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

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Catalog # MBS947962
Unit / Price
Scan QR to view Datasheet
  0.01 mg (E-Coli)  /  $160 +1 FREE 8GB USB
  0.05 mg (E-Coli)  /  $200 +1 FREE 8GB USB
  0.1 mg (E-Coli)  /  $295 +1 FREE 8GB USB
  0.2 mg (E-Coli)  /  $480 +1 FREE 8GB USB
  0.5 mg (E-Coli)  /  $790 +1 FREE 8GB USB
  1 mg (E-Coli)  /  $1,215 +1 FREE 8GB USB
SDS-Page
Product Name

3-hydroxy-3-methylglutaryl-coenzyme A reductase (HMGCR), Recombinant Protein

Popular Item
Full Product Name

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

Research Use Only
For Research Use Only. Not for use in diagnostic procedures.
Sequence Positions
588-887aa; Partial
Sequence
MTRGPVVRLP RACDSAEVKA WLETSEGFAV IKEAFDSTSR FARLQKLHTS IAGRNLYIRF QSRSGDAMGM NMISKGTEKA LSKLHEYFPE MQILAVSGNY CTDKKPAAIN WIEGRGKSVV CEAVIPAKVV REVLKTTTEA MIEVNINKNL VGSAMAGSIG GYNAHAANIV TAIYIACGQD AAQNVGSSNC ITLMEASGPT NEDLYISCTM PSIEIGTVGG GTNLLPQQAC LQMLGVQGAC KDNPGENARQ LARIVCGTVM AGELSLMAAL AAGHLVKSHM IHNRSKINLQ DLQGACTKKT
OMIM
142910
3D Structure
ModBase 3D Structure for P04035
Host
E Coli or Yeast or Baculovirus or Mammalian Cell
Purity/Purification
Greater than 90% as determined by SDS-PAGE. (lot specific)
Form/Format
Liquid containing glycerol
Tag Information
This protein contains an N-terminal tag and may also contain a C-terminal tag. Tag types are determined by various factors including tag-protein stability, please inquire for tag information.
Sterility
Sterile filter available upon request.
Endotoxin
Low endotoxin available upon request.
Preparation and Storage
Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.
ISO Certification
Manufactured in an ISO 9001:2008 Certified Laboratory.
Other Notes
Small volumes of HMGCR recombinant protein vial(s) may occasionally become entrapped in the seal of the product vial during shipment and storage. If necessary, briefly centrifuge the vial on a tabletop centrifuge to dislodge any liquid in the container`s cap. Certain products may require to ship with dry ice and additional dry ice fee may apply.
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

HMGCR recombinant protein SDS-Page image
(Note: Representative image, actual molecular weight may vary depending on Tag type and expression host)
NCBI/Uniprot data below describe general gene information for HMGCR. It may not necessarily be applicable to this product.
NCBI GI #
NCBI GeneID
NCBI Accession #
NCBI GenBank Nucleotide #
UniProt Primary Accession #
UniProt Secondary Accession #
UniProt Related Accession #
Molecular Weight
36.1kD
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  [Similar Products]
NCBI Official Synonym Symbols
LDLCQ3
  [Similar Products]
NCBI Protein Information
3-hydroxy-3-methylglutaryl-Coenzyme A reductase
UniProt Protein Name
3-hydroxy-3-methylglutaryl-coenzyme A reductase
UniProt Gene Name
HMGCR  [Similar Products]
UniProt Synonym Gene Names
HMG-CoA reductase  [Similar Products]
UniProt Entry Name
HMDH_HUMAN
NCBI Summary for HMGCR
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 Comments for HMGCR
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
Product References and Citations for HMGCR recombinant protein
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)

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