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.
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*For more information, see UniProt Accession P23528
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*All molecular weights (MW) are confirmed by comparison to Bio-Rad Rainbow Markers and to western blot mobilities of known proteins with similar MW.
Product References:Rufanova, V.A. et al. (2009) Cell Health and Cytoskel. 1:17. (WB: Glomerular mesangial cell)
Giacobbe, A. et al. (2016) Oncogene. 35(12):1602-8. (WB: MCF-7)
Amelio, I. et al. (2012) J Cell Biol. 199(2):347. (WB: human primary epidermal keratinocytes)
Couch, B.A. et al. (2010) J Alzheimers Disease. 20:1003. (WB: mouse hippocampus, fasudil)
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