LIMK2 Blocking Peptide – >85% Purity

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]

LIMK2: a TKL kinase of the LISK family that regulates actin dynamics. Contains two N-terminal LIM motifs. Phosphorylated and activated by PAK1 and ROCK, downstream effectors of Rho. Phosphorylates cofilin, inhibiting its actin-depolymerizing activity. May contributes to Rho-induced reorganization of the actin cytoskeleton. Two alternative splice variants have been identified.

Protein type: EC 2.7.11.1; Protein kinase, Ser/Thr (non-receptor); Protein kinase, TKL; Kinase, protein; TKL group; LISK family; LIMK subfamily

Chromosomal Location of Human Ortholog: 22q12.2

Cellular Component: cis-Golgi network; cytoplasm; nucleus

Molecular Function: protein serine/threonine kinase activity; protein binding; zinc ion binding; protein heterodimerization activity; ATP binding

Biological Process: spermatogenesis; protein amino acid phosphorylation; phosphorylation