DHFR Protein, Human

DHFR protein, a pivotal enzyme in folate metabolism, is crucial for multiple pathways. It catalyzes reactions essential for de novo mitochondrial thymidylate biosynthesis, de novo glycine and purine synthesis, and DNA precursor synthesis. Beyond its catalytic role, DHFR binds its own mRNA and DHFR2 mRNA, hinting at a regulatory role in self-expression control and potential influence on related cellular processes. DHFR Protein, Human is the recombinant human-derived DHFR protein, expressed by E. coli , with tag free. The total length of DHFR Protein, Human is 187 a.a., .

Dihydrofolate reductase (DHFR) stands as a pivotal enzyme in folate metabolism, playing a crucial role in multiple essential pathways. It contributes significantly to the de novo mitochondrial thymidylate biosynthesis pathway, catalyzing reactions vital for de novo glycine and purine synthesis, as well as the synthesis of DNA precursors. Beyond its catalytic functions, DHFR exhibits the ability to bind its own mRNA and that of DHFR2, thereby suggesting a regulatory role in the control of its own expression and potentially influencing related cellular processes.

Human

E. coli

Tag Free

P00374-1 (M1-D187)

1719

Greater than 90% as determined by reducing SDS-PAGE.

<1 EU/μg, determined by LAL method.