Cyclophilin F/PPIF Protein, Human (HEK293, His)

Cyclophilin F/PPIF Protein functions as a peptidyl-prolyl cis-trans isomerase (PPIase), playing a vital role in catalyzing the cis-trans isomerization of proline imidic peptide bonds in oligopeptides, thereby potentially facilitating protein folding. Beyond its involvement in protein folding, Cyclophilin F/PPIF is a key player in the regulation of the mitochondrial permeability transition pore (mPTP), where its association with the mPTP is suggested to mask a binding site for inhibiting inorganic phosphate (Pi), ultimately promoting the open probability of the mPTP and leading to apoptosis or necrosis; however, the requirement for PPIase activity in this process is a matter of debate. Additionally, in collaboration with mitochondrial p53/TP53, Cyclophilin F/PPIF contributes to the activation of oxidative stress-induced necrosis. It further participates in modulating mitochondrial membrane F(1)F(0) ATP synthase activity and regulating mitochondrial matrix adenine nucleotide levels. Exhibiting anti-apoptotic activity independently of the mPTP, Cyclophilin F/PPIF, in cooperation with BCL2, effectively inhibits cytochrome c-dependent apoptosis, highlighting its multifaceted roles in mitochondrial function and cell survival mechanisms.