476485
PKA Inhibitor 14-22 Amide, Cell-Permeable, Myristoylated
PKA Inhibitor 14-22 Amide is myristoylated at the N-terminus that enhances its cell-permeability. The non-myristoylated version is shown to be a specific inhibitor of PKA (Ki = 36 nM).
Synonyme(s) :
PKA Inhibitor 14-22 Amide, Cell-Permeable, Myristoylated, PKI 14-22 Amide, Cell-Permeable, Myristoylated Protein Kinase A Inhibitor Amide 14-22, Cell-Permeable, Myr-GRTGRRNAI-NH₂, Protein Kinase A Inhibitor 14-22 Amide, PKA Inhibitor XIII
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About This Item
Formule empirique (notation de Hill):
C53H100N20O12
Poids moléculaire :
1209.49
Code UNSPSC :
12352200
Nomenclature NACRES :
NA.77
Produits recommandés
Niveau de qualité
Pureté
≥95% (HPLC)
Forme
lyophilized
Fabricant/nom de marque
Calbiochem®
Conditions de stockage
OK to freeze
desiccated (hygroscopic)
Solubilité
water: 1 mg/mL
Conditions d'expédition
ambient
Température de stockage
−20°C
Description générale
Heat-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.
Heat-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).
Actions biochimiques/physiologiques
Cell permeable: yes
Primary Target
cAMP-dependent protein kinase
cAMP-dependent protein kinase
Product does not compete with ATP.
Reversible: no
Target Ki: 36 nMf or cAMP-dependent protein kinase
Avertissement
Toxicity: Standard Handling (A)
Séquence
Myr-N-Gly-Arg-Thr-Gly-Arg-Arg-Asn-Ala-Ile-NH₂
Forme physique
Supplied as a trifluoroacetate salt.
Reconstitution
Following reconstitution, aliquot and freeze (-20°C). Stock solutions are stable for up to 3 months at -20°C.
Autres remarques
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. Biochemistry32, 11903.
Walsh, D.A. and Glass, D.B. 1991. Methods Enzymol. 201, 304.
Glass, D.B., et al. 1989. J. Biol. Chem.264, 8802.
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. Biochemistry32, 11903.
Walsh, D.A. and Glass, D.B. 1991. Methods Enzymol. 201, 304.
Glass, D.B., et al. 1989. J. Biol. Chem.264, 8802.
Informations légales
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
Code de la classe de stockage
11 - Combustible Solids
Classe de danger pour l'eau (WGK)
WGK 1
Point d'éclair (°F)
Not applicable
Point d'éclair (°C)
Not applicable
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