Cyclophilin D Human, His

Cyclophilin-D Human Recombinant, His Tag

Recombinant Human Cyclophilin-D, expressed in E. coli, is a non-glycosylated polypeptide chain containing 390 amino acids (including a 20 aa His Tag at the N-terminus), resulting in a molecular weight of 42.9kDa. Purification is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT3252
Source
Escherichia Coli.
Appearance
Clear, colorless solution, sterile-filtered.

Cyclophilin E Human

Cyclophilin-E Human Recombinant

Recombinant Human Cyclophilin-E, expressed in E. coli, is a non-glycosylated polypeptide chain with a molecular weight of 37.5 kDa. This single-chain protein comprises 337 amino acids (1-301 a.a.) and includes a 36 amino acid His Tag fused at the N-terminus. Purification is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT3385
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

Cyclophilin F Rat

Cyclophilin F Rat Recombinant

Recombinant Cyclophilin F from Rat, expressed in E. coli, is a single, non-glycosylated polypeptide chain containing 200 amino acids (residues 30-206). It has a molecular weight of 21.2 kDa and includes a 23 amino acid His-tag at the N-terminus. The protein is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT3422
Source
Escherichia Coli.
Appearance
Clear, sterile-filtered solution.

Cyclophilin F Rat Bioactive

Cyclophilin-F Rat Recombinant Bioactive

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.
Shipped with Ice Packs
Cat. No.
BT3483
Source
Escherichia Coli.
Appearance
The product is a clear, sterile solution without any color.

Cyclophilin G Human

Cyclophilin-G Human Recombinant

Recombinant human Cyclophilin-G, produced in E. coli, is a single, non-glycosylated polypeptide chain comprising 195 amino acids (1-175 a.a.) with a molecular weight of 21.6 kDa. This protein includes a 20 amino acid His Tag fused at the N-terminus and undergoes purification via proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT3528
Source
Escherichia Coli.
Appearance
A clear, colorless solution that has been sterilized by filtration.

Cyclophilin A Rat

Cyclophilin-A Rat Recombinant

Recombinant Cyclophilin-A from Rat, produced in E. coli, is a single, non-glycosylated polypeptide chain. It consists of 173 amino acids, including a 10 amino acid His tag located at the N-terminus, and encompasses amino acids Val2 to Leu164. The calculated molecular mass of the protein is 19kDa.
Shipped with Ice Packs
Cat. No.
BT2927
Source
Escherichia Coli.
Appearance
White powder, lyophilized (freeze-dried) and filtered.

Cyclophilin B Human

Cyclophilin-B Human Recombinant

Recombinant Human Cyclophilin-B, produced in E. coli, is a single, non-glycosylated polypeptide chain consisting of 192 amino acids (26-216) with a molecular weight of 21.2 kDa. PPIB is purified using proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT2984
Source
Escherichia Coli.
Appearance
Clear, colorless, and sterile-filtered solution.

Cyclophilin B Human, His

Cyclophilin-B Human Recombinant, His Tag

Recombinant Human Cyclophilin-B, expressed in E. coli, is a single, non-glycosylated polypeptide chain encompassing amino acids Asp34 to Glu216 (193 amino acids total) and containing a 10-amino acid His tag at the N-terminus. The calculated molecular mass is 22 kDa.
Shipped with Ice Packs
Cat. No.
BT3035
Source
Escherichia Coli.
Appearance
White lyophilized (freeze-dried) powder.

Cyclophilin B Mouse

Cyclophilin-B Mouse Recombinant

Recombinant Cyclophilin B from Mouse, produced in E. coli, is a single, non-glycosylated polypeptide chain encompassing amino acids 34-216 (totaling 207 amino acids). With a molecular weight of 22.7 kDa, it features a 24 amino acid His-tag at the N-terminus. Purification is achieved through proprietary chromatographic techniques.
Shipped with Ice Packs
Cat. No.
BT3080
Source
Escherichia Coli.
Appearance
A clear and colorless solution, sterilely filtered.

Cyclophilin C Human

Cyclophilin-C Human Recombinant

Recombinant Cyclophilin-C, of human origin, is produced in E. coli. It is a single, non-glycosylated polypeptide chain encompassing amino acids Phe29 to Trp212 (194 amino acids total), including an N-terminal 10-amino acid His tag. The calculated molecular mass is 21.3 kDa.
Shipped with Ice Packs
Cat. No.
BT3148
Source
Escherichia Coli.
Appearance
The product appears as a white lyophilized (freeze-dried) powder after filtration.
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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