Cyclophilin F exhibits enzymatic and regulatory functions:
PPIase Activity: Catalyzes cis-trans isomerization of proline imidic peptide bonds, accelerating protein folding .
Mitochondrial Permeability Transition Pore (mPTP) Regulation: Binds to and modulates the mPTP, influencing apoptosis and necrosis .
Anti-Apoptotic Role: Cooperates with BCL2 to inhibit cytochrome c-dependent apoptosis independently of mPTP .
Specific Activity: >1,300 nmol/min/mg (measured using suc-AAFP-PNA cleavage at 37°C) .
This protein is widely used to study:
Mitochondrial Dynamics: Mechanisms of mPTP opening and its role in oxidative stress-induced necrosis .
Cell Death Pathways: Interactions with TP53 and BCL2 to regulate apoptosis .
Enzyme Kinetics: Structure-activity relationships of PPIase family members .
Recent studies highlight efforts to develop subtype-selective cyclophilin inhibitors:
CypD-Selective Inhibitors: Engineered macrocycles target non-conserved residues in the S2 pocket of Cyclophilin D (CypD), achieving >10,000-fold selectivity over other cyclophilins .
CypE-Selective Inhibitors: Reversible covalent bonding with lysine residues in CypE’s S2 pocket enables 30- to 4,000-fold selectivity .
Cyclophilin-F is a key component of the mitochondrial permeability transition pore (mPTP) in the inner mitochondrial membrane . The activation of this pore is thought to be involved in the induction of apoptotic and necrotic cell death . The specific activity of Cyclophilin-F is greater than 1,300 nmol/min/mg, defined as the amount of enzyme that cleaves 1 nmol of suc-AAPF-pNA per minute at 37°C in Tris-HCl pH 8.0 using chymotrypsin .
Cyclophilin-F (Rat Recombinant Bioactive) is used primarily for laboratory research purposes. It is not approved for use in humans or for clinical diagnosis . For storage, it is recommended to keep the protein at 4°C for short-term use (2-4 weeks) and at -20°C for long-term storage. It is advisable to avoid multiple freeze-thaw cycles to maintain protein stability .