A variety of enzymes catalyze reactions involved in the synthesis, modification, and degradation of nucleic acids within cells. Many of these enzymes are being targeted in the development of anticancer drugs.
Thymidylate synthetase (TS) is used to synthesize thymidine monophosphate (dTMP), which is subsequently phosphorylated to thymidine triphosphate for use in DNA synthesis and repair. It is a target of anticancer drugs such as 5-fluorouracil and folate analogs. TS is also known as TMS, TSase, and HsT422.
Dihydropyrimidine dehydrogenase (DPD) is one of the enzymes required for pyrimidine degradation, the initial and rate-limiting step in pyrimidine catabolism. DPD catalyzes the reduction of uracil and thymine. It is a traget of the anticancer drug 5-fluorouracil. DPD is also known as dihydrothymine dehydrogenase, dihydrouracil dehydrogenase, DHP, dihydropyrimidine dehydrogenase [NADP(+)], and DHPDHase.
Orotate phosphoribosyltransferase (OPRT) catalyzes the formation of orotidine 5'-monophosphate (OMP) from orotate and phosphoribosyl pyrophosphate, as part of the pyrimidine biosynthetic pathway. In yeast and bacteria, OPRT is an independent enzyme with a unique gene coding for the protein; in higher eukaryotes, the catalytic function is performed by a subdomain of the enzyme uridine monophosphate (UMP) synthase. Human OPRT is also known as uridine monophosphate synthetase, UMP synthase, OMPdecase, OPRTase, orotidine 5'-phosphate decarboxylase, and uridine 5'-monophosphate synthase.
These products are affinity-purified IgG antibodies that recognize TS, DPD, and OPRT. The antibodies were raised in rabbit or mouse using recombinant protein or a synthetic peptide and can be used for Western blot (WB) detection or immunohistochemical (IHC) detection of TS, DPD, and OPRT.