3-hydroxy-3-methylglutaryl-coenzyme A reductase Recombinant Protein | HMGCR recombinant protein

Recombinant Human 3-hydroxy-3-methylglutaryl-coenzyme A reductase

Cat. Num. AAA947962

• Gene Names: HMGCR; LDLCQ3
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: 3-hydroxy-3-methylglutaryl-coenzyme A reductase; Recombinant Human 3-hydroxy-3-methylglutaryl-coenzyme A reductase; HMGCR recombinant protein

• Host: E Coli or Yeast or Baculovirus or Mammalian Cell
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Lyophilized or liquid (Format to be determined during the manufacturing process)
• Sequence Positions: 588-887aa; Partial
• Sequence: MTRGPVVRLPRACDSAEVKAWLETSEGFAVIKEAFDSTSRFARLQKLHTSIAGRNLYIRFQSRSGDAMGMNMISKGTEKALSKLHEYFPEMQILAVSGNYCTDKKPAAINWIEGRGKSVVCEAVIPAKVVREVLKTTTEAMIEVNINKNLVGSAMAGSIGGYNAHAANIVTAIYIACGQDAAQNVGSSNCITLMEASGPTNEDLYISCTMPSIEIGTVGGGTNLLPQQACLQMLGVQGACKDNPGENARQLARIVCGTVMAGELSLMAALAAGHLVKSHMIHNRSKINLQDLQGACTKKT

• Production Note: Special Offer: The E Coli host-expressed protein is manufactured from a stock plasmid containing the protein gene. E Colihost-expressed protein is stocked in different unit sizes ranging from as small as 10 ug to as large as 1 mg. Bulk inventory is also available. The E Coli host-expressed protein has been ordered over and over again by researchers and has stood the test of time as both a robust protein and important target for the research community. It is part of our new program to make our most popular protein targets and corresponding hosts available in expanded unit sizes and with a quick processing time. Select E Coli host-expressed protein for the fastest delivery among all hosts. Please contact our technical support team or email to [email protected] for more details.
• Preparation and Storage: Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

SDS-Page

Related Product Information for HMGCR recombinant protein

Transmembrane glycoprotein that is the rate-limiting enzyme in cholesterol biosynthesis as well as in the biosynthesis of nonsterol isoprenoids that are essential for normal cell function including ubiquinone and geranylgeranyl proteins.

Product Categories/Family for HMGCR recombinant protein

Metabolism

References

Human 3-hydroxy-3-methylglutaryl coenzyme A reductase. Conserved domains responsible for catalytic activity and sterol-regulated degradation.Luskey K.L., Stevens B.J. Biol. Chem. 260:10271-10277(1985) Human HMG-CoA reductase gene.Nakajima T., Iwaki K., Hamakubo T., Kodama T., Emi M.Rieder M.J., da Ponte S.H., Kuldanek S.A., Rajkumar N., Smith J.D., Toth E.J., Nickerson D.A.Complete sequencing and characterization of 21,243 full-length human cDNAs.Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.Nat. Genet. 36:40-45(2004) The DNA sequence and comparative analysis of human chromosome 5.Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S., Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.Nature 431:268-274(2004) Multivalent feedback regulation of HMG CoA reductase, a control mechanism coordinating isoprenoid synthesis and cell growth.Brown M.S., Goldstein J.L.J. Lipid Res. 21:505-517(1980) Accelerated degradation of HMG CoA reductase mediated by binding of insig-1 to its sterol-sensing domain.Sever N., Yang T., Brown M.S., Goldstein J.L., DeBose-Boyd R.A.Mol. Cell 11:25-33(2003) Dislocation of HMG-CoA reductase and Insig-1, two polytopic endoplasmic reticulum proteins, en route to proteasomal degradation.Leichner G.S., Avner R., Harats D., Roitelman J.Mol. Biol. Cell 20:3330-3341(2009) Metabolically regulated endoplasmic reticulum-associated degradation of 3-hydroxy-3-methylglutaryl-CoA reductase evidence for requirement of a geranylgeranylated protein.Leichner G.S., Avner R., Harats D., Roitelman J.J. Biol. Chem. 286:32150-32161(2011) A novel 3-hydroxy-3-methylglutaryl-coenzyme A reductase (HMGCR) splice variant with an alternative exon 1 potentially encoding an extended N-terminus.Stormo C., Kringen M.K., Grimholt R.M., Berg J.P., Piehler A.P.BMC Mol. Biol. 13:29-29(2012) The UBIAD1 prenyltransferase links menaquione-4 synthesis to cholesterol metabolic enzymes.Nickerson M.L., Bosley A.D., Weiss J.S., Kostiha B.N., Hirota Y., Brandt W., Esposito D., Kinoshita S., Wessjohann L., Morham S.G., Andresson T., Kruth H.S., Okano T., Dean M.Hum. Mutat. 34:317-329(2013) An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.J. Proteomics 96:253-262(2014) Crystal structure of the catalytic portion of human HMG-CoA reductase insights into regulation of activity and catalysis.Istvan E.S., Palnitkar M., Buchanan S.K., Deisenhofer J.EMBO J. 19:819-830(2000) Structural mechanism for statin inhibition of HMG-CoA reductase.Istvan E.S., Deisenhofer J.Science 292:1160-1164(2001) Thermodynamic and structure guided design of statin based inhibitors of 3-hydroxy-3-methylglutaryl coenzyme A reductase.Sarver R.W., Bills E., Bolton G., Bratton L.D., Caspers N.L., Dunbar J.B., Harris M.S., Hutchings R.H., Kennedy R.M., Larsen S.D., Pavlovsky A., Pfefferkorn J.A., Bainbridge G.J. Med. Chem. 51:3804-3813(2008) Characterization of single-nucleotide polymorphisms in coding regions of human genes.Cargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S.Nat. Genet. 22:231-238(1999) ErratumCargill M., Altshuler D., Ireland J., Sklar P., Ardlie K., Patil N., Shaw N., Lane C.R., Lim E.P., Kalyanaraman N., Nemesh J., Ziaugra L., Friedland L., Rolfe A., Warrington J., Lipshutz R., Daley G.Q., Lander E.S.Nat. Genet. 23:373-373(1999)

NCBI and Uniprot Product Information

• NCBI GI #: 4557643
• NCBI GeneID: 3156
• NCBI Accession #: NP_000850.1
• NCBI GenBank Nucleotide #: NM_000859.2
• UniProt Accession #: P04035; Q8N190; B7Z3Y9
• Molecular Weight: 36 kDa
• NCBI Official Full Name: 3-hydroxy-3-methylglutaryl-Coenzyme A reductase isoform 1
• NCBI Official Synonym Full Names: 3-hydroxy-3-methylglutaryl-CoA reductase
• NCBI Official Symbol: HMGCR
• NCBI Official Synonym Symbols: LDLCQ3
• NCBI Protein Information: 3-hydroxy-3-methylglutaryl-Coenzyme A reductase
• UniProt Protein Name: 3-hydroxy-3-methylglutaryl-coenzyme A reductase
• Protein Family: 3-hydroxy-3-methylglutaryl-coenzyme A reductase
• UniProt Gene Name: HMGCR
• UniProt Synonym Gene Names: HMG-CoA reductase
• UniProt Entry Name: HMDH_HUMAN

NCBI Description

HMG-CoA reductase is the rate-limiting enzyme for cholesterol synthesis and is regulated via a negative feedback mechanism mediated by sterols and non-sterol metabolites derived from mevalonate, the product of the reaction catalyzed by reductase. Normally in mammalian cells this enzyme is suppressed by cholesterol derived from the internalization and degradation of low density lipoprotein (LDL) via the LDL receptor. Competitive inhibitors of the reductase induce the expression of LDL receptors in the liver, which in turn increases the catabolism of plasma LDL and lowers the plasma concentration of cholesterol, an important determinant of atherosclerosis. Alternatively spliced transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Aug 2008]

Uniprot Description

HMGCR: the rate-limiting enzyme for cholesterol synthesis. Regulated via a negative feedback mechanism mediated by sterols and non-sterol metabolites derived from mevalonate, the product of the reaction catalyzed by this reductase. Normally in mammalian cells this enzyme is suppressed by cholesterol derived from the internalization and degradation of low density lipoprotein (LDL) via the LDL receptor. Competitive inhibitors of the reductase induce the expression of LDL receptors in the liver, which in turn increases the catabolism of plasma LDL and lowers the plasma concentration of cholesterol, an important determinant of atherosclerosis.

Protein type: Membrane protein, integral; EC 1.1.1.34; Membrane protein, multi-pass; Secondary Metabolites Metabolism - terpenoid backbone biosynthesis; Endoplasmic reticulum; Oxidoreductase; Motility/polarity/chemotaxis

Chromosomal Location of Human Ortholog: 5q13.3-q14

Cellular Component: endoplasmic reticulum; endoplasmic reticulum membrane; integral to membrane; peroxisomal membrane

Molecular Function: coenzyme binding; hydroxymethylglutaryl-CoA reductase (NADPH) activity; hydroxymethylglutaryl-CoA reductase activity; protein binding; protein homodimerization activity; protein phosphatase 2A binding

Biological Process: aging; cellular lipid metabolic process; cholesterol biosynthetic process; coenzyme A metabolic process; isoprenoid biosynthetic process; myoblast differentiation; negative regulation of MAP kinase activity; negative regulation of vasodilation; positive regulation of skeletal muscle development; positive regulation of smooth muscle cell proliferation; positive regulation of stress-activated MAPK cascade; protein tetramerization; response to ethanol; response to nutrient; ubiquinone metabolic process; visual learning