Human LIMK2 (NP_005560.1, 1 a.a. - 638 a.a.) full-length recombinant protein with GST tag expressed in baculovirus infected Sf21 cells.
Theoretical MW (kDa):
Baculovirus infected insect cell (Sf21) expression system
Glutathione sepharose chromatography
90 % by SDS-PAGE/CBB staining
The activity was determined by ELISA. The enzyme was incubated with GST-fused substrate protein, and after stopping kinase reaction by EDTA, the reaction solution was transferred into glutathione- coated plate. Phosphorylation was detected by anti-phospho antibody and HRP-labeled anti-rabbit IgG. Substrate: Cofilin2. ATP: 100 uM.
Quality Control Testing:
Loading 1 ug protein in SDS-PAGE
In 50 mM Tris-HCl, 150 mM NaCl, pH 7.5 (0.1% CHAPS, 1 mM DTT, 10% glycerol)
Store at -80°C. Aliquot to avoid repeated freezing and thawing.
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