Glucose-6-phosphate isomerase Recombinant Protein | GPI recombinant protein

Recombinant Human Glucose-6-phosphate isomerase

Cat. Num. AAA15945

• Gene Names: GPI; AMF; NLK; PGI; PHI; GNPI; SA36; SA-36
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Glucose-6-phosphate isomerase; N/A; Recombinant Human Glucose-6-phosphate isomerase; Autocrine motility factor; AMF; Neuroleukin; NLK; Phosphoglucose isomerase; PGI; Phosphohexose isomerase; PHI; Sperm antigen 36; SA-36; GPI recombinant protein

• Host: E Coli
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Liquid containing glycerol
• Sequence Positions: 2-554aa; Partial
• Sequence: AALTRDPQFQKLQQWYREHRSELNLRRLFDANKDRFNHFSLTLNTNHGHILVDYSKNLVTEDVMRMLVDLAKSRGVEAARERMFNGEKINYTEGRAVLHVALRNRSNTPILVDGKDVMPEVNKVLDKMKSFCQRVRSGDWKGYTGKTITDVINIGIGGSDLGPLMVTEALKPYSSGGPRVWYVSNIDGTHIAKTLAQLNPESSLFIIASKTFTTQETITNAETAKEWFLQAAKDPSAVAKHFVALSTNTTKVKEFGIDPQNMFEFWDWVGGRYSLWSAIGLSIALHVGFDNFEQLLSGAHWMDQHFRTTPLEKNAPVLLALLGIWYINCFGCETHAMLPYDQYLHRFAAYFQQGDMESNGKYITKSGTRVDHQTGPIVWGEPGTNGQHAFYQLIHQGTKMIPCDFLIPVQTQHPIRKGLHHKILLANFLAQTEALMRGKSTEEARKELQAAGKSPEDLERLLPHKVFEGNRPTNSIVFTKLTPFMLGALVAMYEHKIFVQGIIWDINSFDQWGVELGKQLAKKIEPELDGSAQVTSHDASTNGLINFIKQQRE

• 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 GPI recombinant protein

Besides it's role as a glycolytic enzyme, mammalian GPI can function as a tumor-secreted cytokine and an angiogenic factor (AMF) that stimulates endothelial cell motility. GPI is also a neurotrophic factor (Neuroleukin) for spinal and sensory neurons.

Product Categories/Family for GPI recombinant protein

Signal Transduction

References

Gurney M.E.Cloning of a glucose phosphate isomerase/neuroleukin-like sperm antigen involved in sperm agglutination.Yakirevich E., Naot Y.Biol. Reprod. 62:1016-1023(2000) NIEHS SNPs programComplete 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 biology of human chromosome 19.Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.Nature 428:529-535(2004) Characterization of the 5' end of the gene for human glucose phosphate isomerase (GPI) .Walker J.I.H., Faik P., Morgan M.J.Genomics 7:638-643(1990) Bienvenut W.V.Submitted (OCT-2004) to UniProtKB Mouse glucose-6-phosphate isomerase and neuroleukin have identical 3' sequences.Faik P., Walker J.I.H., Redmill A.A.M., Morgan M.J.Nature 332:455-456(1988) Phosphohexose isomerase/autocrine motility factor/neuroleukin/maturation factor is a multifunctional phosphoprotein.Haga A., Niinaka Y., Raz A.Biochim. Biophys. Acta 1480:235-244(2000) Tumor autocrine motility factor is an angiogenic factor that stimulates endothelial cell motility.Funasaka T., Haga A., Raz A., Nagase H.Biochem. Biophys. Res. Commun. 285:118-128(2001) Species specificity of the cytokine function of phosphoglucose isomerase.Amraei M., Nabi I.R.FEBS Lett. 525:151-155(2002) Proteomic identification of proteins conjugated to ISG15 in mouse and human cells.Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J., Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E.Biochem. Biophys. Res. Commun. 336:496-506(2005) Differential regulation of phosphoglucose isomerase/autocrine motility factor activities by protein kinase CK2 phosphorylation.Yanagawa T., Funasaka T., Tsutsumi S., Raz T., Tanaka N., Raz A.J. Biol. Chem. 280:10419-10426(2005) A quantitative atlas of mitotic phosphorylation.Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.Anal. Chem. 81:4493-4501(2009) Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.Sci. Signal. 2:RA46-RA46(2009) Lysine acetylation targets protein complexes and co-regulates major cellular functions.Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.Science 325:834-840(2009) 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) The first identification of lysine malonylation substrates and its regulatory enzyme.Peng C., Lu Z., Xie Z., Cheng Z., Chen Y., Tan M., Luo H., Zhang Y., He W., Yang K., Zwaans B.M., Tishkoff D., Ho L., Lombard D., He T.C., Dai J., Verdin E., Ye Y., Zhao Y.Mol. Cell. Proteomics 10:M111.012658.01-M111.012658.12(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) The crystal structure of human phosphoglucose isomerase at 1.6 A resolution implications for catalytic mechanism, cytokine activity and haemolytic anaemia.Read J., Pearce J., Li X., Muirhead H., Chirgwin J., Davies C.J. Mol. Biol. 309:447-463(2001) Inhibition mechanism of cytokine activity of human autocrine motility factor examined by crystal structure analyses and site-directed mutagenesis studies.Tanaka N., Haga A., Uemura H., Akiyama H., Funasaka T., Nagase H., Raz A., Nakamura K.T.J. Mol. Biol. 318:985-997(2002) The structure of human phosphoglucose isomerase complexed with a transition-state analogue.Davies C., Muirhead H., Chirgwin J.Acta Crystallogr. D 59:1111-1113(2003) Crystal structure of human phosphoglucose isomerase and analysis of the initial catalytic steps.Cordeiro A.T., Godoi P.H., Silva C.H., Garratt R.C., Oliva G., Thiemann O.H.Biochim. Biophys. Acta 1645:117-122(2003) DNA sequence abnormalities in human glucose 6-phosphate isomerase deficiency.Walker J.I.H., Layton D.M., Bellingham A.J., Morgan M.J., Faik P.Hum. Mol. Genet. 2:327-329(1993) The characterization of gene mutations for human glucose phosphate isomerase deficiency associated with chronic hemolytic anemia.Xu W., Beutler E.J. Clin. Invest. 94:2326-2329(1994) Study of the molecular defects in glucose phosphate isomerase-deficient patients affected by chronic hemolytic anemia.Baronciani L., Zanella A., Bianchi P., Zappa M., Alfinito F., Iolascon A., Tannoia N., Beutler E., Sirchia G.Blood 88:2306-2310(1996) Molecular analysis of glucose phosphate isomerase deficiency associated with hereditary hemolytic anemia.Kanno H., Fujii H., Hirono A., Ishida Y., Ohga S., Fukumoto Y., Matsuzawa K., Ogawa S., Miwa S.Blood 88:2321-2325(1996) Glucosephosphate isomerase (GPI) deficiency mutations associated with hereditary nonspherocytic hemolytic anemia (HNSHA) .Beutler E., West C., Britton H.A., Harris J., Forman L.Blood Cells Mol. Dis. 23:402-409(1997) Molecular basis of neurological dysfunction coupled with haemolytic anaemia in human glucose-6-phosphate isomerase (GPI) deficiency.Kugler W., Breme K., Laspe P., Muirhead H., Davies C., Winkler H., Schroter W., Lakomek M.Hum. Genet. 103:450-454(1998) +Additional computationally mapped references.<p>Provides general information on the entry.

NCBI and Uniprot Product Information

• NCBI GI #: 18201905
• NCBI GeneID: 2821
• NCBI Accession #: NP_000166.2
• NCBI GenBank Nucleotide #: NM_000175.3
• UniProt Accession #: P06744; Q9BRD3; Q9BSK5; Q9UHE6; B4DG39
• Molecular Weight: 66.6 kDa
• NCBI Official Full Name: glucose-6-phosphate isomerase isoform 2
• NCBI Official Synonym Full Names: glucose-6-phosphate isomerase
• NCBI Official Symbol: GPI
• NCBI Official Synonym Symbols: AMF; NLK; PGI; PHI; GNPI; SA36; SA-36
• NCBI Protein Information: glucose-6-phosphate isomerase
• UniProt Protein Name: Glucose-6-phosphate isomerase
• UniProt Gene Name: GPI
• UniProt Synonym Gene Names: GPI; AMF; NLK; PGI; PHI; SA-36
• UniProt Entry Name: G6PI_HUMAN