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

Cyclophilin F/PPIF Protein, a peptidyl-prolyl cis-trans isomerase (PPIase), catalyzes proline imidic peptide bond isomerization, potentially aiding in protein folding. It crucially regulates the mitochondrial permeability transition pore (mPTP), influencing apoptosis or necrosis. Collaborating with mitochondrial p53/TP53, it activates oxidative stress-induced necrosis and modulates mitochondrial membrane F(1)F(0) ATP synthase activity. Cyclophilin F/PPIF, with BCL2, inhibits cytochrome c-dependent apoptosis independently of the mPTP, highlighting its diverse roles in mitochondrial function and cell survival mechanisms. Cyclophilin F/PPIF Protein, Human (HEK293, His) is the recombinant human-derived Cyclophilin F/PPIF protein, expressed by HEK293, with C-6*His labeled tag. The total length of Cyclophilin F/PPIF Protein, Human (HEK293, His) is 178 a.a., with molecular weight of ~24-34 kDa.

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.

Human

HEK293

C-6*His

P30405 (C30-S207)

10105

CSKGSGDPSSSSSSGNPLVYLDVDANGKPLGRVVLELKADVVPKTAENFRALCTGEKGFGYKGSTFHRVIPSFMCQAGDFTNHNGTGGKSIYGSRFPDENFTLKHVGPGVLSMANAGPNTNGSQFFICTIKTDWLDGKHVVFGHVKEGMDVVKKIESFGSKSGRTSKKIVITDCGQLS

Approximately 24-34 kDa

Greater than 95% as determined by reducing SDS-PAGE.

Lyophilized powder.

Lyophilized from a 0.22 μm filtered solution of PBS, pH 7.4.

<1 EU/μg, determined by LAL method.

It is not recommended to reconstitute to a concentration less than 100 μg/mL in ddH₂O. For long term storage it is recommended to add a carrier protein (0.1% BSA, 5% HSA, 10% FBS or 5% Trehalose).

Stored at -20°C for 2 years. After reconstitution, it is stable at 4°C for 1 week or -20°C for longer (with carrier protein). It is recommended to freeze aliquots at -20°C or -80°C for extended storage.

Room temperature in continental US; may vary elsewhere.