DHRS9 Human

The recombinant form of DHRS9 is typically produced in Escherichia coli (E. coli) and is a single, non-glycosylated polypeptide chain containing 327 amino acids. It has a molecular mass of approximately 35.9 kDa . The protein is often tagged with a His-tag at the N-terminus to facilitate purification through chromatographic techniques .

DHRS9 exhibits dehydrogenase and reductase activities, which are crucial for the conversion of various substrates. One of its primary functions is the conversion of 3-alpha-tetrahydroprogesterone (allopregnanolone) to dihydroxyprogesterone and 3-alpha-androstanediol to dihydroxyprogesterone . Additionally, DHRS9 plays a significant role in the biosynthesis of retinoic acid from retinaldehyde, which is essential for vision and cellular differentiation .

The activity of DHRS9 is vital for maintaining the balance of steroid hormones and retinoids in the body. These compounds are involved in numerous physiological processes, including vision, immune response, and cellular growth. Dysregulation of DHRS9 activity has been associated with various diseases, such as prostate cancer and epilepsy .

Recombinant DHRS9 is widely used in biochemical and pharmacological research to study its enzymatic properties and potential therapeutic applications. The high purity and stability of the recombinant protein make it suitable for various experimental techniques, including SDS-PAGE and mass spectrometry .

For optimal stability, recombinant DHRS9 should be stored at -20°C. It is recommended to avoid multiple freeze-thaw cycles to maintain its activity. For long-term storage, adding a carrier protein such as human serum albumin (HSA) or bovine serum albumin (BSA) can help preserve its stability .