Destrin antibody

GeneTex

Destrin antibody

9

WB: 1:600. *Optimal dilutions/concentrations should be determined by the researcher.Not tested in other applications.

Western Blot

Research Use Only

Polyclonal

~0.8-1.2 mg/ml

Unconjugated

DSTN

destrin, actin depolymerizing factor

ACTDP; actin-depolymerizing factor; ADF; bA462D18.2; bA462D18.2 (destrin (actin depolymerizing factor ADF) (ACTDP)); destrin; epididymis luminal protein 32; epididymis secretory sperm binding protein; HEL32

Rabbit

IgG

Destrin

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 the dissociation of actin subunits from their epointedi (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 co-localize in cell nuclei. Both are present in eHirano bodiesi 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 beta-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.

-20°C or -80°C,2°C to 8°C

12352203