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).
Synonyma:
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
Přihlásitk zobrazení cen stanovených pro organizaci a smluvních cen
About This Item
Empirický vzorec (Hillův zápis):
C53H100N20O12
Molekulová hmotnost:
1209.49
UNSPSC Code:
12352200
NACRES:
NA.77
Doporučené produkty
Quality Level
assay
≥95% (HPLC)
form
lyophilized
manufacturer/tradename
Calbiochem®
storage condition
OK to freeze
desiccated (hygroscopic)
solubility
water: 1 mg/mL
shipped in
ambient
storage temp.
−20°C
General description
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).
Biochem/physiol Actions
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
Warning
Toxicity: Standard Handling (A)
Sequence
Myr-N-Gly-Arg-Thr-Gly-Arg-Arg-Asn-Ala-Ile-NH₂
Physical form
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.
Other Notes
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.
Legal Information
CALBIOCHEM is a registered trademark of Merck KGaA, Darmstadt, Germany
Storage Class
11 - Combustible Solids
wgk_germany
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable
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