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SAB4200529

Sigma-Aldrich

Anti-HMGCR (internal) antibody produced in rabbit

~1.0 mg/mL, affinity isolated antibody

Synonym(s):

Anti-3-hydroxy-3-methylglutaryl-CoA reductase, LDLCQ3

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen ~100 kDa

species reactivity

human, mouse, rat

concentration

~1.0 mg/mL

technique(s)

western blot: 1.5-3.0 μg/mL using extracts of mevastatin-treated HepG2 cells, and of mouse and rat liver microsomes.

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... HMGCR(3156)

General description

3-hydroxy-3-methylglutaryl-CoA reductase (HMGCR) is a transmembrane glycoprotein, encoded by the gene mapped to human chromosome 5q13.3-q14. HMGCR has a molecular mass of 97kDa and is mainly localized to smooth endoplasmic reticulum. The encoded protein is predominantly expressed in liver tissues.
The 3-hydroxy-3-methylglutaryl-CoA reductase (HMGCR) codes for a part of the statin-binding domain of the enzyme. This gene is located on human chromosome 5q13. HMGCR has a molecular mass of 97kDa and is mainly localized to smooth endoplasmic reticulum. The encoded protein is predominantly expressed in liver tissues.

Immunogen

synthetic peptide corresponding to an internal sequence of human HMGCR, conjugated to KLH. The corresponding sequence is identical in human HMGCR isoform 2 and highly conserved in mouse (89% identity) and in rat (83% identity) HMGCR.

Biochem/physiol Actions

3-hydroxy-3-methylglutaryl-CoA reductase (HMGCR) plays a major role in mevalonate biosynthesis, which is a rate limiting step of cholesterol biosynthesis in the liver. Additionally, it also plays a key role in various biological process such as, embryogenesis and cancer. Elevated expression of the gene is associated with the development of gastric cancer(GC) and glioblastoma cells. Thus, HMGCR can be considered as a potent therapeutic target for GC and glioblastoma.
The 3-hydroxy-3-methylglutaryl-CoA reductase (HMGCR) acts as the rate-limiting step in cholesterol synthesis. Polymorphism in HMGCR results in late-onset Alzheimer′s disease. It induces the growth and migration of the cancer cells.

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

Disclaimer

Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.

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Storage Class Code

10 - Combustible liquids

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.

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HMGCR positively regulated the growth and migration of glioblastoma cells.
Qiu Z
Gene, 576, 22-27 (2016)
Hmgcr in the Corpus Allatum Controls Sexual Dimorphism of Locomotor Activity and Body Size via the Insulin Pathway in Drosophila
Belgacem YH and Martin JR
PLoS ONE, 2 (2007)
Xiaojia Chen et al.
Heliyon, 9(12), e22785-e22785 (2023-12-13)
Methyl protodioscin (MPD) is the main component of total diosgenin, which was reported to reduce cholesterol and triglyceride levels potentially. This study aimed to investigate the beneficial effects of MPD against lipid disorder in hyperlipidemic gerbils induced by a high-fat
Genes for HMG-CoA reductase and serotonin 1a receptor are on mouse chromosome 13
Sundaresan S
Somatic Cell and Molecular Genetics, 15, 465-469 (1989)
Association of HMGCR polymorphism with late-onset Alzheimer's disease in Han Chinese
Chang XL, et al.
Oncotarget, 7(16), 22746-22751 (2016)

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