Cyclophilin F Rat

Cyclophilin F, also known as Peptidyl-prolyl cis-trans isomerase F (PPIase F), is a mitochondrial protein that plays a crucial role in protein folding and mitochondrial function. The recombinant form of Cyclophilin F from rats is often used in research to study its functions and interactions.

Recombinant Rat Cyclophilin F is typically produced in Escherichia coli expression systems. The protein is a single, non-glycosylated polypeptide chain containing 200 amino acids, with a molecular mass of approximately 21.2 kDa . It is often fused to a His-tag at the N-terminus to facilitate purification .

Cyclophilin F accelerates the folding of proteins by catalyzing the cis-trans isomerization of proline imidic peptide bonds in oligopeptides . It is involved in the regulation of the mitochondrial permeability transition pore (mPTP), which is crucial for maintaining mitochondrial function and integrity . Cyclophilin F, in cooperation with mitochondrial TP53, plays a role in activating oxidative stress-induced necrosis .

Additionally, Cyclophilin F modulates the activity of mitochondrial membrane F1F0 ATP synthase and regulates mitochondrial matrix adenine nucleotide levels . It also exhibits anti-apoptotic activity independently of mPTP and, in cooperation with BCL2, inhibits cytochrome c-dependent apoptosis .

Recombinant Cyclophilin F is used in various biochemical and cell biology studies to understand its role in mitochondrial function and apoptosis. It is also utilized in studies investigating the mechanisms of oxidative stress and necrosis .

Recombinant Rat Cyclophilin F is typically stored at 4°C if used within 2-4 weeks. For longer storage, it is recommended to keep it frozen at -20°C with the addition of a carrier protein to prevent degradation . The protein is stable and retains its activity under these conditions.