深圳欣博盛生物科技有限公司

Destrin antibody

destrin, actin depolymerizing factor , ACTDP , ADF , HEL32 , bA462D18.2

Human, Mouse, Rat

Rabbit

WB

IgG

synthetic peptide corresponding to amino acids 137-150 of human destriDF.

Polyclonal

Purified by affinity chromatography

Unconjugated

~0.8-1.2 mg/ml (Please refer to the vial label for the specific concentration.)

Store as concentrated solution. Centrifuge briefly prior to opening vial. For short-term storage (1-2 weeks), store at 4ºC. For long-term storage, aliquot and store at -20ºC or below. Avoid multiple freeze-thaw cycles.

4°C

19

Liquid

PBS, 1% BSA, 15mM Sodium azide.

GeneTex

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.