Overview |
bs-70539r-100ul |
LIMK1 (C-terminus) Antibody |
WB |
The antibody detects a 72 kDa* protein corresponding to the molecular mass of LIMK1 on SDS-PAGE immunoblots of mouse recombinant LIMK1. This sequence is conserved in rat and mouse LIMK1, and is not found in LIMK2. |
Human, Mouse, Rat |
Specifications |
Unconjugated |
Rabbit |
LIMK1 (C-terminus) synthetic peptide (coupled to carrier protein) corresponding to amino acids at the C-terminus of human LIMK1. |
Polyclonal |
IgG |
Antigen Affinity purification |
PBS + 1 mg/ml BSA, 0.05% NaN3 and 50% glycerol |
Storage at -20°C is recommended, as aliquots may be taken without freeze/thawing due to presence of 50% glycerol. Stable for at least 1 year at -20°C. |
Target |
P53667 |
LIMK |
LIM kinases (LIMK1 and LIMK2) are serine/threonine kinases that have two zinc finger motifs, known as LIM motifs, in their amino-terminal regulatory domains. LIM kinases are involved in actin cytoskeletal regulation downstream of Rho-family GTPases, PAKs, and ROCK. PAK1 and ROCK phosphorylate LIMK1 or LIMK2 at the conserved Thr-508 or Thr-505 residues in the activation loop, increasing LIMK activity. In addition, VEGF-induced stress fiber formation has been linked to p38-mediated activation of LIMK through MK-2 phosphorylation of Ser-323. Activated LIM kinases inhibit the actin depolymerization activity of cofilin by phosphorylation at the amino-terminal Ser-3 residue of cofilin. In addition, LIMKs may have a function in the nucleus. It has been shown that the nuclear localization of LIMKs can mediate suppression of Rac/Cdc42-mediated cyclin D1 expression. This effect of LIMKs was independent of cofilin phosphorylation and the regulation of actin dynamics. |
Application Dilution |
WB |
1:300-5000 |