Cyclophilin C Human

Cyclophilin-C (CypC) is a member of the cyclophilin family of peptidyl-prolyl cis/trans isomerases (PPIases). These enzymes play a crucial role in protein folding by catalyzing the isomerization of peptide bonds at proline residues. Cyclophilins are highly conserved across species, found in both prokaryotes and eukaryotes .

Cyclophilin-C, like other cyclophilins, possesses PPIase activity, which is essential for various cellular processes, including protein folding, trafficking, and signaling . The enzyme’s activity is inhibited by the immunosuppressive drug cyclosporine A (CsA), which is used to prevent organ transplant rejection .

Cyclophilin-C, along with Cyclophilin-A (CypA) and Cyclophilin-B (CypB), has been implicated in inflammatory conditions. These cyclophilins interact with the CD147 receptor, which plays a role in the development and progression of the inflammatory response . Upon activation of T lymphocytes, both intra- and extracellular levels of CypC increase, leading to cell migration towards circulating CypA and CypB as chemoattractants .

Recombinant human Cyclophilin-C is produced using recombinant DNA technology, which involves inserting the gene encoding CypC 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 .

Recombinant Cyclophilin-C is used in various research applications, including studies on protein folding, enzyme kinetics, and drug interactions. It is also valuable in investigating the role of cyclophilins in inflammatory diseases and developing potential therapeutic agents targeting these enzymes .