DHFR Enzyme

Description:
|Introduction Dihydrofolate reductase (DHFR) is an enzyme that reduces dihydrofolic acid to tetrahydrofolic acid, with NADPH as electron donor that can be converted to the kinds of tetrahydrofolate cofactors applied in 1-carbon transfer chemistry. DHFR converts dihydrofolate into tetrahydrofolate, which is a methyl group shuttle required for the de novo synthesis of purines, thymidylic acid, and specific amino acids. Even though the functional DHFR gene is mapped to chromosome 5, numerous intronless processed pseudogenes or dihydrofolate reductase-like genes are identified on se|E.coli-derived. DHFR fused with 20 amino acid His tag at N-terminus is a single, non-glycosylated, polypeptide chain containing 207 amino acids (1-187 a.a.) and having a molecular mass of 23.6 kDa. Specific activity is 1.5 – 2.5 units/ml and was obtained by measuring the oxidation of NADPH in absorbance at 340 nm during reaction. One unit will convert 1.0 umole of 7,8 dihydrofolate and beta-NADPH to 5,6,7,8-tetrahydrofolate and beta-NADP per minute at pH 6.5 at 25C. Purity > 95%, by SDS-|The DHFR solution (1 ug/ml) contains 20 mM Tris-HCl buffer(pH 8.0), 10% glycerol, 2 mM DTT and 0.1 M NaCl. Shipping: The product is shipped at a|Use a manual defrost freezer and avoid repeated freeze-thaw cycles. 12 months from date of receipt, -20 to -70°C as supplied. 1 month, 2 to 8°C under sterile conditions after reconstitution. 3 months, -20 to -70°C under sterile conditions after reconstitution. |Other DHFR Enzymes: Recombinant Mouse Dihydrofolate Reductase