PPIL1 Human
Description
Product Specs
MAAIPPDSWQ PPNVYLETSM GIIVLELYWK HAPKTCKNFA ELARRGYYNG TKFHRIIKDF MIQGGDPTGT GRGGASIYGK QFEDELHPDL KFTGAGILAM ANAGPDTNGS QFFVTLAPTQ WLDGKHTIFG RVCQGIGMVN RVGMVETNSQ DRPVDDVKII KAYPSGLEHH HHHH.
Product Science Overview
Peptidylprolyl isomerases (PPIases) are a family of enzymes that catalyze the cis-trans isomerization of peptide bonds at proline residues. This isomerization is crucial for protein folding, function, and regulation. Among the PPIases, the cyclophilin family is particularly notable for its role in various biological processes and its interaction with immunosuppressive drugs like cyclosporin A.
Cyclophilin-like 1 (CYP1) is a member of the cyclophilin family of PPIases. It shares structural and functional similarities with other cyclophilins but also exhibits unique characteristics that distinguish it from its counterparts.
Cyclophilin-like 1, like other cyclophilins, possesses a conserved domain responsible for its isomerase activity. This domain facilitates the conversion between cis and trans isomers of proline residues, which is essential for proper protein folding and function. The enzyme’s activity is critical in various cellular processes, including signal transduction, transcription, and cell cycle regulation .
Cyclophilin-like 1 plays a significant role in several physiological and pathological processes. It is involved in protein folding and trafficking, immune response modulation, and cellular stress responses. The enzyme’s ability to interact with various substrates and its involvement in multiple signaling pathways underscore its importance in maintaining cellular homeostasis .
Recombinant human cyclophilin-like 1 is produced using recombinant DNA technology, which involves inserting the gene encoding the enzyme into a suitable expression system, such as bacteria or yeast. This allows for the large-scale production of the enzyme for research and therapeutic purposes. Recombinant cyclophilin-like 1 retains the structural and functional properties of the native enzyme, making it a valuable tool for studying its biological roles and potential applications in medicine .
The recombinant form of cyclophilin-like 1 is widely used in biochemical and structural studies to understand its function and interactions with other molecules. Additionally, it serves as a model for developing isoform-specific inhibitors that could be used to modulate its activity in various diseases. The enzyme’s involvement in immune response regulation also makes it a potential target for therapeutic interventions in autoimmune diseases and organ transplantation .
