| 名称 | Calmodulin Binding Peptide 1 | 
		 
		| 别名 |  | 
		 
		| 序列(单字母缩写) | GVMPREETDSKTASPWKSARLMVHTVATFNSIKELNERWRSLQQLA | 
		
		
		 
		| 序列(三字母缩写) | {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} | 
		 
		| 基本描述 | 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. | 
		 
		| 分子量 | 5301.010 | 
		 
		| 化学式 | C231H373N69O70S2 | 
		 
		| 纯度 | > 95% | 
		 
		| 存储条件 | Store at -20°C. Keep tightly closed. Store in a cool dry place. | 
		 
		| 注释 |  | 
		
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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. |