| Name
|
Calmodulin Binding Peptide 1
|
| Sequence (Single letter abbreviations)
|
GVMPREETDSKTASPWKSARLMVHTVATFNSIKELNERWRSLQQLA
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| Sequence（Three letter abbreviations）
|
{GLY}{VAL}{MET}{PRO}{ARG}{GLU}{GLU}{THR}{ASP}{SER}{LYS}{THR}{ALA}{SER}{PRO}{TRP}{LYS}{SER}{ALA}{ARG}{LEU}{MET}{VAL}{HIS}{THR}{VAL}{ALA}{THR}{PHE}{ASN}{SER}{ILE}{LYS}{GLU}{LEU}{ASN}{GLU}{ARG}{TRP}{ARG}{SER}{LEU}{GLN}{GLN}{LEU}{ALA}
|
| Basic description
|
Removing endogenously bound CaM by titration with a affinity (pM) CaM-binding peptide derived from smooth muscle myosin light-chain kinase (MLCK peptide) strongly inhibited IP3-induced Ca2+ release. This inhibition was concentration- and time-dependent.
|
| The molecular weight
|
5301.010
|
| Chemical formula
|
C231H373N69O70S2
|
| The purity
|
> 95%
|
| Storage conditions
|
Store at -20°C. Keep tightly closed. Store in a cool dry place.
|
| Annotation
|
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| Documents
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| Figures
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| Reference
|
GonzÁlez-Andrade M., et al. Importance of the interaction protein-protein of the CaM-PDE1A and CaM-MLCK complexes in the development of new antiâ€CaM drugs. J Mol Recognit. 2013 Apr;26(4):165-74.
N. Dephoure., et al. Hyperplexing: a method for er-order multiplexed quantitative proteomics provides a map of the dynamic response to rapamycin in yeast. Sci Signal. 2012 Mar;5(217):2.
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Calmodulin Binding Peptide 1
