Calcineurin Autoinhibitory Peptide - Calbiochem

General description

Corresponds to a C-terminal domain (residues 457-482) of the calmodulin-binding domain of calcineurin. Specific calcineurin inhibitor. Does not inhibit CaM kinase II, protein phosphatase I or 2A. Inhibits Mn²⁺-stimulated calcineurin activity (IC₅₀ = 10 µM using ³²P myosin light chain as a substrate) but has no effect on Ni²⁺-stimulated activity.

Specific calcineurin inhibitor. Corresponds to the C-terminal domain (residues 457-482) of the calmodulin-binding domain of calcineurin (PP2B). Inhibits Mn²⁺-stimulated calcineurin activity (IC₅₀ = 10 µM using ³²P-myosin light chain as a substrate) but has no effect on Ni²⁺-stimulated enzyme activity. Does not inhibit CaM kinase II, protein phosphatase 1 or 2A.

Biochem/physiol Actions

Cell permeable: no

Primary Target
Mn²⁺-stimulated calcineurin activity

Product does not compete with ATP.

Reversible: no

Target IC₅₀: 10 µM using 32P-myosin light chain as a substrate

Packaging

Yes

Warning

Toxicity: Standard Handling (A)

Sequence

H-Ile-Thr-Ser-Phe-Glu-Glu-Ala-Lys-Gly-Leu-Asp-Arg-Ile-Asn-Glu-Arg-Met-Pro-Pro-Arg-Arg-Asp-Ala-Met-Pro-OH

Physical form

Supplied as a trifluoroacetate salt.

Reconstitution

Following reconstitution, aliquot and freeze (-20°C). Aqueous stock solutions are stable for up to 2 months at -20°C.

Other Notes

Perrino, B.A., et al. 1995. J. Biol. Chem. 270, 340.
Yokoyama, Y., and Wang, J.H. 1994. FEBS Lett.337, 128.
Yokoyama, N., et al. 1993. Arch. Biochem. Biophys.300, 615.
Matsui, H., et al. 1991. Biochem. Int.24, 1119.
Hashimoto, Y., et al. 1990. J. Biol. Chem.265, 1924.

Legal Information

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