Destrin

GWB-4676D0

Synthetic peptide conjugated to KLH corresponding to amino acids 153-165 of Destrin with N-terminal added lysine.

Destrin

The antibody is affinity-purified using the immunizing peptide immobilized on agarose. Storage

IF: Use at a dilution of 1/100. WB: Use at a dilution of 1/1500. Detects a band of approximately 19 kDa. Not tested in other applications. Optimal dilutions/concentrations should be determined by the end user. Destrin/ADF (Actin Depolymerizing Factor) is a small phosphoinositide-sensitive actin-binding protein capable of depolymerizing actin-filaments in vitro. Under certain conditions it fragments the filaments and accelerates actin subunits dissociation from their ë pointedí (minus) ends. Destrin/ADF binds stoichiometrically to monomeric G-actin and to actin protomers in filaments in an apparently pH-dependent Ca2+- independent manner. Actin-ADP is preferentially bound. Destrin/ADF intercalates between longitudinally associated actin monomers within the filament and distorts its helical twist. The sequence of destrin/ADF is highly homologous to that of cofilin a related gelsolin-like actin filament-severing protein also belonging to the actin-depolymerizing factor/cofilin (AC) family. Destrin/ADF and cofilin are widely distributed in tissues of eukaryotes and both contain a nuclear localization sequence. Destrin/ADF is found in various epithelial and endothelial cells but is practically absent from adult mouse heart and skeletal muscle cells. Destrin/ADF and cofilin are usually found in regions containing dynamic actin pools such as the leading edge of migrating cells and neuronal growth cones and may also colocalize in cell nuclei. Both are present in ë Hirano bodiesí in certain brain neurons of dementia patients. Destrin/ADF 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 and cytokinesis. In vivo activity of vertebrate destrin/ADF is regulated through reversible phosphorylation and dephosphorylation at serine-3 (Ser3). Dephosphorylation of destrin/ADF at this site was described in rat parotis response to ?-adrenergic or cholinergic stimulation and also in dog thyroid cells following treatment with thyrotropin or phorbol ester. The phosphorylated form is inactive and incapable of association with actin. Regulation of destrin/ADF in vertebrates is carried out by the Lim kinases 1 and 2.

Widely distributed in various tissues.

Contains 1 ADF-H domain.