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Product List
Cyclophilin D Human
Cyclophilin-D Human Recombinant
Recombinant Human Cyclophilin-D, expressed in E. coli, is a single, non-glycosylated polypeptide chain with a molecular weight of 18.9 kDa, comprising 178 amino acids. Purification is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs 
Cat. No.
BT3207
Source
Escherichia Coli.
Appearance
Clear, colorless solution, sterile filtered.
Cyclophilin A E.Coli
Cyclophilin A E.Coli Recombinant
Recombinant Cyclophilin A, derived from E. coli, is a single, non-glycosylated polypeptide chain comprising 189 amino acids (25-190a.a.) with a molecular weight of 20.5 kDa. This protein is expressed with a 23 amino acid His-tag fused to its N-terminus and is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cyclophilin A Human
Cyclophilin-A Human Recombinant
Recombinant Human Cyclophilin-A, expressed in E. coli, is a non-glycosylated polypeptide with a 20 amino acid His tag at its N-terminus. This protein consists of 185 amino acids (including the His tag; the native protein sequence comprises residues 1-165) and has a molecular weight of 20 kDa. Purification is achieved through proprietary chromatographic techniques, resulting in a single polypeptide chain.
Shipped with Ice Packs
Cat. No.
BT2717
Source
Escherichia Coli.
Appearance
A clear, colorless solution free from particulate matter.
Cyclophilin A Mouse
Cyclophilin A Mouse Recombinant
Recombinant Mouse Cyclophilin A protein was expressed in E. coli. It is a single, non-glycosylated polypeptide chain containing 187 amino acids (1-164a.a.) and having a molecular mass of 20.4 kDa. The protein is fused to a 23 amino acid His-tag at the N-terminus and is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT2777
Source
E.coli.
Appearance
Clear, colorless, and sterile-filtered solution.
PPIH Human, His
Cyclophilin-H Human Recombinant, His Tag
Recombinant Human PPIH, expressed in E. coli, is a non-glycosylated polypeptide chain containing 186 amino acids (a.a 2-177). This includes a 10 a.a N-terminal His tag, resulting in a calculated molecular mass of 20.3 kDa.
Shipped with Ice Packs
PPIL1 Human
Peptidylprolyl Isomerase (Cyclophilin)-Like 1 Human Recombinant
Recombinant human PPIL1 protein, expressed in E. coli, is a single, non-glycosylated polypeptide chain. It consists of 174 amino acids, with amino acids 1-166 representing the PPIL1 sequence, and has a molecular weight of 19.3 kDa. An 8 amino acid His tag is fused to the C-terminus of PPIL1. The protein is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT4024
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.
PPIL2 Human
Cyclophilin-60 Human Recombinant
Recombinant human PPIL2, with a 20 amino acid His Tag at the N-terminus, is produced in E. coli. This protein is a single, non-glycosylated polypeptide chain consisting of 547 amino acids (1-527 a.a.) with a molecular weight of 61.6 kDa. The purification of PPIL2 is achieved using proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT4110
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.
PPIL3 Human
Cyclophilin-J Human Recombinant
Recombinant human PPIL3, expressed in E. coli, is a non-glycosylated polypeptide chain. It consists of 181 amino acids, with a 20 amino acid His-tag attached to the N-terminus (total length: 1-161 a.a.), resulting in a molecular weight of 20.3kDa. Purification is achieved using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT4191
Source
Escherichia Coli.
Appearance
A clear, colorless solution, sterile-filtered.
PPIL4 Human
Peptidylprolyl Isomerase (Cyclophilin)-Like 4 Human Recombinant
Recombinant human PPIL4, expressed in E. coli, is a single, non-glycosylated polypeptide chain with a molecular weight of 59.4 kDa. It consists of 512 amino acids, including a 20 amino acid His tag at the N-terminus (1-492 a.a.). Purification is achieved through proprietary chromatographic methods.
Shipped with Ice Packs
Cat. No.
BT4271
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.
PIN1 Human
Peptidyl-Prolyl Cis/Trans Isomerase NIMA-Interacting 1 Human Recombinant
Recombinant Human PPIase, produced in E. Coli, is a single, non-glycosylated polypeptide chain. It consists of 163 amino acids, resulting in a molecular mass of 18.2 kDa. The PIN1 protein undergoes purification using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT3595
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.
Introduction
Definition and Classification
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 .
Biological Properties
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 .
Biological Functions
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 .
Modes of Action
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 .
Regulatory Mechanisms
The expression and activity of cyclophilins are controlled by several regulatory mechanisms:
Applications
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 .
Role in the Life Cycle
Cyclophilins play essential roles throughout the life cycle:
