Inosine-5'-monophosphate dehydrogenase 2 Recombinant Protein | IMPD2 recombinant protein

Recombinant Human Inosine-5'-monophosphate dehydrogenase 2

Cat. Num. AAA717083

• Gene Names: IMPDH2; IMPD2; IMPDH-II
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Inosine-5'-monophosphate dehydrogenase 2; Recombinant Human Inosine-5'-monophosphate dehydrogenase 2; IMPDH-II; IMPD2 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: 5-514aa; Partial
• Sequence: LISGGTSYVPDDGLTAQQLFNCGDGLTYNDFLILPGYIDFTADQVDLTSALTKKITLKTPLVSSPMDTVTEAGMAIAMALTGGIGFIHHNCTPEFQANEVRKVKKYEQGFITDPVVLSPKDRVRDVFEAKARHGFCGIPITDTGRMGSRLVGIISSRDIDFLKEEEHDCFLEEIMTKREDLVVAPAGITLKEANEILQRSKKGKLPIVNEDDELVAIIARTDLKKNRDYPLASKDAKKQLLCGAAIGTHEDDKYRLDLLAQAGVDVVVLDSSQGNSIFQINMIKYIKDKYPNLQVIGGNVVTAAQAKNLIDAGVDALRVGMGSGSICITQEVLACGRPQATAVYKVSEYARRFGVPVIADGGIQNVGHIAKALALGASTVMMGSLLAATTEAPGEYFFSDGIRLKKYRGMGSLDAMDKHLSSQNRYFSEADKIKVAQGVSGAVQDKGSIHKFVPYLIAGIQHSCQDIGAKSLTQVRAMMYSGELKFEKRTSSAQVEGGVHSLHSYEKRLF
• Sequence Length: 514

• 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 IMPD2 recombinant protein

Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth. Could also have a single-stranded nucleic acid-binding activity and could play a role in RNA and/or DNA metabolism. It may also have a role in the development of malignancy and the growth progression of some tumors.

Product Categories/Family for IMPD2 recombinant protein

Cancer

References

Cloning and sequence analysis of the human and Chinese hamster inosine-5'-monophosphate dehydrogenase cDNAs.Collart F.R., Huberman E.J. Biol. Chem. 263:15769-15772(1988) Two distinct cDNAs for human IMP dehydrogenase.Natsumeda Y., Ohno S., Kawasaki H., Konno Y., Weber G., Suzuki K.J. Biol. Chem. 265:5292-5295(1990) Cloning and sequence of the human type II IMP dehydrogenase gene.Glesne D.A., Huberman E.Biochem. Biophys. Res. Commun. 205:537-544(1994) Characterization of the human inosine-5'-monophosphate dehydrogenase type II gene.Zimmermann A.G., Spychala J., Mitchell B.S.J. Biol. Chem. 270:6808-6814(1995) Chromosomal localization and structure of the human type II IMP dehydrogenase gene.Glesne D.A., Collart F.R., Varkony T., Drabkin H., Huberman E.Genomics 16:274-277(1993) Characterization of human type I and type II IMP dehydrogenases.Carr S.F., Papp E., Wu J.C., Natsumeda Y.J. Biol. Chem. 268:27286-27290(1993) Recombinant human inosine monophosphate dehydrogenase type I and type II proteins. Purification and characterization of inhibitor binding.Hager P.W., Collart F.R., Huberman E., Mitchell B.S.Biochem. Pharmacol. 49:1323-1329(1995) Inosine 5'-monophosphate dehydrogenase binds nucleic acids in vitro and in vivo.McLean J.E., Hamaguchi N., Belenky P., Mortimer S.E., Stanton M., Hedstrom L.Biochem. J. 379:243-251(2004) Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.Nat. Biotechnol. 23:94-101(2005) Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.Cell 127:635-648(2006) A novel variant L263F in human inosine 5'-monophosphate dehydrogenase 2 is associated with diminished enzyme activity.Wang J., Zeevi A., Webber S., Girnita D.M., Addonizio L., Selby R., Hutchinson I.V., Burckart G.J.Pharmacogenet. Genomics 17:283-290(2007) 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) 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) Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.Sci. Signal. 3:RA3-RA3(2010) 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 human type II inosine monophosphate dehydrogenase implications for ligand binding and drug design.Colby T.D., Vanderveen K., Strickler M.D., Markham G.D., Goldstein B.M.Proc. Natl. Acad. Sci. U.S.A. 96:3531-3536(1999) Crystal structure of human inosine monophosphate dehydrogenase type II complexed with the MPA/NAD analog C2-MAD.Risal D., Strickler M.D., Goldstein B.M.Submitted (DEC-2002) to the PDB data bankThe conformation of NAD bound to human inosine monophosphate Dehydrogenase Type II.Risal D., Strickler M.D., Goldstein B.M.Submitted (DEC-2002) to the PDB data bank

NCBI and Uniprot Product Information

• NCBI GI #: 66933016
• NCBI GeneID: 3615
• NCBI Accession #: NP_000875.2
• NCBI GenBank Nucleotide #: NM_000884.2
• UniProt Accession #: P12268; Q6LEF3
• Molecular Weight: 82.3 kDa
• NCBI Official Full Name: inosine-5'-monophosphate dehydrogenase 2
• NCBI Official Synonym Full Names: inosine monophosphate dehydrogenase 2
• NCBI Official Symbol: IMPDH2
• NCBI Official Synonym Symbols: IMPD2; IMPDH-II
• NCBI Protein Information: inosine-5'-monophosphate dehydrogenase 2
• UniProt Protein Name: Inosine-5'-monophosphate dehydrogenase 2
• Protein Family: Inosine-5'-monophosphate dehydrogenase
• UniProt Gene Name: IMPDH2
• UniProt Synonym Gene Names: IMP dehydrogenase 2; IMPD 2; IMPDH 2
• UniProt Entry Name: IMDH2_HUMAN

NCBI Description

This gene encodes the rate-limiting enzyme in the de novo guanine nucleotide biosynthesis. It is thus involved in maintaining cellular guanine deoxy- and ribonucleotide pools needed for DNA and RNA synthesis. The encoded protein catalyzes the NAD-dependent oxidation of inosine-5'-monophosphate into xanthine-5'-monophosphate, which is then converted into guanosine-5'-monophosphate. This gene is up-regulated in some neoplasms, suggesting it may play a role in malignant transformation. [provided by RefSeq, Jul 2008]

Uniprot Description

Catalyzes the conversion of inosine 5'-phosphate (IMP) to xanthosine 5'-phosphate (XMP), the first committed and rate-limiting step in the de novo synthesis of guanine nucleotides, and therefore plays an important role in the regulation of cell growth. Could also have a single-stranded nucleic acid-binding activity and could play a role in RNA and/or DNA metabolism. It may also have a role in the development of malignancy and the growth progression of some tumors.