Peptidyl-prolyl cis-trans isomerase F, mitochondrial

E2334Mo

Sandwich

48T,96T

5.49ng/L

10-2000ng/L

Serum, plasma, cell culture supernates

Mouse

2-8ºC

1h 30m

PPIase that catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and may therefore assist protein folding (By similarity). Involved in regulation of the mitochondrial permeability transition pore (mPTP) (PubMed:15800626, PubMed:15800627, PubMed:16103352, PubMed:18684715, PubMed:31489369). It is proposed that its association with the mPTP is masking a binding site for inhibiting inorganic phosphate (Pi) and promotes the open probability of the mPTP leading to apoptosis or necrosis; the requirement of the PPIase activity for this function is debated (PubMed:15800626, PubMed:15800627, PubMed:16103352, PubMed:18684715, PubMed:31489369). In cooperation with mitochondrial p53/TP53 is involved in activating oxidative stress-induced necrosis (PubMed:22726440). Involved in modulation of mitochondrial membrane F1F0 ATP synthase activity and regulation of mitochondrial matrix adenine nucleotide levels (PubMed:19801635, PubMed:21281446). Has anti-apoptotic activity independently of mPTP and in cooperation with BCL2 inhibits cytochrome c-dependent apoptosis (By similarity).

21,737

105675

Cyclophilin D;Cyclophilin F;Cyp;CyP-;CypD;CyP-D;CyP-F;Peptidyl-prolyl cis-trans isomerase F, mitochondrial;PPIase;PPIase F;PPIF;Rotamase F

Ppif

Others

PPIF