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Cyclophilin A (human), (recombinant)

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Activity	Catalyzes the cis-trans-isomeration of X-Pro-peptide bonds. The protein folding that is limited by the isomeration of X-Pro-peptide bonds can be accelerated by cyclophilin A. Also binds to cyclosporins and the cyclophilin A/cyclosporin A (Prod. No. BML-SE163).
Alternative Name	Peptidylproline cis-trans-isomerase
Application Notes	Catalyzes the cis-trans-isomerization of X-Pro-peptide bonds. Protein folding reactions that are limited by the isomerization of X-Pro-peptide bonds are accelerated by cyclophilin A. Cyclophilin A binds tightly to the immunosuppressive agent Cyclosporin A. This complex binds calcineurin (PP2B) and inhibits its phosphatase activity.
Endotoxin Content	Packaged under sterile conditions with a maximum endotoxin content of 0.1 EU/μg determined using the chromogenic Limulus amebocyte lysate (LAL) test.
Formulation	Liquid. In 20 mM TRIS-HCl, pH 7.8.
MW	18kDa
Purity	≥95% (SDS-PAGE)
Purity Detail	Purified by multi-step chromatography.
Source	Produced in E. coli.
UniProt ID	P62937

Use/Stability	Caution: Loss of protein may occur at high dilutions due to adsorption to container surfaces. Freezing of the enzyme or storage of the enzyme in diluted form could lead to loss of activity. In order to best maintain the endotoxin specification and peptidyl prolyl isomerase activity, it is recommended that aliquots be withdrawn with sterile pipet tips, if possible under a sterile hood.
Long Term Storage	+4°C
Shipping	Blue Ice

Regulatory Status	RUO – Research Use Only

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Immunosuppressant

Alternative Name	Protein phosphatase 2B, PP2B
Purity	≥90% (SDS-PAGE)
Source	Produced in E. coli. Human calcineurin Aα (MW 60kDa) and calcineurin B (MW 15kDa) heterodimer. Both subunits are coexpressed in a construct with yeast myristoyl-CoA:protein N-myristoyltransferase. The resulting highly active calcineurin (protein phosphatase 2B) is N-myristoylated on the CaNB subunit, similar to the native protein.

Last modified: May 29, 2024

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