Anti-Cofilin

0.5mg/ml if reconstituted with 0.2ml sterile DI water. Cofilin is a ubiquitous actin-binding factor required for the reorganization of actin filaments. The protein is known to sever actin filaments by creating more positive ends on filament fragments, it can cause depolymerization at the minus end of filaments, thereby preventing their reassembly. As a long-lasting in vivo effect, Cofilin recycles older ADP-F-actin, helping cell to maintain ATP-G-actin pool for sustained motility. pH, phosphorylation and phosphoinositides regulate cofilins binding and associating activity with actin. Protein function: Binds to F-actin and exhibits pH-sensitive F-actin depolymerizing activity. Regulates actin cytoskeleton dynamics. Important for normal progress through mitosis and normal cytokinesis. Plays a role in the regulation of cell morphology and cytoskeletal organization. Required for the up-regulation of atypical chemokine receptor ACKR2 from endosomal compartment to cell membrane, increasing its efficiency in chemokine uptake and degradation. [The UniProt Consortium]