protein

Recombinant Human Cytidine deaminase

MBS717182

0.5 mg (E-Coli)

885 USD

Recombinant Protein

Recombinant Human Cytidine deaminase

Cytidine deaminase

Cytidine aminohydrolase

cytidine deaminase; Cytidine deaminase; cytidine deaminase; cytidine deaminase; Cytidine aminohydrolase

CDA

CDD; HI_1350

CDA; CDA; CDD; CDD

CDD_HUMAN

E Coli or Yeast or Baculovirus or Mammalian Cell

1-146, Full length.

146

MAQKRPACTLKPECVQQLLVCSQEAKKSAYCPYSHFPVG
AALLTQEGRIFKGCNIENACYPLGICAERTAIQKAVSEG
YKDFRAIAIASDMQDDFISPCGACRQVMREFGTNWPVYM
TKPDGTYIVMTVQELLPSSFGPEDLQKTQ

Greater than 90% as determined by SDS-PAGE.

Liquid containing glycerol; lyophilization may be available upon request.

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

Species: Homo sapiens (Human)

Epigenetics and Nuclear Signaling

This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis.

Human cytidine deaminase purification of enzyme, cloning, and expression of its complementary DNA.Laliberte J., Momparler R.L.Cancer Res. 54:5401-5407(1994) Isolation and characterization of the gene coding for human cytidine deaminase.Demontis S., Terao M., Brivio M., Zanotta S., Bruschi M., Garattini E.Biochim. Biophys. Acta 1443:323-333(1998) Growth inhibition of granulocyte-macrophage colony forming cells by human cytidine deaminase requires the catalytic function of the protein.Gran C., Boyum A., Johansen R.F., Lovhaug D., Seeberg E.C.Blood 91:4127-4135(1998) The DNA sequence and biological annotation of human chromosome 1.Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.Nature 441:315-321(2006) Cloning of a functional cDNA for human cytidine deaminase (CDD) and its use as a marker of monocyte/macrophage differentiation.Kuhn K., Bertling W.M., Emmrich F.Biochem. Biophys. Res. Commun. 190:1-7(1993) Structure of human cytidine deaminase bound to a potent inhibitor.Chung S.J., Fromme J.C., Verdine G.L.J. Med. Chem. 48:658-660(2005)

11386157

NP_001776.1

NM_001785.2

P32320

43.6kD

Drug Metabolism - Other Enzymes Pathway (83033); Drug Metabolism - Other Enzymes Pathway (428); Fluoropyrimidine Activity Pathway (198778); Metabolic Pathways (132956); Metabolism Pathway (1269956); Metabolism Of Nucleotides Pathway (1270133); Pyrimidine Metabolism Pathway (1270138); Pyrimidine Metabolism Pathway (82946); Pyrimidine Metabolism Pathway (309); Pyrimidine Salvage Reactions Pathway (1270140)

This gene encodes an enzyme involved in pyrimidine salvaging. The encoded protein forms a homotetramer that catalyzes the irreversible hydrolytic deamination of cytidine and deoxycytidine to uridine and deoxyuridine, respectively. It is one of several deaminases responsible for maintaining the cellular pyrimidine pool. Mutations in this gene are associated with decreased sensitivity to the cytosine nucleoside analogue cytosine arabinoside used in the treatment of certain childhood leukemias. [provided by RefSeq, Jul 2008]

CDA: This enzyme scavenge exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis. Belongs to the cytidine and deoxycytidylate deaminase family. Protein type: EC 3.5.4.5; Nucleotide Metabolism - pyrimidine; Xenobiotic Metabolism - drug metabolism - other enzymes; Hydrolase. Chromosomal Location of Human Ortholog: 1p36.2-p35. Cellular Component: cytosol; extracellular region. Molecular Function: cytidine deaminase activity; nucleoside binding; protein binding; protein homodimerization activity; zinc ion binding. Biological Process: cell surface receptor linked signal transduction; cytidine deamination; cytosine metabolic process; negative regulation of cell growth; negative regulation of nucleotide metabolic process; nucleobase, nucleoside and nucleotide metabolic process; protein homotetramerization; pyrimidine base metabolic process; pyrimidine nucleoside salvage; pyrimidine salvage

0.5 mg (E-Coli)

885 USD

0.05 mg (Baculovirus)

885

0.05 mg (Mammalian-Cell)

1110

0.5 mg (Yeast)

1110

1 mg (E-Coli)

1280