TPMT blocking peptide

TPMT Immunizing Peptide

Cat. Num. AAA425002

• Reactivity: Human, Mouse, Rat, Dog, Cow
• Synonyms: TPMT; TPMT Immunizing Peptide; TPMT antibody; thiopurine S-methyltransferase antibody; HGNC:12014 antibody; S-adenosyl-L-methionine:thiopurine S-methyltransferase antibody; thiopurine methyltransferase antibody; TPMT blocking peptide

• Reactivity: Human, Mouse, Rat, Dog, Cow
• Form/Format: 100ug of dried peptide
• Sequence: C-DAFEERHKSWGID
• Sequence Length: 13

• Corresponding Antibody: The peptide was used in the production of MBS420849 - Goat Anti-TPMT Antibody.; It is currently untested in blocking applications.
• Preparation and Storage: Shipped at ambient temperature, store at -20 degree C.

NCBI and Uniprot Product Information

• NCBI GI #: 4507653
• NCBI GeneID: 7172
• NCBI Accession #: NP_000358.1
• NCBI GenBank Nucleotide #: NM_000367.2
• UniProt Accession #: P51580; O14806; O15423; O15424; O15425; O15426; O15515; O15548; O43213; Q5VUK6; Q9UBE6; Q9UBT8
• Molecular Weight: 28,180 Da
• NCBI Official Full Name: thiopurine S-methyltransferase
• NCBI Official Synonym Full Names: thiopurine S-methyltransferase
• NCBI Official Symbol: TPMT
• NCBI Protein Information: thiopurine S-methyltransferase; S-adenosyl-L-methionine:thiopurine S-methyltransferase
• UniProt Protein Name: Thiopurine S-methyltransferase
• UniProt Gene Name: TPMT
• UniProt Entry Name: TPMT_HUMAN

NCBI Description

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, Jul 2008]

Uniprot Description

Function: Catalyzes the S-methylation of thiopurine drugs such as 6-mercaptopurine. Ref.10

Catalytic activity: S-adenosyl-L-methionine + a thiopurine = S-adenosyl-L-homocysteine + a thiopurine S-methylether. Ref.10

Enzyme regulation: Inhibited by S-adenosyl-L-homocysteine (SAH).

Subunit structure: Monomer. Ref.16

Subcellular location: Cytoplasm.

Polymorphism: Individual variation in the toxicity and therapeutic efficacy of thiopurine drugs is associated with a common genetic polymorphism that controls levels of TPMT activity. Genetic polymorphism in the TPMT gene is such that about 90% of Caucasians have high TPMT activity, 10% have intermediate activity and 1 in 300 individuals has low activity. TPMT activity varies among ethnic groups.TPMT*3A is the only mutant allele found in the South West Asians. This is also the most common mutant allele in the Caucasians but is not found in the Chinese. All mutant alleles identified in the Chinese population were TPMT*3C. This allele is found at a low frequency in the Caucasians. This suggests that TPMT*3C is the oldest mutation, with TPMT*3B being acquired later to form the TPMT*3A allele in the Caucasian and South West Asian populations. TPMT*2 appears to be a more recent allele, which has only been detected in Caucasians to date. These ethnic differences may be important in the clinical use of thiopurine drugs.

Involvement in disease: Thiopurine S-methyltransferase deficiency (TPMT deficiency) [MIM:610460]: Enzyme involved in the normal metabolic inactivation of thiopurine drugs. These drugs are generally used as immunosupressants or cytotoxic drugs and are prescribed for a variety of clinical conditions including leukemia, autoimmune disease and organ transplantation. Patients with intermediate or no TPMT activity are at risk of toxicity after receiving standard doses of thiopurine drugs and it is shown that inter-individual differences in response to these drugs are largely determined by genetic variation at the TPMT locus.Note: The disease is caused by mutations affecting the gene represented in this entry.

Miscellaneous: TPMT deficiency inherited by TPMT*2 and TPMT*3A alleles, are the most prevalent mutant TPMT in humans. TPMT deficiency is associated with lower cellular levels of TPMT protein, and the proteins encoded by TPMT*2 and TPMT*3A mutant alleles are degraded more rapidly by an ATP-dependent proteasome-mediated pathway.

Sequence similarities: Belongs to the methyltransferase superfamily. TPMT family.

Biophysicochemical propertiesKinetic parameters:KM=5.6 mM for S-adenosyl-L-methionine Ref.10KM=0.35 mM for 6-mercaptopurineVmax=0.6 nmol/sec/mg enzyme toward 6-mercaptopurine (at 37 degrees Celsius)

Sequence caution: The sequence AAB71631.1 differs from that shown. Reason: Erroneous initiation. The sequence AAB71632.1 differs from that shown. Reason: Erroneous initiation.