D8815
Anti-Destrin/ADF (GV-13) antibody produced in rabbit
affinity isolated antibody, buffered aqueous solution
Synonym(e):
Anti-Actin Depolymerizing Factor
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Alle Fotos(4)
About This Item
Empfohlene Produkte
Biologische Quelle
rabbit
Qualitätsniveau
Konjugat
unconjugated
Antikörperform
affinity isolated antibody
Antikörper-Produkttyp
primary antibodies
Klon
polyclonal
Form
buffered aqueous solution
Speziesreaktivität
human, canine, mouse, rat
Konzentration
~0.5-1.0 mg/mL
Methode(n)
indirect immunofluorescence: 1:100 using mouse NIH/3T3 fibroblasts
western blot: 1:1,500 using whole extracts of human A-431 epidermoid carcinoma cells, rat PC-12 pheochromocytoma cells, and dog MDCK kidney cells
UniProt-Hinterlegungsnummer
Versandbedingung
dry ice
Lagertemp.
−20°C
Posttranslationale Modifikation Target
unmodified
Angaben zum Gen
human ... DSTN(11034)
mouse ... Dstn(56431)
rat ... Dstnl1(296197)
Allgemeine Beschreibung
Destrin/ADF is 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. It is also present in ‘Hirano bodies′ in certain brain neurons of dementia patients.
Immunogen
synthetic peptide corresponding to amino acids 153-165 of human destrin/ADF.
Anwendung
Anti-Destrin/ADF antibody produced in rabbit is suitable for immunoblotting at a working dilution of 1:1500 using whole extracts of human A-431 epidermoid carcinoma, rat PC-12 pheochromocytoma, and dog MDCK kidney cells and for indirect immunofluorescence at a working dilution of 1:100 using mouse NIH/3T3 fibroblasts. It was used in a study to label chick neurons treated with antimycin to examine the colocalization of actin, cofilin, and ADF in pMAP (phosphorylated microtubule-associated protein) inclusions after ATP depletion. It was used to specifically detect ADF in a study.
Biochem./physiol. Wirkung
Destrin/ADF (Actin Depolymerizing Factor) is a small phosphoinositide-sensitive actin-binding protein capable of depolymerizing actin-filaments in vitro. It binds stoichiometrically to monomeric G-actin and to actin protomers in filaments in a pH-dependent, Ca2+ independent manner. It intercalates between longitudinally associated actin monomers within the filament and distorts its helical twist. It 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.
Physikalische Form
Solution in phosphate buffered saline containing 1% bovine serum albumin and 15 mM sodium azide.
Haftungsausschluss
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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Barbara Calabrese et al.
PloS one, 9(4), e94787-e94787 (2014-04-18)
A current model posits that cofilin-dependent actin severing negatively impacts dendritic spine volume. Studies suggested that increased cofilin activity underlies activity-dependent spine shrinkage, and that reduced cofilin activity induces activity-dependent spine growth. We suggest instead that both types of structural
E Nishida et al.
Biochemistry, 24(23), 6624-6630 (1985-11-05)
An Mr 19 000 protein (destrin) that has the ability to rapidly depolymerize F-actin in a stoichiometric manner was purified from porcine kidney by sequential chromatography on DNase I-agarose, hydroxyapatite, and Sephadex G-75. Its actin-depolymerizing activity is reversibly controlled by
Michael Hoa et al.
Frontiers in molecular neuroscience, 13, 13-13 (2020-03-03)
Hearing loss is a problem that impacts a significant proportion of the adult population. Cochlear hair cell (HC) loss due to loud noise, chemotherapy and aging is the major underlying cause. A significant proportion of these individuals are dissatisfied with
K Moriyama et al.
The Journal of biological chemistry, 265(10), 5768-5773 (1990-04-05)
Destrin is a mammalian 19-kDa protein that rapidly depolymerizes F-actin in a stoichiometric manner. In this study, we isolated cDNA clones coding for destrin from a porcine brain cDNA library. The deduced amino acid sequence of destrin is 165 residues
M E Adams et al.
Biochemistry, 29(32), 7414-7420 (1990-08-14)
Chick brain actin depolymerizing factor (ADF) is a 19-kDa protein that severs actin filaments and binds actin monomers. We have obtained a cDNA encoding ADF by screening a chick embryo lambda gt11 cDNA library with both a rabbit anti-ADF antiserum
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