ROCK-I is a Rho-associated serine/threonine kinase isozyme that mediates RhoA-induced assembly of focal adhesions and actin stress fibers. It contains an N-terminal kinase domain, a central 600 amino acid long coiled-coil region, a C-terminal pleckstrin homology region (PH) and a Cys-rich zinc finger motif. The ROCK-I kinase domain is approximately 90% identical to that of ROCK-II. ROCK-I binds GTP-bound Rho through a Rho-binding domain (RBD). As a result, the kinase activity of ROCK-I is moderately stimulated. The ROCK isozymes regulate cell contractility through phosphorylation of the myosin light chain. This effect results from either the inhibition of the myosin phosphatase or by direct phosphorylation of the myosin light chain, thus bypassing the myosin light chain kinase. In addition, ROCK-I activates the ubiquitously expressed Na-H exchanger (NHE1) via a number of mechanisms including RhoA. NHE1 may mediate ROCK-I-induced changes in the actin cytoskeleton. Therefore, ROCK-I plays an important role in the regulation of focal adhesion and stress fiber formation.
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1.Since applications vary, each investigator should titrate the reagent to obtain optimal results.
2.Caution: Sodium azide yields highly toxic hydrazoic acid under acidic conditions. Dilute azide compounds in running water before discarding to avoid accumulation of potentially explosive deposits in plumbing.
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