Cloning, Expression, Purification and CD Analysis of Recombinant Human Betatrophin

Betatrophin is a member of the angiopoietin-like (angptl) family that has been implicated in both triglyceride and glucose metabolism. the physiological functions and molecular targets of this protein remain largely unknown; hence, a purified available protein would aid study of the exact role of betatrophin in lipid or glucose metabolism. in this study, we cloned the full-length cdna of betatrophin from a human liver cdna library. betatrophin was expressed in the pet-21b-e. coli bl21 (de3) system and purified by immobilized metal-affinity chromatography and ion-exchange chromatography. circular dichroism spectroscopy revealed α-helix as the major regular secondary structure in recombinant betatrophin. the production method is based on commonly available resources; therefore, it can be readily implemented.