LIMK-2 (phospho Ser283) Rabbit Polyclonal Antibody

There are approximately 40 known eukaryotic LIM proteins, so named for the LIM domains they contain. LIM domains are highly conserved cysteine-rich structures containing 2 zinc fingers. Although zinc fingers usually function by binding to DNA or RNA, the LIM motif probably mediates protein-protein interactions. LIM kinase-1 and LIM kinase-2 belong to a small subfamily with a unique combination of 2 N-terminal LIM motifs and a C-terminal protein kinase domain. The protein encoded by this gene is phosphorylated and activated by ROCK, a downstream effector of Rho, and the encoded protein, in turn, phosphorylates cofilin, inhibiting its actin-depolymerizing activity. It is thought that this pathway contributes to Rho-induced reorganization of the actin cytoskeleton. At least three transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2008], catalytic activity:ATP + a protein = ADP + a phosphoprotein., function:Displays serine/threonine-specific phosphorylation of myelin basic protein and histone (MBP) in vitro., PTM:Phosphorylated on serine and/or threonine residues by ROCK1., similarity:Belongs to the protein kinase superfamily. TKL Ser/Thr protein kinase family., similarity:Contains 1 PDZ (DHR) domain., similarity:Contains 1 protein kinase domain., similarity:Contains 2 LIM zinc-binding domains., subcellular location:Isoform LIMK2a is distributed in the cytoplasm and the nucleus., subcellular location:Isoform LIMK2b occurs mainly in the cytoplasm and is scarcely translocated to the nucleus., subunit:Binds ROCK1 and LKAP. Interacts with PARD3. Interacts with NISCH., tissue specificity:Highest expression in the placenta; moderate level in liver, lung, kidney, and pancreas. LIMK2a is found to be more abundant then LIMK2b in liver, colon, stomach, and spleen, while in brain, kidney, and placenta LIMK2b is the dominant form. In adult lung, both LIMK2a and LIMK2b is nearly equally observed.