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Merck

SAB4200528

Sigma-Aldrich

Anti-HMGCR antibody produced in rabbit

~1.0 mg/mL, affinity isolated antibody

Sinónimos:

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

concentration

~1.0 mg/mL

technique(s)

indirect immunofluorescence: 1.0-2.0 μg/mL using mevastatin-treated HepG2 cells.
western blot: 1.5-3.0 μg/mL using extracts of mevastatin-treated HepG2 cells.

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... HMGCR(3156)

General description

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 97 kDa 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 has 87% sequence identity in mouse HMGCR and 81% identity in rat HMGCR.

Application

Anti-HMGCR antibody produced in rabbit has been used in western blotting.

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. Polymorphism in HMGCR results in late-onset Alzheimer′s disease.

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

10 - Combustible liquids

flash_point_f

Not applicable

flash_point_c

Not applicable


Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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Visite la Librería de documentos

Association of HMGCR polymorphism with late-onset Alzheimer's disease in Han Chinese.
Chang XL, et al.
Oncotarget, 7(16), 22746?22751-22746?22751 (2016)
Jittima Tomacha et al.
Frontiers in pharmacology, 12, 696961-696961 (2021-08-24)
An aberrant regulation of lipid metabolism is involved in the pathogenesis and progression of cancer. Up-regulation of lipid biosynthesis enzymes, including acetyl-CoA carboxylase (ACC), fatty acid synthase (FASN) and HMG-CoA reductase (HMGCR), has been reported in many cancers. Therefore, elucidating
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(1), e187-e187 (2007)
Yuval Yogev et al.
Proceedings of the National Academy of Sciences of the United States of America, 120(7), e2217831120-e2217831120 (2023-02-07)
Myopathy is the main adverse effect of the widely prescribed statin drug class. Statins exert their beneficial effect by inhibiting HMG CoA-reductase, the rate-controlling enzyme of the mevalonate pathway. The mechanism of statin myopathy is yet to be resolved, and
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)

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