protein

Recombinant Human Inosine-5'-monophosphate dehydrogenase 2

MBS717083

0.05 mg (E-Coli)

190 USD

Recombinant Protein

Recombinant Human Inosine-5'-monophosphate dehydrogenase 2

Inosine-5'-monophosphate dehydrogenase 2

IMPDH-II

inosine-5'-monophosphate dehydrogenase 2; Inosine-5'-monophosphate dehydrogenase 2; inosine-5'-monophosphate dehydrogenase 2; IMP (inosine 5'-monophosphate) dehydrogenase 2; IMPDH-II

IMPD2

IMPDH2; IMPDH2; IMPD2; IMPDH-II; IMP dehydrogenase 2; IMPD 2; IMPDH 2

IMDH2_HUMAN

E Coli

5-514

514

LISGGTSYVPDDGLTAQQLFNCGDGLTYNDFLILPGYID
FTADQVDLTSALTKKITLKTPLVSSPMDTVTEAGMAIAM
ALTGGIGFIHHNCTPEFQANEVRKVKKYEQGFITDPVVL
SPKDRVRDVFEAKARHGFCGIPITDTGRMGSRLVGIISS
RDIDFLKEEEHDCFLEEIMTKREDLVVAPAGITLKEANE
ILQRSKKGKLPIVNEDDELVAIIARTDLKKNRDYPLASK
DAKKQLLCGAAIGTHEDDKYR

Greater than 90% as determined by SDS-PAGE.

Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.

Cancer

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.

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

66933016

NP_000875.2

NP_000875.2

P12268

82.7kD

Drug Metabolism - Other Enzymes Pathway (83033); Drug Metabolism - Other Enzymes Pathway (428); Guanine Ribonucleotide Biosynthesis IMP = GDP,GTP Pathway (618581); Guanine Ribonucleotide Biosynthesis IMP = GDP,GTP Pathway (468243); Metabolic Pathways (132956); Metabolism Pathway (1269956); Metabolism Of Nucleotides Pathway (1270133); Purine Metabolism Pathway (82944); Purine Metabolism Pathway (1270134); Purine Metabolism Pathway (307)

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]

0.05 mg (E-Coli)

190 USD

0.2 mg (E-Coli)

460

0.5 mg (E-Coli)

750

1 mg (E-Coli)

1180