This gene encodes the enzyme that metabolizes thiopurine drugs via S-adenosyl-L-methionine as the S-methyl donor and S-adenosyl-L-homocysteine as a byproduct. Thiopurine drugs such as 6-mercaptopurine are used as chemotherapeutic agents. Genetic polymorphisms that affect this enzymatic activity are correlated with variations in sensitivity and toxicity to such drugs within individuals. A pseudogene for this locus is located on chromosome 18q. (provided by RefSeq)
Immunogen
TPMT (AAH05339, 1 a.a. ~ 245 a.a) full-length recombinant protein with GST tag. MW of the GST tag alone is 26 KDa.
TPMT (Thiopurine S-methyltransferase) mainly mediates different catalytic S-methylation reaction such as 6-mercaptopurine and 6-thioguanine. It also participates in the metabolism of some drugs such as thiopurine drugs, which is largely influenced by TPMT polymorphisms. Deficiency in TPMT gene causes an autosomal recessive disorder, childhood acute lymphoblastic leukemia.
Pharmacogenetics and genomics, 25(3), 143-146 (2015-01-08)
Thiopurine S-methyltransferase (TPMT) is a cytoplasmic enzyme involved in the metabolism of thiopurine drugs and its activity is largely influenced by polymorphisms of the TPMT gene. To date, more than 35 TPMT variants are known to be associated with reduced
Thiopurine methyltransferase (TPMT) catalyses the S-methylation of thiopurines, including 6-mercaptopurine and 6-thioguanine. TPMT activity exhibits genetic polymorphism, with about 1/300 inheriting TPMT deficiency as an autosomal recessive trait. If treated with standard doses of thiopurines, TPMTdeficient patients accumulate excessive thioguanine
The Libyan journal of medicine, 10, 27053-27053 (2015-03-31)
Thiopurine S-methyltransferase (TPMT) is a cytosolic enzyme that catalyses the S-methylation of 6-mercaptopurine and azathioprine. Low activity phenotypes are correlated with polymorphism in the TPMT gene. Patients with low or undetectable TMPT activity could develop severe myelosuppression when they are
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