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

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Catalog # MBS717083
Unit / Price
  0.01 mg  /  $110 +1 FREE 8GB USB
  0.05 mg  /  $190 +1 FREE 8GB USB
  0.1 mg  /  $285 +1 FREE 8GB USB
  0.2 mg  /  $460 +1 FREE 8GB USB
  0.5 mg  /  $750 +1 FREE 8GB USB
  1 mg  /  $1,180 +1 FREE 8GB USB
SDS-PAGE
Product Name

Inosine-5'-monophosphate dehydrogenase 2 (IMPD2), Recombinant Protein

Popular Item
Also Known As

Recombinant Human Inosine-5'-monophosphate dehydrogenase 2

Product Synonym Names
IMPDH-II
Research Use Only
For Research Use Only. Not for use in diagnostic procedures.
Sequence Positions
5-514aa; Partial
Sequence Length
514
Sequence
LISGGTSYVP DDGLTAQQLF NCGDGLTYND FLILPGYIDF TADQVDLTSA LTKKITLKTP LVSSPMDTVT EAGMAIAMAL TGGIGFIHHN CTPEFQANEV RKVKKYEQGF ITDPVVLSPK DRVRDVFEAK ARHGFCGIPI TDTGRMGSRL VGIISSRDID FLKEEEHDCF LEEIMTKRED LVVAPAGITL KEANEILQRS KKGKLPIVNE DDELVAIIAR TDLKKNRDYP LASKDAKKQL LCGAAIGTHE DDKYRLDLLA QAGVDVVVLD SSQGNSIFQI NMIKYIKDKY PNLQVIGGNV VTAAQAKNLI DAGVDALRVG MGSGSICITQ EVLACGRPQA TAVYKVSEYA RRFGVPVIAD GGIQNVGHIA KALALGASTV MMGSLLAATT EAPGEYFFSD GIRLKKYRGM GSLDAMDKHL SSQNRYFSEA DKIKVAQGVS GAVQDKGSIH KFVPYLIAGI QHSCQDIGAK SLTQVRAMMY SGELKFEKRT SSAQVEGGVH SLHSYEKRLF
OMIM
146691
3D Structure
ModBase 3D Structure for P12268
Host
E Coli
Purity/Purification
Greater than 90% as determined by SDS-PAGE. (lot specific)
Form/Format
Liquid containing glycerol
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.
Preparation and Storage
Store at -20 degree C, for extended storage, conserve at -20 degree C or -80 degree C.
ISO Certification
Manufactured in an ISO 9001:2008 Certified Laboratory.
Other Notes
Small volumes of IMPD2 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.
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

IMPD2 recombinant protein SDS-PAGE image
(Note: Representative image, actual molecular weight may vary depending on Tag type and expression host)
NCBI/Uniprot data below describe general gene information for IMPD2. It may not necessarily be applicable to this product.
NCBI GI #
NCBI GeneID
NCBI Accession #
NCBI GenBank Nucleotide #
UniProt Primary Accession #
UniProt Secondary Accession #
UniProt Related Accession #
Molecular Weight
82.7kD
NCBI Official Full Name
inosine-5'-monophosphate dehydrogenase 2
NCBI Official Synonym Full Names
inosine monophosphate dehydrogenase 2
NCBI Official Symbol
IMPDH2  [Similar Products]
NCBI Official Synonym Symbols
IMPD2; IMPDH-II
  [Similar Products]
NCBI Protein Information
inosine-5'-monophosphate dehydrogenase 2
UniProt Protein Name
Inosine-5'-monophosphate dehydrogenase 2
UniProt Synonym Protein Names
IMPDH-II
UniProt Gene Name
IMPDH2  [Similar Products]
UniProt Synonym Gene Names
IMP dehydrogenase 2; IMPD 2; IMPDH 2  [Similar Products]
UniProt Entry Name
IMDH2_HUMAN
NCBI Summary for IMPD2
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 Comments for IMPD2
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 References and Citations for IMPD2 recombinant protein
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

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Disclaimer
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