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GNLPESRIEGWLS, corresponding to C terminal amino acids 1114-1126 of Human ROCK1.
The Rho target protein, Rho-associated coiled coil-containing protein kinase (ROCK1) has been found to be a new Caspase 3 substrate. ROCK, one of the effectors of the small GTPase Rho, has recently been shown to contribute significantly to myosin light chain (MLC) activation through two pathways: direct phosphorylation of MLC and phosphorylation of MLC phosphatase, leading to its inhibition. The increase in cellular contractility that is necessary for apoptotic membrane blebbing implies sustained augmentation of MLC phosphorylation. ROCK1 consists of an amino-terminal kinase domain and an inhibitory cysteine/histidine-rich C-terminal domain that is located within a pleckstrin-homology region. They are joined by a variable region that contains the Rho-binding domain. During apoptosis, ROCK1 is cleaved by Caspase 3 at a conserved DETD1113/G sequence and its carboxy-terminal inhibitory domain is removed, resulting in deregulated and constitutive kinase activity. The Caspase 3-mediated cleavage and activation of ROCK1 induces phosphorylation of MLC and membrane blebbing, one of the first events in the execution phase of apoptosis.
Our Abpromise guarantee covers the use of ab13660 in the following tested applications.
|WB||Use a concentration of 1 - 2 µg/ml. Detects a band of approximately 31 kDa (predicted molecular weight: 160 kDa).|
ab13660 has not yet been referenced specifically in any publications.