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PKI (14-22) amide (myristoylated)

PKA inhibitor
 
BML-P210-0500 0.5 mg 95.00 USD
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Heat-stable protein kinase inhibitor (PKI) peptide sequence (14-22). N-terminus is myristoylated to increase cell membrane permeability. The non-myristoylated version of this peptide is a highly specific inhibitor of cAMP-dependent protein kinase (PKA) with Ki=36 nM. This product is a useful tool for studying PKA in cellular systems.

Product Specification

Alternative Name:cAMP-dependent protein kinase inhibitor (14-22) amide (myristoylated)
 
Sequence:N-myristoyl-Gly-Arg-Thr-Gly-Arg-Arg-Asn-Ala-Ile-NH2
 
Formula:C53H100N20O12
 
MW:1209.5
 
Source:Synthetic.
 
CAS:201422-03-9
 
Formulation:Lyophilized. Trifluoroacetate salt.
 
Purity:≥95% (HPLC)
 
Appearance:Solid.
 
Solubility:Soluble to at least 1mg/ml in water.
 
Shipping:Shipped on Blue Ice
 
Long Term Storage:-20°C
 
Handling:Protect from moisture.
 
Technical Info/Product Notes: Replacement for ADI-HPK-108
 

Product Literature References

Crosstalk Between Purinergic Receptors and Canonical Signaling Pathways in the Mouse Salivary Gland: S. Bhattacharya, et al.; Cell Calcium 58, 589 (2015), Abstract;
Lipopolysaccharide induction of REDD1 is mediated by two distinct CREB-dependent mechanisms in macrophages: D.K. Lee, et al.; FEBS Lett. 589, 2859 (2015), Abstract;
Nicotine shifts the temporal activation of hippocampal protein kinase A and extracellular signal-regulated kinase 1/2 to enhance long-term, but not short-term, hippocampus-dependent memory: T. Gould, et al.; Neurobiol. Learn. Mem. 109, 151 (2014), Application(s): EIA using mouse hippocampal tissue, Abstract; Full Text
Regulation of a common, low-affinity binding site for primary prostanoids on bovine aortic endothelial cells: G. Rimon et al.; Biochim. Biophys. Acta. 1380, 289 (1998), Abstract;
Therapy for X-adrenoleukodystrophy: normalization of very long chain fatty acids and inhibition of induction of cytokines by cAMP: K. Pahan et al.; J. Lipid. Res. 39, 1091 (1998), Abstract;
Pseudosubstrate inhibition of cyclic AMP-dependent protein kinase in intact pancreatic islets: effects on cyclic AMP-dependent and glucose-dependent insulin secretion: T. E. Harris et al.; Biochem. Biophys. Res. Commun. 232, 648 (1997), Abstract;
A myristoylated pseudosubstrate peptide, a novel protein kinase C inhibitor: T. Eichholtz et al.; J. Biol. Chem. 268, 1982 (1993), Abstract;
Inhibition of protein kinase C by N-myristoylated peptide substrate analogs: N. E. Ward et al.; Biochemistry 32, 11903 (1993), Abstract;
Utilization of the inhibitor protein of adenosine cyclic monophosphate-dependent protein kinase, and peptides derived from it, as tools to study adenosine cyclic monophosphate-mediated cellular processes: D. A. Walsh et al.; Methods Enzymol. 201, 304 (1991), Abstract;
Primary structural determinants essential for potent inhibition of cAMP-dependent protein kinase by inhibitory peptides corresponding to the active portion of the heat-stable inhibitor protein: D. B. Glass et al.; J. Biol. Chem. 264, 8802 (1989), Abstract;

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