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HMG-CoA Reductase (human recombinant)

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    HMG-<wbr/>CoA Reductase (human recombinant)
  • HMG-<wbr/>CoA Reductase (human recombinant)
Cat No: 14944
Proteins - Enzymes
Cayman

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 ...

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: 250 µg

This product can only be bought through Cayman Chemical. Please contact us.

Territorial Availability: Available through Bertin Technologies only in France
Correlated keywords:
  • cholesterol mevalonate hyperlipidemia cardiovasular disease cancers cell biology recombinant proteins HMGR isoprenoids statins P04035 HMG CoA HMGCoA
Product Overview:
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.{26861,26862} HMGR is controlled by feedback regulation from sterols and non-sterol metabolites derived from mevalonate.{26862,26863,26860} 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.{15309} Potent inhibitors of HMGR, collectively called statins, are effective in lowering mortality due to hypercholesterolemia by lowering serum cholesterol levels.{26864}
Size 250 µg
Shipping dry ice
Formulation 50 mM Tris, pH 8.0, with 300 mM sodium chloride and 20% glycerol
Purity ≥85% estimated by SDS-PAGE
Custom Code 3504.00
UNSPSC code 12352204

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Cayman Chemical's mission is to help make research possible by supplying scientists worldwide with the basic research tools necessary for advancing human and animal health. Our utmost commitment to healthcare researchers is to offer the highest quality products with an affordable pricing policy.

Our scientists are experts in the synthesis, purification, and characterization of biochemicals ranging from small drug-like heterocycles to complex biolipids, fatty acids, and many others. We are also highly skilled in all aspects of assay and antibody development, protein expression, crystallization, and structure determination.

Over the past thirty years, Cayman developed a deep knowledge base in lipid biochemistry, including research involving the arachidonic acid cascade, inositol phosphates, and cannabinoids. This knowledge enabled the production of reagents of exceptional quality for cancer, oxidative injury, epigenetics, neuroscience, inflammation, metabolism, and many additional lines of research.

Our organic and analytical chemists specialize in the rapid development of manufacturing processes and analytical methods to carry out clinical and commercial GMP-API production. Pre-clinical drug discovery efforts are currently underway in the areas of bone restoration and repair, muscular dystrophy, oncology, and inflammation. A separate group of Ph.D.-level scientists are dedicated to offering Hit-to-Lead Discovery and Profiling Services for epigenetic targets. Our knowledgeable chemists can be contracted to perform complete sample analysis for analytes measured by the majority of our assays. We also offer a wide range of analytical services using LC-MS/MS, HPLC, GC, and many other techniques.

Accreditations
ISO/IEC 17025:2005
ISO Guide 34:2009

Cayman is a leader in the field of emerging drugs of abuse, providing high-purity Schedule I-V Controlled Substances to federally-licensed laboratories and qualified academic research institutions for forensic analyses. We are certified by ACLASS Accreditation Services with dual accreditation to ISO/IEC 17025:2005 and ISO Guide 34:2009.

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