D8815
Anti-Destrin/ADF (GV-13) antibody produced in rabbit
affinity isolated antibody, buffered aqueous solution
Synonim(y):
Anti-Actin Depolymerizing Factor
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About This Item
Polecane produkty
pochodzenie biologiczne
rabbit
Poziom jakości
białko sprzężone
unconjugated
forma przeciwciała
affinity isolated antibody
rodzaj przeciwciała
primary antibodies
klon
polyclonal
Postać
buffered aqueous solution
reaktywność gatunkowa
human, canine, mouse, rat
stężenie
~0.5-1.0 mg/mL
metody
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
numer dostępu UniProt
Warunki transportu
dry ice
temp. przechowywania
−20°C
docelowa modyfikacja potranslacyjna
unmodified
informacje o genach
human ... DSTN(11034)
mouse ... Dstn(56431)
rat ... Dstnl1(296197)
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Opis ogólny
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.
Zastosowanie
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.
Działania biochem./fizjol.
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.
Postać fizyczna
Solution in phosphate buffered saline containing 1% bovine serum albumin and 15 mM sodium azide.
Oświadczenie o zrzeczeniu się odpowiedzialności
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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Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.
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
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
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
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
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
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