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Key Documents

D8815

Sigma-Aldrich

Anti-Destrin/ADF (GV-13) antibody produced in rabbit

affinity isolated antibody, buffered aqueous solution

Synonym(s):

Anti-Actin Depolymerizing Factor

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About This Item

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

species reactivity

human, canine, mouse, rat

concentration

~0.5-1.0 mg/mL

technique(s)

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 accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... DSTN(11034)
mouse ... Dstn(56431)
rat ... Dstnl1(296197)

General description

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.

Application

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 Actions

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.

Physical form

Solution in phosphate buffered saline containing 1% bovine serum albumin and 15 mM sodium azide.

Disclaimer

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
Georgios Pampalakis et al.
Molecular oncology, 13(11), 2329-2343 (2019-04-14)
Kallikrein-related peptidase 6 (KLK6) is a serine protease normally expressed in mammary tissue and aberrantly regulated in breast cancer. At physiological levels, KLK6 functions as a suppressor of breast cancer, while its aberrant overexpression (> 50-fold higher than normal) is characteristic
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

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