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207000 Calcineurin Autoinhibitory Peptide - Calbiochem

207000
Purchase on Sigma-Aldrich

Overview

Replacement Information

Key Spec Table

Empirical Formula
C₁₂₄H₂₀₅N₃₉O₃₉S₂

Products

Catalogue NumberPackaging Qty/Pack
207000-250UG Plastic ampoule 250 μg
Description
OverviewSpecific 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.
Catalogue Number207000
Brand Family Calbiochem®
SynonymsITSFEEAKGLDRINERMPPRRDAMP
References
ReferencesPerrino, 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.
Product Information
ATP CompetitiveN
FormLyophilized
FormulationSupplied as a trifluoroacetate salt.
Hill FormulaC₁₂₄H₂₀₅N₃₉O₃₉S₂
Chemical formulaC₁₂₄H₂₀₅N₃₉O₃₉S₂
Hygroscopic Hygroscopic
ReversibleN
Sold on the basis of peptide contentY
Quality LevelMQ100
Applications
Biological Information
Primary TargetMn2+-stimulated calcineurin activity
Primary Target IC<sub>50</sub>10 µM using 32P-myosin light chain as a substrate
Purity≥97% by HPLC
Physicochemical Information
Cell permeableN
Peptide ContentY
Peptide SequenceH-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
Dimensions
Materials Information
Toxicological Information
Safety Information according to GHS
Safety Information
Product Usage Statements
Storage and Shipping Information
Ship Code Ambient Temperature Only
Toxicity Standard Handling
Storage -20°C
Hygroscopic Hygroscopic
Do not freeze Ok to freeze
Special InstructionsFollowing reconstitution, aliquot and freeze (-20°C). Aqueous stock solutions are stable for up to 2 months at -20°C.
Packaging Information
Transport Information
Supplemental Information
Specifications

Documentation

Calcineurin Autoinhibitory Peptide - Calbiochem SDS

Title

Safety Data Sheet (SDS) 

Calcineurin Autoinhibitory Peptide - Calbiochem Certificates of Analysis

TitleLot Number
207000

References

Reference overview
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.

Brochure

Title
Protein Phosphatases Technical Bulletin
Data Sheet

Note that this data sheet is not lot-specific and is representative of the current specifications for this product. Please consult the vial label and the certificate of analysis for information on specific lots. Also note that shipping conditions may differ from storage conditions.

Revision20-October-2008 JSW
SynonymsITSFEEAKGLDRINERMPPRRDAMP
DescriptionCorresponds 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.
FormLyophilized
FormulationSupplied as a trifluoroacetate salt.
Chemical formulaC₁₂₄H₂₀₅N₃₉O₃₉S₂
Peptide SequenceH-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
Purity≥97% by HPLC
SolubilityH₂O
Storage -20°C
Hygroscopic
Do Not Freeze Ok to freeze
Special InstructionsFollowing reconstitution, aliquot and freeze (-20°C). Aqueous stock solutions are stable for up to 2 months at -20°C.
Toxicity Standard Handling
ReferencesPerrino, 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.