Recombinant Human DHFR Protein, CF

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Dihydrofolate Reductase (DHFR) is an approximately 21 kDa enzyme that catalyzes the NADPH-dependent reduction of dihydrofolate to tetrahydrofolate, which is crucial for the synthesis of purines, thymidylate, and certain amino acids (1-4). Structurally, DHFR consists of an eight-stranded beta -sheet and four alpha -helices (2). Human DHFR shares 90% amino acid identity with mouse and rat DHFR. In addition to acting as a cofactor, NADPH protects DHFR from degradation in vitro and in a cellular context (5-8). DHFR protein binds to its own mRNA to self-regulate translation (9-12). The enzymatic activity and subcellular localization of DHFR are at least partially regulated by post-translational modification. Mono-ubiquitination of DHFR by MDM2 reduces the activity of DHFR (13). DHFR is primarily cytoplasmic, but it has been shown to translocate to the nucleus in a SUMO-dependent manner (14). Due to its role in nucleotide biosynthesis, DHFR has long been a therapeutic target for the treatment of various cancers and infectious diseases (15, 16).

Array 8456-DR

• Dihydrofolate Reductase/DHFR Antibodies
• Dihydrofolate Reductase/DHFR Lysate
• Dihydrofolate Reductase/DHFR Proteins and Enzyme