| Description: | Peptidyl-prolyl cis-trans isomerase A (CYP A) catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. This enzyme plays a multifaceted role, exerting a strong chemotactic effect on leukocytes through the activation of its membrane receptor BSG/CD147, initiating a signaling cascade culminating in MAPK/ERK activation. Additionally, CYP A activates endothelial cells (ECs) in a pro-inflammatory manner, inducing NF-kappa-B and MAP-kinase signaling, and upregulating adhesion molecules. It induces apoptosis in ECs, promoting FOXO1-dependent expression of CCL2 and BCL2L11. In response to oxidative stress, CYP A initiates proapoptotic and antiapoptotic signaling in ECs. It negatively regulates MAP3K5/ASK1 kinase activity and is necessary for the assembly of TARDBP in heterogeneous nuclear ribonucleoprotein complexes, regulating TARDBP binding to RNA. CYP A also plays a crucial role in platelet activation and aggregation, regulates calcium mobilization, and facilitates integrin ITGA2B:ITGB3 bidirectional signaling. Moreover, it inhibits replication of influenza A virus and may act as a mediator between the SARS coronavirus nucleoprotein and BSG/CD147 during virus invasion of host cells. Peptidyl-prolyl cis-trans isomerase A/CYPA Protein, Human is the recombinant human-derived Peptidyl-prolyl cis-trans isomerase A/CYPA protein, expressed by E. coli , with tag free. The total length of Peptidyl-prolyl cis-trans isomerase A/CYPA Protein, Human is 165 a.a., with molecular weight of 16-18 kDa. |
