Cyclophilin G Human

Cyclophilin-G (CypG) is a member of the cyclophilin family of peptidyl-prolyl isomerases (PPIases), which are enzymes that catalyze the cis-trans isomerization of proline residues in peptide chains. This family is highly conserved across all organisms and plays a crucial role in protein folding, trafficking, and signaling .

Cyclophilins, including CypG, possess a characteristic β-barrel structure that forms the active site for their isomerase activity. The primary function of these enzymes is to assist in protein folding by catalyzing the isomerization of peptide bonds at proline residues. This activity is essential for the proper folding and function of many proteins .

Cyclophilin-G is one of the lesser-studied members of the cyclophilin family. It shares structural similarities with other cyclophilins but has unique features that distinguish it from its counterparts. The specific physiological roles of CypG are still being elucidated, but it is known to be involved in various cellular processes, including protein folding and immune regulation .

Recombinant human Cyclophilin-G (rhCypG) is produced using recombinant DNA technology, which involves inserting the gene encoding CypG into a suitable expression system, such as bacteria or yeast. This allows for the large-scale production of the protein for research and therapeutic purposes .

Research on rhCypG is ongoing to understand its potential therapeutic applications. Cyclophilins, in general, have been studied for their roles in various diseases, including cancer, neurodegenerative disorders, and viral infections. The ability of cyclophilins to bind to immunosuppressive drugs like cyclosporin A has also made them targets for drug development .