Western blot using LIMK1 polyclonal antibody (Cat # PAB10258) shows detection of a 73 KDa band corresponding to LIMK1 in lysates from mouse brain. Approximately 18 ug of lysate wasrun on a SDS-PAGE and transferred onto nitrocellulose followed by reaction with a 1:500 dilution of LIMK1 polyclonal antibody. The doublet band at ~ 75 KDa may represent phosphorylated and non-phosphorylated forms of the protein. The identity of the strong lower molecular weight band at approximately 20 KDa is unknown. Signal was detected using standard techniques.
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 likely to be a component of an intracellular signaling pathway and may be involved in brain development. LIMK1 hemizygosity is implicated in the impaired visuospatial constructive cognition of Williams syndrome. [provided by RefSeq
LIM motif-containing protein kinase,OTTHUMP00000025066