Recombinant Human Peptidyl-prolyl Cis-trans Isomerase A/Cyclophilin A/CYPA

Source: E.coli.
MW :18kD.
Recombinant Human Peptidyl-prolyl Cis-trans Isomerase A is produced by our E.coli expression system and the target gene encoding Met1-Glu165 is expressed. Peptidyl-prolyl cis-trans isomerase A is a member of the peptidyl-prolyl cis-trans isomerase (PPIase) family, which catalyzes the cis-trans isomerization of proline imidic peptide bonds. Cyclophilin A regulate many biological processes, including intracellular signaling, transcription, inflammation, and apoptosis. Cyclophilin is also incorporated into many viruses, including HIV1, where it has been speculated to be involved in functions such as viral assembly and infectivity. The immunosuppressive activity of cyclosporins has been correlated with their ability to form complexes with cyclophilins that inhibit calcineurin phosphatase activity and prevent incorporation of cyclophilin into viral particles. The cyclosporin/cyclophilin complex selectively binds and inactivates calcineurin, making it a useful inhibitor for studying calcineurin activity.

Endotoxin : Less than 0.1 ng/µg (1 IEU/µg) as determined by LAL test.

For Research Use Only. Not for use in diagnostic/therapeutics procedures.

Subcellular location:	Cytoplasm, Secreted
Post transnational modification:	Acetylation at Lys-125 markedly inhibits catalysis of cis to trans isomerization and stabilizes cis rather than trans forms of the HIV-1 capsid. PPIA acetylation also antagonizes the immunosuppressive effects of cyclosporine by inhibiting the sequential steps of cyclosporine binding and calcineurin inhibition.
BioGrid:	111474. 112 interactions.

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