Cyclophilin A E.Coli
Description
Cyclophilin A is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Product Specs
Product Science Overview
Cyclophilin A (CypA), also known as peptidyl-prolyl cis-trans isomerase A (PPIase A), is a cytoplasmic protein that belongs to the cyclophilin-type PPIase family. It is widely studied due to its role in protein folding, immune response, and its interaction with various viral proteins, including those of HIV.
Cyclophilin A is a highly conserved protein found in organisms ranging from prokaryotes to humans. It exhibits peptidyl-prolyl isomerase activity, which catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. This activity is crucial for accelerating the folding of proteins, making Cyclophilin A an essential player in cellular processes.
Recombinant Cyclophilin A is often expressed in Escherichia coli (E. coli) for research and therapeutic purposes. The gene encoding human Cyclophilin A is cloned into an expression vector, such as pET22b(+), and transformed into an E. coli strain like BL21(DE3). The recombinant protein is then produced in the bacterial cytoplasm, where it can constitute up to 50% of the total cell protein .
The purification of recombinant Cyclophilin A typically involves a single-step tandem anion exchange chromatography on DEAE- and Q-Sepharose columns. This method ensures high purity (up to 95%) and minimal endotoxin contamination, meeting the standards for injectable preparations . The purified protein retains its functional properties, including isomerase and chemokine activities.
Recombinant Cyclophilin A has several applications in research and clinical settings. It is used to study protein folding mechanisms, immune responses, and viral interactions. Additionally, its role in stimulating the migration of hematopoietic stem cells makes it a potential candidate for therapeutic applications .
