Cofilin 1 (Ser-3), phospho-specific polyclonal, anti-human, mouse, rat, chicken

Background:
Members of the ADF/cofilin (AC) family are actin-severing proteins that regulate actin remodeling during cellular events such as cell migration, cytokinesis, phagocytosis, endocytosis, axon development, and immune cell activation. In mammals, there are three members of the AC family, muscle-specific cofilin (Cofilin 2), non-muscle cofilin (Cofilin 1), and ADF. In humans, cofilin 1 and ADF have 72% identity, with the major amino acid differences found in the C-terminal region. Regulation of cofilin activity can occur through serine phosphorylation. Activation of cofilin kinases, LIMK1 or LIMK2, leads to phosphorylation of cofilin at serine 3. This phosphorylation disrupts cofilin binding to actin in vitro and in vivo. Multiple phosphatases, PP1, PP2A, PP2B, slingshot, and chronophin can dephosphorylate Ser-3 and activate actin binding. Thus, Ser-3 phosphorylation is a major site for the regulation of cofilin activity

Immunogen: A synthetic phospho-peptide (coupled to KLH) corresponding to amino acid residues surrounding serine 3 in human Cofilin 1. This sequence has 100% homology with similar regions of rat and mouse Cofilin 1, and has two amino acid differences from human Cofilin 2.

Specificity: This antibody was cross-adsorbed to unphosphorylated Coflin 1 peptide then affinity purified using phospho-Cofilin 1 (Ser-3) peptide (without carrier). The antibody detects a 19 kDa* protein corresponding to the molecular mass of phosphorylated Cofilin 1 on SDS-PAGE immunoblots of Jurkat cells. This band can be removed by lambda phosphatase treatment.

Buffer/Storage:
Rabbit polyclonal, affinity-purified antibody is supplied in 100µl phosphate-buffered saline, 50% glycerol, 1 mg/ml BSA, and 0.05% sodium azide. Store at –20°C. Stable for 1 year.