Peptidyl-prolyl isomerases

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C7696 Cyclophilin A from calf thymus powder Cyclophilins are peptidyl prolyl isomerases that catalyze the cis-trans isomerization of X-Pro peptide bonds. They are highly-conserved cytoplasmic enzymes that accelerate protein folding and facilitate HIV infectivity. Cyclosporin A binds to cyclophilin and inhibits its activity. The cyclosporin A-cyclophilin complex binds to calcineurin and inhibits T-cell activation. The structure of human, recombinant cyclophilin is given by Holzman, et al.
C3805 Cyclophilin A human ≥95% (SDS-PAGE), recombinant, expressed in E. coli, buffered aqueous solution Cyclophilins are peptidyl prolyl isomerases that catalyze the cis-trans isomerization of X-Pro peptide bonds. They are highly-conserved cytoplasmic enzymes that accelerate protein folding and facilitate HIV infectivity. Cyclosporin A binds to cyclophilin and inhibits its activity. The cyclosporin A-cyclophilin complex binds to calcineurin and inhibits T-cell activation. The structure of human, recombinant cyclophilin is given by Holzman, et al.
F5398 FK-Binding Protein human recombinant, expressed in E. coli Enzyme which catalyzes cis-trans isomerization of X-Pro peptide bonds (i.e., a peptidyl prolyl isomerase) in synthetic substrates.