D8815
Anti-Destrin/ADF (GV-13) antibody produced in rabbit
affinity isolated antibody, buffered aqueous solution
Sinónimos:
Anti-Actin Depolymerizing Factor
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About This Item
Productos recomendados
origen biológico
rabbit
Nivel de calidad
conjugado
unconjugated
forma del anticuerpo
affinity isolated antibody
tipo de anticuerpo
primary antibodies
clon
polyclonal
Formulario
buffered aqueous solution
reactividad de especies
human, canine, mouse, rat
concentración
~0.5-1.0 mg/mL
técnicas
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
Nº de acceso UniProt
Condiciones de envío
dry ice
temp. de almacenamiento
−20°C
modificación del objetivo postraduccional
unmodified
Información sobre el gen
human ... DSTN(11034)
mouse ... Dstn(56431)
rat ... Dstnl1(296197)
Descripción general
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.
Inmunógeno
synthetic peptide corresponding to amino acids 153-165 of human destrin/ADF.
Aplicación
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.
Acciones bioquímicas o fisiológicas
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.
Forma física
Solution in phosphate buffered saline containing 1% bovine serum albumin and 15 mM sodium azide.
Cláusula de descargo de responsabilidad
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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Encuentre la documentación para los productos que ha comprado recientemente en la Biblioteca de documentos.
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
H Abe et al.
Biochemistry, 29(32), 7420-7425 (1990-08-14)
Two actin-regulatory proteins of 19 and 20 kDa are involved in the regulation of actin assembly in developing chicken skeletal muscle. They are homologous with actin depolymerizing factor (ADF) and cofilin, a pH-dependent actin-modulating protein, which were originally discovered in
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
J R Bamburg
Annual review of cell and developmental biology, 15, 185-230 (1999-12-28)
Ubiquitous among eukaryotes, the ADF/cofilins are essential proteins responsible for the high turnover rates of actin filaments in vivo. In vertebrates, ADF and cofilin are products of different genes. Both bind to F-actin cooperatively and induce a twist in the
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