Thiopurine S-methyltransferase (TPMT) Recombinant Protein | TPMT recombinant protein

Recombinant Human Thiopurine S-methyltransferase (TPMT), partial

Cat. Num. AAA81611

• Purity: Greater or equal to 85% purity as determined by SDS-PAGE.
• Synonyms: Thiopurine S-methyltransferase (TPMT); N/A; Recombinant Human Thiopurine S-methyltransferase (TPMT), partial; Thiopurine methyltransferase; TPMT 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: 4-244aa; Partial
• Sequence: TRTSLDIEEYSDTEVQKNQVLTLEEWQDKWVNGKTAFHQEQGHQLLKKHLDTFLKGKSGLRVFFPLCGKAVEMKWFADRGHSVVGVEISELGIQEFFTEQNLSYSEEPITEIPGTKVFKSSSGNISLYCCSIFDLPRTNIGKFDMIWDRGALVAINPGDRKCYADTMFSLLGKKFQYLLCVLSYDPTKHPGPPFYVPHAEIERLFGKICNIRCLEKVDAFEERHKSWGIDCLFEKLYLLTE
• Sequence Length: 245

• 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 TPMT recombinant protein

Catalyzes the S-methylation of thiopurine drugs such as 6-mercaptopurine.

Product Categories/Family for TPMT recombinant protein

Metabolism

References

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Res. 14:1672-1678(1997) Human thiopurine methyltransferase pharmacogenetics gene sequence polymorphisms.Otterness D., Szumlanski C., Lennard L., Klemetsdal B., Aarbakke J., Park-Hah J.O., Iven H., Schmiegelow K., Branum E., O'Brien J., Weinshilboum R.M.Clin. Pharmacol. Ther. 62:60-73(1997) Genomic structure of thiopurine S-methyltransferase gene.Nakamura Y.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) Detection of known and new mutations in the thiopurine S-methyltransferase gene by single-strand conformation polymorphism analysis.Spire-Vayron de la Moureyre C., Debuysere H., Sabbagh N., Marez D., Vinner E., Chevalier E.D., Lo-Guidice J.-M., Broly F.3.0.CO;2-E>Hum. Mutat. 12:177-185(1998) Structural basis of substrate recognition in thiopurine s-methyltransferase.Peng Y., Feng Q., Wilk D., Adjei A.A., Salavaggione O.E., Weinshilboum R.M., Yee V.C.Biochemistry 47:6216-6225(2008) 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) Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography.Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D., Zou H., Gu J.Proteomics 8:1346-1361(2008) Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.Sci. Signal. 2:RA46-RA46(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) 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) Structural basis of allele variation of human thiopurine-S-methyltransferase.Wu H., Horton J.R., Battaile K., Allali-Hassani A., Martin F., Zeng H., Loppnau P., Vedadi M., Bochkarev A., Plotnikov A.N., Cheng X.Proteins 67:198-208(2007) A single point mutation leading to loss of catalytic activity in human thiopurine S-methyltransferase.Krynetski E.Y., Schuetz J.D., Galpin A.J., Pui C.-H., Relling M.V., Evans W.E.Proc. Natl. Acad. Sci. U.S.A. 92:949-953(1995) Thiopurine S-methyltransferase deficiency two nucleotide transitions define the most prevalent mutant allele associated with loss of catalytic activity in Caucasians.Tai H.-L., Krynetski E.Y., Yates C.R., Loennechen T., Fessing M.Y., Krynetskaia N.F., Evans W.E.Am. J. Hum. Genet. 58:694-702(1996) Azathioprine-induced severe pancytopenia due to a homozygous two-point mutation of the thiopurine methyltransferase gene in a patient with juvenile HLA-B27-associated spondylarthritis.Leipold G., Schuetz E., Haas J.P., Oellerich M.Arthritis Rheum. 40:1896-1898(1997) Enhanced proteolysis of thiopurine S-methyltransferase (TPMT) encoded by mutant alleles in humans (TPMT*3A, TPMT*2) mechanisms for the genetic polymorphism of TPMT activity.Tai H.-L., Krynetski E.Y., Schuetz E.G., Yanishevski Y., Evans W.E.Proc. Natl. Acad. Sci. U.S.A. 94:6444-6449(1997) Thiopurine methyltransferase alleles in British and Ghanaian populations.Ameyaw M.-M., Collie-Duguid E.S.R., Powrie R.H., Ofori-Adjei D., McLeod H.L.Hum. Mol. Genet. 8:367-370(1999) Polymorphism of the thiopurine S-methyltransferase gene in African-Americans.Hon Y.Y., Fessing M.Y., Pui C.-H., Relling M.V., Krynetski E.Y., Evans W.E.Hum. Mol. Genet. 8:371-376(1999) The frequency and distribution of thiopurine methyltransferase alleles in Caucasian and Asian populations.Collie-Duguid E.S.R., Pritchard S.C., Powrie R.H., Sludden J., Collier D.A., Li T., McLeod H.L.Pharmacogenetics 9:37-42(1999) Genetic analysis of thiopurine methyltransferase polymorphism in a Japanese population.Hiratsuka M., Inoue T., Omori F., Agatsuma Y., Mizugaki M.Mutat. Res. 448:91-95(2000) Thiopurine S-methyltransferase pharmacogenetics variant allele functional and comparative genomics.Salavaggione O.E., Wang L., Wiepert M., Yee V.C., Weinshilboum R.M.Pharmacogenet. Genomics 15:801-815(2005) Severe azathioprine-induced myelotoxicity in a kidney transplant patient with thiopurine S-methyltransferase-deficient genotype (TPMT*3A/*3C) .Kurzawski M., Dziewanowski K., Ciechanowski K., Drozdzik M.Transpl. Int. 18:623-625(2005) Molecular analysis of thiopurine S-methyltransferase alleles in Taiwan aborigines and Taiwanese.Lu H.-F., Shih M.-C., Chang Y.-S., Chang J.-Y., Ko Y.-C., Chang S.-J., Chang J.-G.J. Clin. Pharm. Ther. 31:93-98(2006) Frequency of the thiopurine S-methyltransferase alleles in the ancient genetic population isolate of Sardinia.Rossino R., Vincis C., Alves S., Prata M.J., Macis M.D., Nucaro A.L., Schirru E., Congia M.J. Clin. Pharm. Ther. 31:283-287(2006) +Additional computationally mapped references.<p>Provides general information on the entry.

NCBI and Uniprot Product Information

• NCBI GeneID: 7172
• UniProt Accession #: P51580; O14806; O15423; O15424; O15425; O15426; O15515; O15548; O43213; Q5VUK6; Q9UBE6; Q9UBT8
• Molecular Weight: 54.7 kDa
• NCBI Official Synonym Full Names: thiopurine S-methyltransferase
• NCBI Official Symbol: TPMT
• NCBI Protein Information: thiopurine S-methyltransferase
• UniProt Protein Name: Thiopurine S-methyltransferase
• UniProt Gene Name: TPMT
• UniProt Entry Name: TPMT_HUMAN