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Submit ReviewcGMP Dependent Kinase Inhibitor Peptide is a competitive inhibitor of cGMP-dependent protein kinase (PKG); analog of a substrate peptide corresponding to a phosphorylation site of histone H2B. Competes with synthetic substrates (Ki = 86 mM) but does not inhibit phosphorylation of intact histones by PKG. Inhibits phosphorylation of intact histones by PKA.
M. Wt | 943.12 |
Formula | C38H74N18O10 |
Sequence | RKRARKE |
Storage | Desiccate at -20°C |
CAS Number | 82801-73-8 |
PubChem ID | 134097 |
InChI Key | OUKSKNTVYYVIMZ-DUJSLOSMSA-N |
Smiles | [H]N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](C)C(=O)N[C@@H](CCCNC(N)=N)C(=O)N[C@@H](CCCCN)C(=O)N[C@@H](CCC(O)=O)C(O)=O |
The technical data provided above is for guidance only. For batch specific data refer to the Certificate of Analysis.
Tocris products are intended for laboratory research use only, unless stated otherwise.
References are publications that support the biological activity of the product.
Bhatnagar et al (1988) Synthetic peptide analogues differentially alter the binding affinities of cyclic nucleotide dependent protein kinases for nucleotide substrates. Biochemistry 27 1988 PMID: 2837278
Glass (1983) Differential responses of cyclic GMP-dependent and cyclic AMP-dependent protein kinases to synthetic peptide inhibitors. Biochem.J. 213 159 PMID: 6615418
Glass et al (1986) Differential and common recognition of the catalytic sites of the cGMP-dependent and cAMP-dependent protein kinases by inhibitory peptides derived from the heat-stable inhibitor protein. J.Biol.Chem. 261 12166 PMID: 3017964
Keywords: cGMP dependent kinase inhibitor peptide, cGMP dependent kinase inhibitor peptide supplier, inhibitors, inhibits, protein, kinases, A, G, PKA, PKG, [Ala32]H2B(29-35), Protein, Kinase, 1883, Tocris Bioscience
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We examined the regulatory mechanism of the PKG holoenzymes. The development of cGMP-independent peptide activators of PKG I alpha, derived from this helical segment was found bridging the regulatory and catalytic domains.