Cyclophilin F Rat Bioactive

Cyclophilin-F Rat Recombinant Bioactive
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Description

Biological Activity

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) .

Research Applications

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 .

Selectivity and Inhibitor Development

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 .

Key Synonyms

  • Peptidyl-prolyl cis-trans isomerase F (PPIase F)

  • Cyclophilin D (CypD)

  • Rotamase F .

Product Specs

Introduction
PPIF, a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family, plays a crucial role in protein folding by catalyzing the cis-trans isomerization of proline imidic peptide bonds within oligopeptides. As a key component of the mitochondrial permeability transition pore in the inner mitochondrial membrane, PPIF activation is believed to be involved in triggering both apoptotic and necrotic cell death.
Description
Recombinant Cyclophilin F Rat, produced in E. coli, is a single, non-glycosylated polypeptide chain composed of 200 amino acids (specifically, residues 30-206). It has a molecular weight of 21.2 kDa. This Cyclophilin F variant is fused to a 23 amino acid His-tag at its N-terminus and is purified using proprietary chromatographic techniques.
Physical Appearance
The product is a clear, sterile solution without any color.
Formulation
The Cyclophilin F protein solution is provided at a concentration of 1 mg/ml. It is formulated in a buffer consisting of Phosphate Buffered Saline (pH 7.4), 10% glycerol, and 1mM DTT.
Stability
For short-term storage (2-4 weeks), the product should be kept at 4°C. For longer storage, it is recommended to freeze the product at -20°C. To ensure optimal stability during long-term storage, consider adding a carrier protein like HSA or BSA (0.1%). It's important to avoid repeated freezing and thawing of the product.
Purity
The purity of the product is greater than 90%, as determined by SDS-PAGE analysis.
Biological Activity
The specific activity of the enzyme is measured as greater than 1,300 nmol/min/mg. This is determined by measuring the amount of enzyme required to cleave 1 nmol of the substrate suc-AAFP-PNA per minute at a temperature of 37°C in a Tris-HCl buffer at pH 8.0 using chymotrypsin.
Synonyms
Peptidyl-prolyl cis-trans isomerase F, mitochondrial, PPIase F, Cyclophilin D, CyP-D, CypD, Cyclophilin F, Rotamase F.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSCSDGGAR GANSSSQNPL VYLDVGADGQ PLGRVVLELK ADVVPKTAEN FRALCTGEKG FGYKGSTFHR VIPAFMCQAG DFTNHNGTGG KSIYGSRFPD ENFTLKHVGP GVLSMANAGP NTNGSQFFIC TIKTDWLDGK HVVFGHVKEG MDVVKKIESF GSKSGKTSKK IVITDCGQLS.

Product Science Overview

Molecular Properties
  • Amino Acid Sequence: Cyclophilin-F (Rat Recombinant Bioactive) consists of 200 amino acids, specifically from positions 30 to 206 .
  • Molecular Mass: The molecular mass of this recombinant protein is approximately 21.2 kDa .
  • Tag: It is fused to a 23 amino acid His-tag at the N-terminus, which aids in purification .
Production and Purification

Cyclophilin-F (Rat Recombinant Bioactive) is produced in Escherichia coli (E. coli) as a single, non-glycosylated polypeptide chain . The protein is purified using proprietary chromatographic techniques to ensure high purity, typically greater than 90% as determined by SDS-PAGE .

Biological Activity

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 .

Applications and Storage

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 .

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