protein

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

MBS947962

0.05 mg (E-Coli)

190 USD

Recombinant Protein

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

3-hydroxy-3-methylglutaryl-coenzyme A reductase

3-hydroxy-3-methylglutaryl-Coenzyme A reductase isoform 1; 3-hydroxy-3-methylglutaryl-coenzyme A reductase; 3-hydroxy-3-methylglutaryl-Coenzyme A reductase; 3-hydroxy-3-methylglutaryl-CoA reductase

HMGCR

HMGCR; HMGCR; LDLCQ3; HMG-CoA reductase

HMDH_HUMAN

E Coli or Yeast or Baculovirus or Mammalian Cell

588-887, Partial.

887

MTRGPVVRLPRACDSAEVKAWLETSEGFAVIKEAFDSTS
RFARLQKLHTSIAGRNLYIRFQSRSGDAMGMNMISKGTE
KALSKLHEYFPEMQILAVSGNYCTDKKPAAINWIEGRGK
SVVCEAVIPAKVVREVLKTTTEAMIEVNINKNLVGSAMA
GSIGGYNAHAANIVTAIYIACGQDAAQNVGSSNCITLME
ASGPTNEDLYISCTMPSIEIGTVGGGTNLLPQQACLQML
GVQGACKDNPGENARQLARIVCGTVMAGELSLMAALAAG
HLVKSHMIHNRSKINLQDLQGACTKKT

Greater than 90% as determined by SDS-PAGE.

Liquid containing glycerol; lyophilization may be available upon request.

Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

Metabolism

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.

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)

4557643

NP_000850.1

NM_000859.2

P04035

36.1kD

AMPK Signaling Pathway (198868); AMPK Signaling Pathway (989139); AMPK Signaling Pathway (992181); Activation Of Gene Expression By SREBF (SREBP) Pathway (1270039); Bile Secretion Pathway (193146); Bile Secretion Pathway (193095); C5 Isoprenoid Biosynthesis, Mevalonate Pathway (413387); C5 Isoprenoid Biosynthesis, Mevalonate Pathway (468288); Cholesterol Biosynthesis Pathway (198809); Cholesterol Biosynthesis Pathway (1270037)

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]

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

0.05 mg (E-Coli)

190 USD

0.2 mg (E-Coli)

460

0.5 mg (E-Coli)

750

0.05 mg (Baculovirus)

950

0.05 mg (Mammalian-Cell)

1170