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The recombinant DHPR produced in E. coli is a single, non-glycosylated polypeptide chain containing 237 amino acids, with a molecular mass of approximately 26 kDa . This recombinant protein is fused to a 20 amino acid His-Tag at the N-terminus, which facilitates its purification through chromatographic techniques .
DHPR is essential for the regeneration of BH4 from its oxidized form, quinonoid dihydrobiopterin (qBH2). This regeneration process is vital for maintaining the levels of BH4, which in turn supports the synthesis of critical neurotransmitters. Deficiency in DHPR activity can lead to hyperphenylalaninemia and various neurological disorders due to impaired neurotransmitter synthesis.
Recombinant DHPR produced in E. coli is widely used in biochemical and medical research. It is utilized to study the enzyme’s structure-function relationships, investigate the mechanisms of BH4 metabolism, and develop therapeutic strategies for disorders related to BH4 deficiency. Additionally, it serves as a valuable tool in the production of BH4 and its derivatives for pharmaceutical applications.