Anti-phospho-Cofilin (pSer³) antibody produced in rabbit

Cofilin is a small phosphoinositide-sensitive actin-binding protein capable of depolymerizing actin-filaments in vitro. It has gelsolin-like actin filament-severing protein similar to destrin/ADF (Actin Depolymerizing Factor). Cofilin has has a short β-strand at the C terminus. In mammals it has two isoforms: non-muscle (NM-CF, CF-L1) and muscle (M-CF, CF-L2). The protein is ubiquitiously present in tissues of eukaryotes and is especially abundant in neuronal tissues. It can shuttle between the cytoplasm and the nucleus in response to various stresses or signals, and may translocate from the cytoplasm to the plasma membrane in various cells.

synthetic phosphopeptide corresponding to amino acids 2-9 (pSer³) of human cofilin with a C-terminal added cysteine, conjugated to KLH. This sequence is identical in mouse, rat, and pig.

Anti-phospho-Cofilin antibody was used:

• as primary antibody for immunoblottingto to study the role of the Rac1 GTPase.
• for western blot analysis in a comparative study of signals induced by integrin ligation during cell attachment, mechanical force from intracellular contraction, or cell stretching by external force.
• as primary antibody for western blotting in a study to detect the level of cofilin.

Cofilin binds stoichiometrically to monomeric G-actin and actin protomers in filaments in an apparently pH-dependent, Ca²⁺ independent manner. Cofilin intercalates between longitudinally associated actin monomers within the filament and distorts its helical twist.It cleaves the filaments and accelerates actin subunits dissociation from their ‘pointed′ ends under specific conditions. Cofilin is essential for viability and is important for many cellular processes involving actin remodeling such as motility at the leading edge of cells, polarized cell growth, endocytosis, phagocytosis, cellular activation, cytokinesis, and pathogen intracellular motility. It′s activity is regulated through reversible phosphorylation and dephosphorylation. In phosphorylated form, it behaves inactive and unable to bond with actin. Phosphorylation of cofilin is regulated in vertebrates by at least four protein kinases: LIM Kinase 1, LIM Kinase 2, Testicular Kinase 1, and Testicular Kinase 2. The dephosphorylation of cofilin enables its actin severing and depolymerizing activity and drives directional cell motility, thus providing a simple phosphoregulatory mechanism for actin reorganization.

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

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