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

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

Cat. Num. AAA18405

• 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

• 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

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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. 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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
• UniProt Gene Name: HMGCR
• UniProt Synonym Gene Names: HMG-CoA reductase
• UniProt Entry Name: HMDH_HUMAN