PPIL2 Human
Description
Product Specs
MGSSHHHHHH SSGLVPRGSH MGKRQHQKDK MYITCAEYTH FYGGKKPDLP QTNFRRLPFD HCSLSLQPFV YPVCTPDGIV FDLLNIVPWL KKYGTNPSNG EKLDGRSLIK LNFSKNSEGK YHCPVLFTVF TNNTHIVAVR TTGNVYAYEA VEQLNIKAKN FRDLLTDEPF SRQDIITLQD PTNLDKFNVS NFYHVKNNMK IIDPDEEKAK QDPSYYLKNT NAETRETLQE YKEFKGDEI LAATMKAPEK KKVDKLNAAH YSTGKVSASF TSTAMVPETT EAAAIDEDV LRYQFVKKKG YVRLHTNKGD LNLELHCDLT PKTCENFIRL CKKHYYDGTI FHRSIRNFVI QGGDPTGTGT GGESYWGKPF KDEFRPNLSH TGRGILSMAN SGPNSNRSQF FITFRSCAYL DKKHTIFGRV VGGFDVLTAM ENVESDPKTD RPKEEIRIDA TTVFVDPYEE ADAQIAQERK TQLKVAPETK VKSSQPQAGS QGPQTFRQGV GKYINPAATE QQRKSPQPVP LSPCPRRSPV GVLGTSAPGS SRLPDDH.
Product Science Overview
Cyclophilin-60 (Cyp60) is a member of the cyclophilin family of peptidyl-prolyl isomerases (PPIases), which are enzymes that catalyze the cis-trans isomerization of proline imidic peptide bonds in proteins. This family of enzymes is highly conserved and ubiquitous, playing crucial roles in various cellular processes, including protein folding, immunosuppression, and viral infection .
Cyclophilins, including Cyp60, are characterized by their ability to bind cyclosporin A (CsA), an immunosuppressive drug widely used in organ transplantation to prevent rejection. The binding of CsA to cyclophilins inhibits their PPIase activity, which is essential for their role in protein folding and function .
Cyp60, like other cyclophilins, has a conserved domain structure that includes a peptidyl-prolyl isomerase domain. This domain is responsible for the enzyme’s catalytic activity, facilitating the proper folding of proteins by accelerating the interconversion between cis and trans forms of proline residues .
Cyclophilins, including Cyp60, are involved in various biological processes. They act as chaperones, assisting in the proper folding of newly synthesized proteins and preventing the aggregation of misfolded proteins. Additionally, cyclophilins play a role in the immune response by modulating the activity of immune cells and influencing the production of cytokines .
Cyp60 has been implicated in several physiological and pathological processes. For instance, it has been shown to interact with HIV-1 virions, facilitating their replication and infection. This interaction makes cyclophilins potential targets for antiviral therapies .
Recombinant human cyclophilin-60 (rhCyp60) is produced using recombinant DNA technology, which involves the insertion of the human Cyp60 gene into a suitable expression system, such as bacteria or yeast. This allows for the large-scale production of the protein for research and therapeutic purposes.
Recombinant cyclophilins, including rhCyp60, are valuable tools in biochemical and pharmacological studies. They are used to investigate the structure-function relationships of cyclophilins, their interactions with ligands such as CsA, and their roles in various cellular processes. Additionally, recombinant cyclophilins are employed in drug discovery efforts to develop isoform-selective inhibitors that can modulate cyclophilin activity for therapeutic benefit .
The study of cyclophilins, including Cyp60, has significant implications for understanding and treating various diseases. For example, cyclophilin inhibitors are being explored as potential therapies for viral infections, including HIV and hepatitis C, as well as for inflammatory and autoimmune diseases .
Furthermore, the development of isoform-specific cyclophilin inhibitors holds promise for targeted therapies with reduced side effects. By selectively inhibiting specific cyclophilin isoforms, researchers aim to achieve therapeutic benefits while minimizing the impact on other cellular processes .
In conclusion, Cyclophilin-60 (Human Recombinant) is a crucial member of the cyclophilin family with diverse roles in cellular processes and disease mechanisms. Its study and application in research and therapy continue to advance our understanding of protein folding, immune regulation, and potential therapeutic interventions.
