Anti-Dihydrofolate reductase (DHFR) Antibody Picoband® (FITC Conjugate)

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. In humans, the DHFR enzyme is encoded by the DHFR gene. It is found in the q11→q22 region of chromosome 5. What's more, 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. DHFR 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.

E.coli-derived human DHFR recombinant protein (Position: V2-D187). Human DHFR shares 90% amino acid (aa) sequence identity with both mouse and rat DHFR.

Widely expressed in fetal and adult tissues, including throughout the fetal and adult brains and whole blood. Expression is higher in the adult brain than in the fetal brain. .

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. .

Store at -20℃ for one year from date of receipt. After reconstitution, at 4℃ for one month. It can also be aliquotted and stored frozen at -20℃ for six months. Avoid repeated freeze-thaw cycles.

Immunohistochemistry (Paraffin-embedded Section), 0.5-1μg/ml, Human, Mouse, Rat, By Heat<br>Western blot, 0.1-0.5μg/ml, Human, Mouse, Rat<br>Immunocytochemistry/Immunofluorescence, 2μg/ml, Human<br> Flow Cytometry (Fixed), 1-3μg/1x10⁶ cells, Human<br>