Recombinant Human DHFR Protein，His

Dihydrofolate reductase (DHFR) is a pivotal enzyme in the folate metabolism pathway, responsible for the reduction of dihydrofolate to tetrahydrofolate, a crucial cofactor in the synthesis of nucleotides and amino acids. Its significance is underscored by its role in cellular proliferation and survival, making it a key target in cancer therapy and antimicrobial drug development. Over the years, recombinant protein technology has enabled the production of DHFR with high purity and yield, facilitating detailed biochemical studies and structural analyses. Understanding the structure-function relationship of DHFR through crystallography and mutagenesis has provided insights into enzyme mechanisms and has led to the identification of novel inhibitors. Moreover, the recombinant DHFR protein has been utilized in various applications, including drug screening and the development of biosensors. Given the increasing prevalence of drug resistance, ongoing studies focus on engineering DHFR variants with improved properties or altered specificity to counteract resistance mechanisms. Overall, the research surrounding DHFR recombinant proteins not only enhances our understanding of fundamental biological processes but also holds significant therapeutic potential in combating diseases linked to folate metabolism dysregulation.