ROCK (Rho-associated, coiled-coil containing protein kinase) has two isoforms, ROCK1 and ROCK2 that share 65% sequence similarity. ROCK has three domains that include the N-terminal catalytic domain (CAT), a middle coiled-coil domain that mediates homodimerization, and Rho-binding (RB) and pleckstrin homology (PH) domains (RB/PH domain) at the C-terminus. The RB/PH domain acts as an autoinhibitory domain and suppresses the kinase activity of CAT.
Synonyms: Anti-ρ Kinase 2 antibody produced in rabbit; Anti-ρ-Associated protein kinase 2 antibody produced in rabbit; Anti-ρ-Associated, coiled-coil-containing protein kinase 2 antibody produced in rabbit; Anti-p164 ROCK-2 antibody produced in rabbit
MDL Number: MFCD07370479
Storage: -20C
Application: Anti-ROCK2 antibody produced in rabbit, a Prestige Antibody, is developed and validated by the Human Protein Atlas (HPA) project (www.proteinatlas.org). Each antibody is tested by immunohistochemistry against hundreds of normal and disease tissues. These images can be viewed on the Human Protein Atlas (HPA) site by clicking on the Image Gallery link. The antibodies are also tested using immunofluorescence and western blotting. To view these protocols and other useful information about Prestige Antibodies and the HPA, visit sigma.com/prestige.
Biochem Physiol Actions: ROCK2 (Rho-associated, coiled-coil containing protein kinase 2) gene encodes a serine/threonine kinase that serves as an effector for the small GTPase RhoA. ROCK2 is localized to the nucleus and is capable of associating with and phosphorylating p300, thereby increasing the acetyltransferase activity of p300. ROCK functions in several cellular activities, such as regulation of actin cytoskeleton and cell polarity, cell adhesion, cytokinesis, and gene expression. It inhibits keratinocyte terminal differentiation. In ROCK2, the RB/PH domain is cleaved by granzyme B to generate an active form that is involved in the generation of cytoplasmic apoptotic bleb. It interacts with nucleophosmin/B23 and initiates centrosome duplication.
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