Anti-DHFR

0.5mg/ml if reconstituted with 0.2ml sterile DI water. Dihydrofolate reductase, or DHFR, is an enzyme that reduces dihydrofolic acid to tetrahydrofolic acid using NADPH as electron donor, which can be converted to the kinds of tetrahydrofolate cofactors used in 1-carbon transfer chemistry. DHFR belongs to the dihydrofolate reductase family, and it converts dihydrofolate into tetrahydrofolate, a methyl group shuttle required for the de novo synthesis of purines, thymidylic acid, and certain amino acids. It is the key enzyme in folate metabolism. In addition, DHFR catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. Protein function: Key enzyme in folate metabolism. Contributes to the de novo mitochondrial thymidylate biosynthesis pathway. Catalyzes an essential reaction for de novo glycine and purine synthesis, and for DNA precursor synthesis. Binds its own mRNA and that of DHFRL1. [The UniProt Consortium]