476485 | PKA Inhibitor 14-22 Amide, Cell-Permeable, Myristoylated - Calbiochem

476485
Price could not be retrieved
Minimum Quantity needs to be mulitiple of
Upon Order Completion More Information
You Saved ()
 
Request Pricing
Limited AvailabilityLimited Availability
Stocked 
Discontinued
Limited Quantities Available
Available
    Remaining : Will advise
      Remaining : Will advise
      Will advise
      Contact Customer Service
      View Pricing & Availability
      Click To Print This Page

      Overview

      Replacement Information

      Key Specifications Table

      Empirical Formula
      C₅₃H₁₀₀N₂₀O₁₂

      Pricing & Availability

      Catalog NumberAvailability Packaging Qty/Pack Price Quantity
      476485-500UG
      Retrieving availability...
      Limited AvailabilityLimited Availability
      Stocked 
      Discontinued
      Limited Quantities Available
      Available
        Remaining : Will advise
          Remaining : Will advise
          Will advise
          Contact Customer Service

          Plastic ampoule 500 μg
          Retrieving price...
          Price could not be retrieved
          Minimum Quantity needs to be mulitiple of
          Upon Order Completion More Information
          You Saved ()
           
          Request Pricing
          Description
          OverviewHeat-stable protein kinase inhibitor (PKI) peptide sequence (14 - 22) that has been myristoylated at the N-terminus, enhancing its cell-permeability. The non-myristoylated version of this peptide is a highly specific inhibitor (Ki = 36 nM) of cAMP-dependent protein kinase.
          Catalogue Number476485
          Brand Family Calbiochem®
          SynonymsPKI 14-22 Amide, Cell-Permeable, Myr-GRTGRRNAI-NH₂, Myristoylated Protein Kinase A Inhibitor Amide 14-22, Cell-Permeable, Protein Kinase A Inhibitor 14-22 Amide, PKA Inhibitor XIII
          References
          ReferencesPaman, K., et al. 1998. J. Lipid Res. 39, 1091.
          Rimon, G., and Rubin M. 1998. Biochim. Biophys. Acta 1380, 289.
          Harris, T.E., et al. 1997. Biochem. Biophys. Res. Commun. 232, 648.
          Muniz, M., et al. 1997. Proc. Natl. Acad. Sci. USA 94, 14461.
          Zoukhri, D., et al. 1997. Am. J. Physiol. 272, C263.
          Eichholtz, T., et al. 1993. J. Biol. Chem. 268, 1982.
          Ward, N.E. and O’Brian, C.A. 1993. Biochemistry 32, 11903.
          Walsh, D.A. and Glass, D.B. 1991. Methods Enzymol. 201, 304.
          Glass, D.B., et al. 1989. J. Biol. Chem. 264, 8802.
          Product Information
          ATP CompetitiveN
          FormLyophilized
          FormulationSupplied as a trifluoroacetate salt.
          Hill FormulaC₅₃H₁₀₀N₂₀O₁₂
          Chemical formulaC₅₃H₁₀₀N₂₀O₁₂
          Hygroscopic Hygroscopic
          ReversibleN
          Applications
          Biological Information
          Primary TargetcAMP-dependent protein kinase
          Primary Target K<sub>i</sub>36 nMf or cAMP-dependent protein kinase
          Purity≥95% by HPLC
          Physicochemical Information
          Cell permeableY
          Peptide SequenceMyr-N-Gly-Arg-Thr-Gly-Arg-Arg-Asn-Ala-Ile-NH₂
          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). Stock solutions are stable for up to 3 months at -20°C.
          Packaging Information
          Transport Information
          Supplemental Information
          Specifications

          Documentation

          SDS

          Title

          Safety Data Sheet (SDS) 

          Certificates of Analysis

          TitleLot Number
          476485

          References

          Reference overview
          Paman, K., et al. 1998. J. Lipid Res. 39, 1091.
          Rimon, G., and Rubin M. 1998. Biochim. Biophys. Acta 1380, 289.
          Harris, T.E., et al. 1997. Biochem. Biophys. Res. Commun. 232, 648.
          Muniz, M., et al. 1997. Proc. Natl. Acad. Sci. USA 94, 14461.
          Zoukhri, D., et al. 1997. Am. J. Physiol. 272, C263.
          Eichholtz, T., et al. 1993. J. Biol. Chem. 268, 1982.
          Ward, N.E. and O’Brian, C.A. 1993. Biochemistry 32, 11903.
          Walsh, D.A. and Glass, D.B. 1991. Methods Enzymol. 201, 304.
          Glass, D.B., et al. 1989. J. Biol. Chem. 264, 8802.
          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.

          Revision11-August-2008 RFH
          SynonymsPKI 14-22 Amide, Cell-Permeable, Myr-GRTGRRNAI-NH₂, Myristoylated Protein Kinase A Inhibitor Amide 14-22, Cell-Permeable, Protein Kinase A Inhibitor 14-22 Amide, PKA Inhibitor XIII
          DescriptionHeat-stable protein kinase inhibitor (PKI) peptide sequence (14-22) that has been myristoylated at the N-terminus, enhancing its cell-permeability. The non-myristoylated version of this peptide is a highly specific inhibitor (Ki = 36 nM) of cAMP-dependent protein kinase (PKA).
          FormLyophilized
          FormulationSupplied as a trifluoroacetate salt.
          Chemical formulaC₅₃H₁₀₀N₂₀O₁₂
          Peptide SequenceMyr-N-Gly-Arg-Thr-Gly-Arg-Arg-Asn-Ala-Ile-NH₂
          Purity≥95% by HPLC
          SolubilityH₂O (1 mg/ml)
          Storage -20°C
          Hygroscopic
          Do Not Freeze Ok to freeze
          Special InstructionsFollowing reconstitution, aliquot and freeze (-20°C). Stock solutions are stable for up to 3 months at -20°C.
          Toxicity Standard Handling
          ReferencesPaman, K., et al. 1998. J. Lipid Res. 39, 1091.
          Rimon, G., and Rubin M. 1998. Biochim. Biophys. Acta 1380, 289.
          Harris, T.E., et al. 1997. Biochem. Biophys. Res. Commun. 232, 648.
          Muniz, M., et al. 1997. Proc. Natl. Acad. Sci. USA 94, 14461.
          Zoukhri, D., et al. 1997. Am. J. Physiol. 272, C263.
          Eichholtz, T., et al. 1993. J. Biol. Chem. 268, 1982.
          Ward, N.E. and O’Brian, C.A. 1993. Biochemistry 32, 11903.
          Walsh, D.A. and Glass, D.B. 1991. Methods Enzymol. 201, 304.
          Glass, D.B., et al. 1989. J. Biol. Chem. 264, 8802.