opin. Lipidol. 19(6), 558-562 (2008).