Cyclophilin E Human

Cyclophilin-E Human Recombinant

Cyclophilin-E Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 337 amino acids (1-301 a.a.) and having a molecular mass of 37.5 kDa. Cyclophilin-E is fused to a 36 amino acids long His Tag at N-terminus and is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT3385
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.

Cyclophilin F Rat

Cyclophilin F Rat Recombinant

Cyclophilin F Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 200 amino acids (30-206a.a.) and having a molecular mass of 21.2kDa.
Cyclophilin F is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT3422
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

Cyclophilin F Rat Bioactive

Cyclophilin-F Rat Recombinant Bioactive

Cyclophilin F Rat Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 200 amino acids (30-206 a.a) and having a molecular mass of 21.2Da.
Cyclophilin F is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT3483
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.

Cyclophilin G Human

Cyclophilin-G Human Recombinant

Cyclophilin-G Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 195 amino acids (1-175 a.a.) and having a molecular mass of 21.6 kDa. Cyclophilin-G is fused to a 20 amino acid His Tag at N-terminus and is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT3528
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.

PIN1 Human

Peptidyl-Prolyl Cis/Trans Isomerase NIMA-Interacting 1 Human Recombinant

PPIase Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 163 amino acids & having a molecular mass of 18.2 kDa.
The PIN1 is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT3595
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.

PIN1 Mouse

Peptidyl-Prolyl Cis/Trans Isomerase NIMA-Interacting 1 Mouse Recombinant

PIN1 Mouse Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 188 amino acids (1-165 a.a) and having a molecular mass of 20.8kDa. PIN1 is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Shipped with Ice Packs
Cat. No.
BT3677
Source
Escherichia Coli.
Appearance
Sterile Filtered clear solution.

PPIF Human

Cyclophilin-F Human Recombinant

PPIF Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 198 amino acids (30-207) and having a molecular mass of 21 kDa. The PPIF is fused to a 20 amino acid His tag at N-terminus and is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT3749
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.

PPIH Human

Cyclophilin-H Human Recombinant

PPIH Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 177 amino acids (1-177) and having a molecular mass of 19.2 kDa.
PPIH is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT3833
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.

PPIH Human, His

Cyclophilin-H Human Recombinant, His Tag

PPIH Human Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain (a.a 2-177) containing 186 amino acids and including a 10 a.a N-terminal His tag. The total molecular mass is 20.3kDa (calculated).
Shipped with Ice Packs
Cat. No.
BT3918
Source
Escherichia Coli.
Appearance
Filtered White lyophilized (freeze-dried) powder.

PPIL1 Human

Peptidylprolyl Isomerase (Cyclophilin)-Like 1 Human Recombinant

PPIL1 Human Recombinant protein produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 174 amino acids (1-166) and having a molecular mass of 19.3 kDa. PPIL1 is fused to 8 amino acid His Tag at C-terminus and is purified by proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT4024
Source
Escherichia Coli.
Appearance
Sterile filtered colorless solution.
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:

  • Transcriptional Regulation: Cyclophilin genes are regulated at the transcriptional level by various transcription factors .
  • Post-Translational Modifications: Cyclophilins undergo post-translational modifications such as phosphorylation, which can alter their activity and interactions .
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:

  • Development: Cyclophilins are involved in embryonic development by regulating protein folding and cellular signaling .
  • Aging and Disease: Cyclophilins contribute to the aging process and the development of age-related diseases by modulating stress responses and protein homeostasis .
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