Glutathione peroxidase 1 Recombinant Protein | GPX1 recombinant protein

Recombinant Human Glutathione peroxidase 1

• Gene Names: GPX1; GPXD; GSHPX1
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Glutathione peroxidase 1; Recombinant Human Glutathione peroxidase 1; Cellular glutathione peroxidase; GPX1 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: 1-203
• Sequence: MCAARLAAAAAAAQSVYAFSARPLAGGEPVSLGSLRGKVLLIENVASLSGTTVRDYTQMNELQRRLGPRGLVVLGFPCNQFGHQENAKNEEILNSLKYVRPGGGFEPNFMLFEKCEVNGAGAHPLFAFLREALPAPSDDATALMTDPKLITWSPVCRNDVAWNFEKFLVGPDGVPLRRYSRRFQTIDIEPDIEALLSQGPSCA
• Sequence Length: 203

• 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 GPX1 recombinant protein

Protects the hoglobin in erythrocytes from oxidative breakdown.

Product Categories/Family for GPX1 recombinant protein

Cancer

References

cDNA sequence coding for human glutathione peroxidase.Sukenaga Y., Ishida K., Takeda T., Takagi K.Nucleic Acids Res. 15:7178-7178(1987) Nucleotide sequence of a human gene for glutathione peroxidase.Ishida K., Morino T., Takagi K., Sukenaga Y.Nucleic Acids Res. 15:10051-10051(1987) Sequence of a cDNA coding for human glutathione peroxidase confirms TGA encodes active site selenocysteine.Mullenbach G.T., Tabrizi A., Irvine B.D., Bell G.I., Hallewell R.A.Nucleic Acids Res. 15:5484-5484(1987) Isolation and chromosomal localization of the human glutathione peroxidase gene.Chada S., le Beau M.M., Casey L., Newburger P.E.Genomics 6:268-271(1990) Structure and function of the 5'-flanking sequence of the human cytosolic selenium-dependent glutathione peroxidase gene (hgpx1) .Moscow J.A., Morrow C.S., He R., Mullenbach G.T., Cowan K.H.J. Biol. Chem. 267:5949-5958(1992) NIEHS SNPs programThe DNA sequence, annotation and analysis of human chromosome 3.Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.Nature 440:1194-1198(2006) Initial characterization of the human central proteome.Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.BMC Syst. Biol. 5:17-17(2011) 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 selenocysteine to glycine mutant of human glutathione peroxidase 1.Structural genomics consortium (SGC) Submitted (FEB-2009) to the PDB data bankLow yield of polymorphisms from EST blast searching analysis of genes related to oxidative stress and verification of the P197L polymorphism in GPX1.Forsberg L., de Faire U., Morgenstern R.3.0.CO;2-5>Hum. Mutat. 13:294-300(1999) Association between the GCG polymorphism of the selenium dependent GPX1 gene and the risk of young onset prostate cancer.Kote-Jarai Z., Durocher F., Edwards S.M., Hamoudi R., Jackson R.A., Ardern-Jones A., Murkin A., Dearnaley D.P., Kirby R., Houlston R., Easton D.F., Eeles R.Prostate Cancer Prostatic Dis. 5:189-192(2002) Functional variants in the glutathione peroxidase-1 (GPx-1) gene are associated with increased intima-media thickness of carotid arteries and risk of macrovascular diseases in Japanese type 2 diabetic patients.Hamanishi T., Furuta H., Kato H., Doi A., Tamai M., Shimomura H., Sakagashira S., Nishi M., Sasaki H., Sanke T., Nanjo K.Diabetes 53:2455-2460(2004) Increased risk of bladder cancer associated with a glutathione peroxidase 1 codon 198 variant.Ichimura Y., Habuchi T., Tsuchiya N., Wang L., Oyama C., Sato K., Nishiyama H., Ogawa O., Kato T.J. Urol. 172:728-732(2004)

NCBI and Uniprot Product Information

• NCBI GI #: 41406084
• NCBI GeneID: 2876
• NCBI Accession #: NP_000572.2
• NCBI GenBank Nucleotide #: NM_000581.2
• UniProt Accession #: P07203; Q7Z5H1; Q9BW12; E9PAS1
• Molecular Weight: 38kD
• NCBI Official Full Name: glutathione peroxidase 1 isoform 1
• NCBI Official Synonym Full Names: glutathione peroxidase 1
• NCBI Official Symbol: GPX1
• NCBI Official Synonym Symbols: GPXD; GSHPX1
• NCBI Protein Information: glutathione peroxidase 1
• UniProt Protein Name: Glutathione peroxidase 1
• Protein Family: Glutathione peroxidase
• UniProt Gene Name: GPX1
• UniProt Synonym Gene Names: GPx-1; GSHPx-1
• UniProt Entry Name: GPX1_HUMAN

NCBI Description

This gene encodes a member of the glutathione peroxidase family. Glutathione peroxidase functions in the detoxification of hydrogen peroxide, and is one of the most important antioxidant enzymes in humans. This protein is one of only a few proteins known in higher vertebrates to contain selenocysteine, which occurs at the active site of glutathione peroxidase and is coded by UGA, that normally functions as a translation termination codon. In addition, this protein is characterized in a polyalanine sequence polymorphism in the N-terminal region, which includes three alleles with five, six or seven alanine (ALA) repeats in this sequence. The allele with five ALA repeats is significantly associated with breast cancer risk. Two alternatively spliced transcript variants encoding distinct isoforms have been found for this gene. [provided by RefSeq, Jul 2008]

Uniprot Description

GPX1: Protects the hemoglobin in erythrocytes from oxidative breakdown. Homotetramer. Interacts with MIEN1. Belongs to the glutathione peroxidase family.

Protein type: Lipid Metabolism - arachidonic acid; EC 1.11.1.9; Other Amino Acids Metabolism - glutathione; Oxidoreductase

Chromosomal Location of Human Ortholog: 3p21.3

Cellular Component: cytoplasm; cytosol; mitochondrial matrix; mitochondrion

Molecular Function: glutathione peroxidase activity; SH3 domain binding

Biological Process: angiogenesis involved in wound healing; arachidonic acid metabolic process; blood vessel endothelial cell migration; cell redox homeostasis; endothelial cell development; fat cell differentiation; glutathione metabolic process; heart contraction; hydrogen peroxide catabolic process; induction of apoptosis by oxidative stress; interaction with symbiont; lipoxygenase pathway; myoblast proliferation; negative regulation of caspase activity; negative regulation of inflammatory response to antigenic stimulus; nucleobase, nucleoside and nucleotide metabolic process; positive regulation of protein kinase B signaling cascade; protein amino acid oxidation; purine base metabolic process; purine nucleotide catabolic process; regulation of gene expression, epigenetic; regulation of mammary gland epithelial cell proliferation; regulation of neuron apoptosis; response to gamma radiation; response to hydrogen peroxide; response to hydroperoxide; response to reactive oxygen species; response to selenium ion; response to symbiotic bacterium; response to xenobiotic stimulus; sensory perception of sound; skeletal muscle fiber development; skeletal muscle regeneration; thermoregulation; triacylglycerol metabolic process; UV protection; vasodilation

Disease: Glutathione Peroxidase Deficiency