Enzymes
Product List
Cyclophilin A E.Coli
Cyclophilin A E.Coli Recombinant
Cyclophilin A is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Cyclophilin A Human
Cyclophilin-A Human Recombinant
PPIase-A is purified by proprietary chromatographic techniques.
Cyclophilin A Mouse
Cyclophilin A Mouse Recombinant
Cyclophilin A is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Cyclophilin A Rat
Cyclophilin-A Rat Recombinant
Cyclophilin B Human
Cyclophilin-B Human Recombinant
PPIB is purified by proprietary chromatographic techniques.
Cyclophilin B Human, His
Cyclophilin-B Human Recombinant, His Tag
Cyclophilin B Mouse
Cyclophilin-B Mouse Recombinant
Cyclophilin B Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 207 amino acids (34-216 a.a) and having a molecular mass of 22.7kDa.
Cyclophilin B is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Cyclophilin C Human
Cyclophilin-C Human Recombinant
Cyclophilin D Human
Cyclophilin-D Human Recombinant
The Cyclophilin-D is purified by proprietary chromatographic techniques.
Cyclophilin D Human, His
Cyclophilin-D Human Recombinant, His Tag
Cyclophilin-D is fused to a 20 aa His Tag at N-terminus and is purified by proprietary chromatographic techniques.
Introduction
Cyclophilins (CyPs) are a family of proteins known for their ability to bind to the immunosuppressant drug cyclosporin A . They are peptidyl-prolyl cis-trans isomerases (PPIases) that catalyze the isomerization of peptide bonds at proline residues, facilitating protein folding . Cyclophilins are found in all domains of life and are classified into various isoforms, including Cyclophilin A, B, C, and D .
Cyclophilins exhibit several key biological properties:
- Expression Patterns: Cyclophilins are ubiquitously expressed in various tissues and cells . Cyclophilin A (CypA) is the most abundantly expressed isoform in human cells .
- Tissue Distribution: Cyclophilins are found in the cytoplasm, endoplasmic reticulum, nucleus, mitochondria, and even secreted outside the cell . For example, Cyclophilin D is located in the mitochondrial matrix .
Cyclophilins play crucial roles in various biological processes:
- Protein Folding: They assist in the proper folding of proteins by catalyzing the cis-trans isomerization of proline residues .
- Immune Responses: Cyclophilin A is involved in immune responses by modulating the activity of immune cells and cytokine production .
- Pathogen Recognition: Cyclophilins interact with viral proteins, aiding in the replication and infection processes of viruses such as HIV-1 .
Cyclophilins interact with other molecules and cells through various mechanisms:
- Binding Partners: Cyclophilin A binds to the HIV-1 capsid protein, modulating viral infectivity . It also forms complexes with cyclosporin A to inhibit calcineurin, a phosphatase involved in T-cell activation .
- Downstream Signaling Cascades: Cyclophilin D regulates the mitochondrial permeability transition pore, affecting cell death pathways .
The expression and activity of cyclophilins are controlled by several regulatory mechanisms:
Cyclophilins have significant applications in biomedical research and therapeutic strategies:
- Biomedical Research: Cyclophilins are studied for their roles in diseases such as cancer, cardiovascular diseases, and neurodegenerative disorders .
- Diagnostic Tools: Cyclophilin levels can serve as biomarkers for certain diseases .
- Therapeutic Strategies: Cyclophilin inhibitors, such as cyclosporin A, are used to prevent organ transplant rejection and treat viral infections .
Cyclophilins play essential roles throughout the life cycle:
