GMP reductase 1 Recombinant Protein | GMPR recombinant protein

Recombinant Human GMP reductase 1

Cat. Num. AAA1138517

• Gene Names: GMPR; GMPR1; GMPR 1
• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: GMP reductase 1; Recombinant Human GMP reductase 1; Guanosine 5'-monophosphate oxidoreductase 1; Guanosine monophosphate reductase 1; GMPR recombinant protein

• Host: E Coli or Yeast or Baculovirus or Mammalian Cell
• Purity/Purification: Greater or equal to 85% purity as determined by SDS-PAGE.
• Form/Format: Lyophilized or liquid (Format to be determined during the manufacturing process)
• Sequence Positions: 1-345aa; Full Length
• Sequence: MPRIDADLKLDFKDVLLRPKRSSLKSRAEVDLERTFTFRNSKQTYSGIPIIVANMDTVGTFEMAAVMSQHSMFTAIHKHYSLDDWKLFATNHPECLQNVAVSSGSGQNDLEKMTSILEAVPQVKFICLDVANGYSEHFVEFVKLVRAKFPEHTIMAGNVVTGEMVEELILSGADIIKVGVGPGSVCTTRTKTGVGYPQLSAVIECADSAHGLKGHIISDGGCTCPGDVAKAFGAGADFVMLGGMFSGHTECAGEVFERNGRKLKLFYGMSSDTAMNKHAGGVAEYRASEGKTVEVPYKGDVENTILDILGGLRSTCTYVGAAKLKELSRRATFIRVTQQHNTVFS
• Sequence Length: 345

• 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 GMPR recombinant protein

Catalyzes the irreversible NADPH-dependent deamination of GMP to IMP. It functions in the conversion of nucleobase, nucleoside and nucleotide derivatives of G to A nucleotides, and in maintaining the intracellular balance of A and G nucleotides.

Product Categories/Family for GMPR recombinant protein

Cell Biology

References

Two structural genes on different chromosomes are required for encoding the major subunit of human red cell glucose-6-phosphate dehydrogenase.Kanno H., Huang I.Y., Kan Y.W., Yoshida A.Cell 58:595-606(1989) Genomic structure and expression of human guanosine monophosphate reductase.Kondoh T., Kanno H., Chang L., Yoshida A.Hum. Genet. 88:219-224(1991) The DNA sequence and analysis of human chromosome 6.Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.Nature 425:805-811(2003) The human mRNA that provides the N-terminus of chimeric G6PD encodes GMP reductase.Henikoff S., Smith J.M.Cell 58:1021-1022(1989) Origin of 'fused' glucose-6-phosphate dehydrogenase.Yoshida A., Kan Y.W.Cell 62:11-12(1990) 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) Structure of human guanosine monophosphate reductase GMPR1 in complex with GMP.Structural genomics consortium (SGC) Submitted (JUL-2005) to the PDB data bankIdentification of common variant alleles of the human guanosine monophosphate reductase gene.Kondoh T., Kanno H., Chang L., Yoshida A.Hum. Genet. 88:225-227(1991)

NCBI and Uniprot Product Information

• NCBI GI #: 156104880
• NCBI GeneID: 2766
• NCBI Accession #: NP_006868.3
• NCBI GenBank Nucleotide #: NM_006877.3
• UniProt Accession #: P36959; Q96HQ6
• Molecular Weight: 53.4 kDa
• NCBI Official Full Name: GMP reductase 1
• NCBI Official Synonym Full Names: guanosine monophosphate reductase
• NCBI Official Symbol: GMPR
• NCBI Official Synonym Symbols: GMPR1; GMPR 1
• NCBI Protein Information: GMP reductase 1
• UniProt Protein Name: GMP reductase 1
• Protein Family: GMP reductase
• UniProt Gene Name: GMPR
• UniProt Synonym Gene Names: GMPR 1; Guanosine monophosphate reductase 1
• UniProt Entry Name: GMPR1_HUMAN

NCBI Description

This gene encodes an enzyme that catalyzes the irreversible and NADPH-dependent reductive deamination of GMP to IMP. The protein also functions in the re-utilization of free intracellular bases and purine nucleosides.[provided by RefSeq, Oct 2009]

Uniprot Description

GMPR: Catalyzes the irreversible NADPH-dependent deamination of GMP to IMP. It functions in the conversion of nucleobase, nucleoside and nucleotide derivatives of G to A nucleotides, and in maintaining the intracellular balance of A and G nucleotides. Belongs to the IMPDH/GMPR family.

Protein type: Nucleotide Metabolism - purine; EC 1.7.1.7; Oxidoreductase

Chromosomal Location of Human Ortholog: 6p23

Cellular Component: cytosol

Molecular Function: GMP reductase activity; metal ion binding

Biological Process: nucleobase, nucleoside and nucleotide metabolic process; nucleotide metabolic process; purine base metabolic process; purine salvage; response to cold