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Merck

D3816

Sigma-Aldrich

Anti-Drebrin antibody produced in rabbit

IgG fraction of antiserum, buffered aqueous solution

Sinónimos:

Anti-developmentally-regulated brain protein

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About This Item

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.46

biological source

rabbit

Quality Level

conjugate

unconjugated

antibody form

IgG fraction of antiserum

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

species reactivity

human, rat

technique(s)

western blot: 1:1,000 using rat brain cytosol extract
western blot: 1:1,000 using whole extract of the human epitheloid carcinoma HeLa cell line

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... DBN1(1627)
rat ... Dbn1(81653)

General description

Drebrin is a member of the newly identified ADF-H family of actin-binding proteins that share the structurally conserved actin-depolymerizing factor (ADF) binding module. It is composed of a single ADF-H domain at its N-terminus, followed by a non-conserved central region and a C-terminal SH3 domain. Three isoforms, E1 and E2 (embryonic) and A (adult), have been identified in the brain. An additional truncated form of drebrin A, s-drebrin/A2, is specifically expressed in the adult brain, but not in non-neuronal tissues. Drebrin is also widely expressed in a variety of cells including epithelial, endothelial, and smooth muscle cells and is associated at cell-cell adhering junction sites.

Immunogen

synthetic peptide corresponding to the N-terminal region of human drebrin E/A (amino acids 22-42) conjugated to KLH.

Biochem/physiol Actions

Drebrin (developmentally-regulated brain protein) is a major neuronal F-actin binding protein involved in the control of actin dynamics and neuronal morphogenesis. It colocalizes with actin filaments and dendritic-like cell processes and may be involved in actin remodeling. It binds to and dissociates F-actin stabilizing proteins such as α-actinin, fascin, and tropomyosin from actin filaments. It plays an important role in the formation of axons and dendrites during neuronal development and in neuronal plasticity in the adult brain.

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 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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Storage Class

12 - Non Combustible Liquids

wgk_germany

nwg

flash_point_f

Not applicable

flash_point_c

Not applicable


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T Shirao et al.
Experimental cell research, 215(1), 145-153 (1994-11-01)
Drebrin A is a neuron-specific protein, the expression of which is regulated during development. Upon transfection of fibroblasts with drebrin A cDNA, the protein is expressed at high levels in fibroblasts and the outgrowth of highly branched, neurite-like cell processes
11991718
10th Internatl. Conf. on Organic Synthesis, Bangalore, India, December 1994 null
H Asada et al.
Journal of neuroscience research, 38(2), 149-159 (1994-06-01)
Drebrins are developmentally regulated actin-binding proteins. In this study, we analyzed subcellular distribution of drebrin E in neuroblastoma cells (SH-SY5Y) in culture, especially in terms of its relationship to actin filaments. In undifferentiated cells, drebrin E was scattered as flocculus
R Ishikawa et al.
The Journal of biological chemistry, 269(47), 29928-29933 (1994-11-25)
Drebrin is a development-associated neuroprotein whose cDNA into fibroblasts causes the formation of dendrite-like structures (Shirao, T., Kojima, N., and Obata, K. (1992) Neuroreport 3, 109-112). To explore molecular functions of drebrin during brain development, we purified drebrin from brains
The ADF homology (ADF-H) domain: a highly exploited actin-binding module.
P Lappalainen et al.
Molecular biology of the cell, 9(8), 1951-1959 (1998-08-07)

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