Application Note
*Optimal dilutions/concentrations should be determined by the researcher.
| Application |
Recommended Dilution |
| 1:1500 |
| 1:100 |
| Assay dependent |
Not tested in other applications.
Calculated MW
Positive Control
A431, PC-12, MDCK, NIH3T3
Form
Liquid
Buffer
PBS, 1% BSA
Preservative
15mM Sodium azide
Storage
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.
Concentration
~0.5-1.0 mg/ml (Please refer to the vial label for the specific concentration.)
Antigen Species
Human
Immunogen
synthetic peptide corresponding to amino acids 153-165 of human destriDF.
Purification
Purified by affinity chromatography
Conjugation
Unconjugated
RRID
AB_381235
Note
For laboratory research use only. Not for any clinical, therapeutic, or diagnostic use in humans or animals. Not for animal or human consumption.
Purchasers shall not, and agree not to enable third parties to, analyze, copy, reverse engineer or otherwise attempt to determine the structure or sequence of the product.
Synonyms
destrin, actin depolymerizing factor , ACTDP , ADF , HEL32 , bA462D18.2
Background
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 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 colocalize 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 ?-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.
Database
Research Area
