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LYS-LYS-ARG-ALA-ALA-ARG-ALA-THR-SER-NH2

LYS-LYS-ARG-ALA-ALA-ARG-ALA-THR-SER-NH2结构式
LYS-LYS-ARG-ALA-ALA-ARG-ALA-THR-SER-NH2结构式
品牌特惠专场
常用名 LYS-LYS-ARG-ALA-ALA-ARG-ALA-THR-SER-NH2 英文名 LYS-LYS-ARG-ALA-ALA-ARG-ALA-THR-SER-NH2
CAS号 119386-39-9 分子量 987.16100
密度 N/A 沸点 N/A
分子式 C40H78N18O11 熔点 N/A
MSDS 中文版 美版 闪点 N/A

Minimum requirements for inhibition of smooth-muscle myosin light-chain kinase by synthetic peptides.

Biochem. J. 257 , 73, (1989)

Although the amino acid residues that are important for peptide substrates of myosin light-chain kinase have been reported, those that are important for peptide inhibitors of this enzyme have not previously been investigated. Synthetic peptides based on the s...

Smooth muscle myosin kinase requires residues on the COOH-terminal side of the phosphorylation site. Peptide inhibitors.

J. Biol. Chem. 261 , 25, (1986)

The COOH-terminal residue in peptide analogs of the phosphorylation site sequence in smooth muscle myosin light chains, Lys11-Lys12-Arg13-Ala-Ala-Arg16-Ala-Thr-Ser19 -(P)Asn20-Val21-Phe22-Ala23, were shown to have a strong influence on the kinetics of peptide...

Rabbit skeletal muscle myosin light chain kinase. The calmodulin binding domain as a potential active site-directed inhibitory domain.

J. Biol. Chem. 262 , 11958-11963, (1987)

A synthetic peptide modeled after the calmodulin (CaM)-binding domain of rabbit skeletal muscle myosin light chain kinase, Lys-Arg-Arg-Trp-Lys5-Lys-Asn-Phe-Ile-Ala10-Val-Ser-Ala-Ala-+ ++Asn15-Arg-Phe-Glycyl amide (M5), inhibited the CaM-independent chymotrypt...