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Glucose-6-Phosphate Isomerase (GPI) Human Recombinant Protein

For Research Use Only. Not for use in diagnostic procedures. Special Promotion Catalog #: MBS719369
PROMOTIONAL PRICING: 10% OFF web price. Discount is not applicable for bulk pricing such as 5x96T or 10x96T. Discount will be applied after order has been placed

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. 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
Glucose-6-phosphate isomerase (GPI), Recombinant Protein
Full Product Name
Recombinant Human Glucose-6-phosphate isomerase
Product Gene Name
Product Synonym Names
Autocrine motility factor; AMF; Neuroleukin; NLK; Phosphoglucose isomerase; PGI; Phosphohexose isomerase; PHI; Sperm antigen 36; SA-36
Sequence
AALTRDPQFQ KLQQWYREHR SELNLRRLFD ANKDRFNHFS LTLNTNHGHI LVDYSKNLVT EDVMRMLVDL AKSRGVEAAR ERMFNGEKIN YTEGRAVLHV ALRNRSNTPI LVDGKDVMPE VNKVLDKMKS FCQRVRSGDW KGYTGKTITD VINIGIGGSD LGPLMVTEAL KPYSSGGPRV WYVSNIDGTH IAKTLAQLNP ESSLFIIASK TFTTQETITN AETAKEWFLQ AAKDPSAVAK HFVALSTNTT KVKEFGIDPQ NMFEFWDWVG GRYSLWSAIG LSIALHVGFD NFEQLLSGAH WMDQHFRTTP LEKNAPVLLA LLGIWYINCF GCETHAMLPY DQYLHRFAAY FQQGDMESNG KYITKSGTRV DHQTGPIVWG EPGTNGQHAF YQLIHQGTKM IPCDFLIPVQ TQHPIRKGLH HKILLANFLA QTEALMRGKS TEEARKELQA AGKSPEDLER LLPHKVFEGN RPTNSIVFTK LTPFMLGALV AMYEHKIFVQ GIIWDINSFD QWGVELGKQL AKKIEPELDG SAQVTSHDAS TNGLINFIKQ QRE
Host
E Coli or Yeast or Baculovirus or Mammalian Cell
Form/Format
Liquid or Lyophilized powder
If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol.If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.
Purity/Purification
Greater than 85% as determined by SDS-PAGE. (lot specific)
Preparation and Storage
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself. Generally, the shelf life of liquid form is 6 months at -20 degree C/-80 degree C. The shelf life of lyophilized form is 12 months at -20 degree C/-80 degree C.
Repeated freezing and thawing is not recommended. Store working aliquots at 4 degree C for up to one week.
Molecular Weight
66.6 kDa
Sequence Positions
2-554aa, 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
172400
3D Structure
ModBase 3D Structure for P06744
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 GPI recombinant protein

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

Product References and Citations for GPI recombinant protein

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.

Other Notes

Small volumes of GPI 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 GPI purchase

MBS719369 is a recombinant protein targeting GPI. Also known as Recombinant Human Glucose-6-phosphate isomerase. Host: E Coli or Yeast or Baculovirus or Mammalian Cell.

Additional Details

NCBI/Uniprot data below describe general gene information for GPI. 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
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
UniProt Protein Name
Glucose-6-phosphate isomerase
UniProt Synonym Protein Names
Autocrine motility factor; AMF; Neuroleukin; NLK; Phosphoglucose isomerase; PGI; Phosphohexose isomerase; PHI; Sperm antigen 36; SA-36
UniProt Gene Name
GPI
UniProt Synonym Gene Names
GPI; AMF; NLK; PGI; PHI; SA-36
UniProt Entry Name
G6PI_HUMAN
NCBI Protein Information
glucose-6-phosphate isomerase

NCBI Summary for GPI

This gene encodes a member of the glucose phosphate isomerase protein family. The encoded protein has been identified as a moonlighting protein based on its ability to perform mechanistically distinct functions. In the cytoplasm, the gene product functions as a glycolytic enzyme (glucose-6-phosphate isomerase) that interconverts glucose-6-phophsate and fructose-6-phosphate. Extracellularly, the encoded protein (also referred to as neuroleukin) functions as a neurotrophic factor that promotes survival of skeletal motor neurons and sensory neurons, and as a lymphokine that induces immunoglobulin secretion. The encoded protein is also referred to as autocrine motility factor based on an additional function as a tumor-secreted cytokine and angiogenic factor. Defects in this gene are the cause of nonspherocytic hemolytic anemia and a severe enzyme deficiency can be associated with hydrops fetalis, immediate neonatal death and neurological impairment. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jan 2014]
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UniProt Comments for GPI

G6PI: belongs to the GPI family whose members encode multifunctional phosphoglucose isomerase proteins involved in energy pathways. A dimeric enzyme that catalyzes the reversible isomerization of glucose-6-phosphate and fructose-6-phosphate. Functions in different capacities inside and outside the cell. In the cytoplasm, the gene product is involved in glycolysis and gluconeogenesis, while outside the cell it functions as a neurotrophic factor for spinal and sensory neurons. Defects in this gene are the cause of nonspherocytic hemolytic anemia and a severe enzyme deficiency can be associated with hydrops fetalis, immediate neonatal death and neurological impairment.

Protein type: Apoptosis; Cytokine; EC 5.3.1.9; Carbohydrate Metabolism - amino sugar and nucleotide sugar; Carbohydrate Metabolism - pentose phosphate pathway; Carbohydrate Metabolism - starch and sucrose; Carbohydrate Metabolism - glycolysis and gluconeogenesis; Isomerase

Chromosomal Location of Human Ortholog: 19q13.1

Cellular Component: cytoplasm; cytosol; extracellular space; membrane; neuron projection; nucleoplasm; plasma membrane

Molecular Function: cytokine activity; glucose-6-phosphate isomerase activity; growth factor activity; intramolecular transferase activity; monosaccharide binding; ubiquitin protein ligase binding

Biological Process: aldehyde catabolic process; angiogenesis; carbohydrate metabolic process; gene expression; gluconeogenesis; glucose 6-phosphate metabolic process; glucose metabolic process; hemostasis; humoral immune response; learning and/or memory; methylglyoxal biosynthetic process; negative regulation of caspase activity; negative regulation of neuron apoptosis; transcription initiation from RNA polymerase II promoter

Disease: Hemolytic Anemia, Nonspherocytic, Due To Glucose Phosphate Isomerase Deficiency
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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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