|Tested species reactivity||Dog, Human, Mouse, Non-human primate, Rabbit, Rat|
|Host / Isotype||Mouse / IgG|
|Immunogen||Synthetic peptide corresponding to residues G(1114) N L P E S R I E G W L S(1126) of human ROCK-1.|
|Storage buffer||PBS with 0.05% BSA|
|Contains||0.05% sodium azide|
|Storage Conditions||Store at 4°C short term. For long term storage, store at -20°C, avoiding freeze/thaw cycles.|
|Tested Applications||Dilution *|
|Western Blot (WB)||1-2 µg/ml|
* Suggested working dilutions are given as a guide only. It is recommended that the user titrate the product for use in their own experiment using appropriate negative and positive controls.
Suggested positive control: Jurkat cells treated with camptothecin or anti-Fas antibody to induce apoptosis..
The Rho target protein, Rho-associated coiled coil-containing protein kinase (ROCK)-1 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. ROCK-1 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, ROCK-I 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 ROCK I induces phosphorylation of MLC and membrane blebbing, one of the first events in the execution phase of apoptosis.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.