Anti-HMG-CoA reductase Antibody

Epitope: Linker domain

KLH-conjugated linear peptide corresponding to the linker domain of human HMG CoA reductase.

Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.

Replaces: 07-572

Evaluated by Western Blot in HepG2 cell lysate.

Western Blot Analysis: 1 µg/mL of this antibody detected HMG CoA reductase on 10 µg of HepG2 cell lysate.

Anti-HMG-CoA reductase Antibody detects level of HMG-CoA reductase & has been published & validated for use in Immunoprecipitation, Western Blotting.

Immunoprecipitation Analysis: 10 µg/mL from a representative lot immunoprecipitated HMG CoA reductase from HepG2 cell lysate.

Other homologies: Porcine (85% sequence homology).

This antibody recognizes HMG CoA reductase at the linker domain.

The 3-hydroxy-3-methylglutaryl-coenzyme A reductase (HMG-CoA reductase) enzyme is a ubiquitously expressed glycoprotein that is bound to the membrane of the endoplasmic reticulum (ER), but also projects an active C-terminal catalytic tail into the cytoplasm. It is the rate-limiting enzyme in the mevalonate pathway as it catalyzes the conversion of HMG CoA to mevalonate, which is a critical precursor protein in the synthesis of sterols such as cholesterols. In mammalian cells, HMG-CoA reductase is regulated by multiple mechanisms. It is downregulated by high levels of exogenous cholesterol bound to the low density lipoprotein. It is also regulated by sterol and nonsterol metabolites of mevalonate which may exert inhibitory effects at the transcriptional level. Previous studies have suggested that sterols may inhibit the sterol regulatory element-binding proteins (SREBPs) which function as transcription factors that enhance the expression of genes required for sterol biosynthesis. The end-stage degradation process may be mediated by the ubiquitin degradation system. The inhibition of HMG-CoA reductase has been widely studied for the treatment of cholesterol-related conditions.

~97 kDa observed