LIMK-1/2 (phospho Thr508/505) Polyclonal Antibody

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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. LIMK1 is a serine/threonine kinase that regulates actin polymerization via phosphorylation and inactivation of the actin binding factor cofilin. LIM domain kinase 1 is ubiquitously expressed during development and plays a role in many cellular processes associated with cytoskeletal structure. LIM domain kinase 1 also stimulates axon growth and may play a role in brain development. LIMK1 hemizygosity is implicated in the impaired visuospatial constructive cognition of Williams syndrome. Alternative splicing results in multiple transcript variants encoding distinct isoforms.

Synthesized peptide derived from human LIMK-1/2 around the phosphorylation site of T508/505

The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen

Phospho-LIMK-1/2 (T508/505) Polyclonal Antibody detects endogenous levels of LIMK-1/2 protein only when phosphorylated at T508/505.