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3-Hydroxy-3-Methylglutaryl-Coenzyme A Reductase (HMGCR) Human Recombinant Protein

For Research Use Only. Not for use in diagnostic procedures. Catalog #: MBS947962

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. More details

$275 / 0.02 mg (E-Coli) +1 FREE 8GB USB
Product Documentation
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Sample Manual Insert View PDF
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Testing Data View PDF
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Certificate of Analysis (COA) View PDF
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QC Report View PDF
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Material Safety Data Sheet View PDF
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Technical Datasheet View PDF
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Protocol View PDF

Product Overview

Online Datasheet in PDF
Product Name
3-hydroxy-3-methylglutaryl-coenzyme A reductase (HMGCR), Recombinant Protein
Full Product Name
Recombinant Human 3-hydroxy-3-methylglutaryl-coenzyme A reductase
Product Gene Name
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
Host
E Coli or Yeast or Baculovirus or Mammalian Cell
Form/Format
Lyophilized or liquid (Format to be determined during the manufacturing process)
Purity/Purification
Greater or equal to 85% purity as determined by SDS-PAGE. (lot specific)
Preparation and Storage
Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.
Molecular Weight
36 kDa
Sequence Positions
588-887aa; partial
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.
OMIM
142910
3D Structure
ModBase 3D Structure for P04035
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 support@mybiosource.com for more details.

Product Categories/Family for HMGCR recombinant protein

ISO Certification
Manufactured in an ISO 9001:2015 Certified Laboratory.

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)

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.

Searchable Terms for HMGCR purchase

MBS947962 is a recombinant protein targeting HMGCR. Also known as Recombinant Human 3-hydroxy-3-methylglutaryl-coenzyme A reductase. Host: E Coli or Yeast or Baculovirus or Mammalian Cell.

Additional Details

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 #
UniProt Primary Accession #
UniProt Secondary Accession #
UniProt Related Accession #
GenBank Nucleotide #
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
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
NCBI Protein Information
3-hydroxy-3-methylglutaryl-Coenzyme A reductase

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]
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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
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Precautions

All of MyBioSource's Products are for scientific laboratory research purposes and are not for diagnostic, therapeutics, prophylactic or in vivo use. Through your purchase, you expressly represent and warrant to MyBioSource that you will properly test and use any Products purchased from MyBioSource in accordance with industry standards. MyBioSource and its authorized distributors reserve the right to refuse to process any order where we reasonably believe that the intended use will fall outside of our acceptable guidelines.

Disclaimer

While every efforts were made to ensure the accuracy of the information provided in this datasheet, MyBioSource will not be liable for any omissions or errors contained herein. MyBioSource reserves the right to make changes to this datasheet at any time without prior notice.

It is the responsibility of the customer to report product performance issues to MyBioSource within 30 days of receipt of the product. Please visit our Terms & Conditions page for more information.

Product Note

Select online data sheet information is drawn from bioinformatics databases, occasionally resulting in ambiguous or non-relevant product information. It is the responsibility of the customer to review, verify, and evaluate the information to make sure it matches their requirements before purchasing the kit. Our ELISA Kit assays are dynamic research tools and sometimes they may be updated and improved. If the format of this assay is important to you then please request the current manual or contact our technical support team with a presales inquiry before placing an order. We will confirm the current details of the assay. We cannot guarantee the sample manual posted online is the most current manual, it is intended to serve as an example only. Please refer to the instructions For Use provided with the assay kit for precise details.

Product PubMed Publications

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