476485
PKA Inhibitor 14-22 Amide
≥95% (HPLC), PKA Inhibitor, lyophilized
別名:
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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この商品について
実験式（ヒル表記法）:
C53H100N20O12
分子量:
1209.49
UNSPSC Code:
12352200
NACRES:
NA.77
Assay:
≥95% (HPLC)
Form:
lyophilized
Storage condition:
OK to freeze, desiccated (hygroscopic)
製品名
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).
Quality Segment
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 (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
Physical form
Supplied as a trifluoroacetate salt.
Preparation Note
Following reconstitution, aliquot and freeze (-20°C). Stock solutions are stable for up to 3 months at -20°C.
Other Notes
Myr-N-Gly-Arg-Thr-Gly-Arg-Arg-Asn-Ala-Ile-NH₂
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
Disclaimer
Toxicity: Standard Handling (A)
保管分類
11 - Combustible Solids
wgk
WGK 1
flash_point_f
Not applicable
flash_point_c
Not applicable