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D1569

Sigma-Aldrich

Anti-Dab-1 (C-terminal) from rabbit

enhanced validation

~1 mg/mL, affinity isolated antibody, buffered aqueous solution

Synonym(s):

Anti-Dab1, Anti-Disabled homolog 1, Anti-Yotari

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.43

biological source

rabbit

Quality Level

200

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen ~80 kDa

species reactivity

mouse, human, rat

enhanced validation

recombinant expression
Learn more about Antibody Enhanced Validation

concentration

~1 mg/mL

technique(s)

western blot: 2-4 μg/mL using HEK-293T cells expressing human DAB1
western blot: 2-4 μg/mL using mouse and rat brain extracts (S1 fraction)

UniProt accession no.

O75553

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... DAB1(1600)
mouse ... Dab1(13131)
rat ... Dab1(266729)

Related Categories

General description

Disabled-1 is an intracellular adaptor protein that belongs to the Reelin signaling pathway. The amino terminus of Dab1 contains a phosphotyrosine-binding (PTB) domain. The domain interacts with NPXY sequences within the cytoplasmic regions of several membrane-bound proteins including lipoprotein receptors and amyloid precursor protein (APP) family.

Application

Anti-Dab-1 (C-terminal) was used at a working dilution of 1:2000 to probe the protein sample extracted from brain tissue of mice by western blotting in a study.

Biochem/physiol Actions

Dab1 plays a key role during brain development by controlling neuronal positioning as well as modulation of long-term potentiation (LTP) in the adult brain. Tyrosine phosphorylation of Dab1 is triggered by the binding of reelin to the lipoprotein receptors Apolipoprotein E receptor 2 (ApoER2) and the very low density lipoprotein receptor (VLDLR), thus initiating a signaling cascade that includes the Src-family kinases and Akt.

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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Danielle E Whittaker et al.
The Journal of clinical investigation, 127(3), 874-887 (2017-02-07)
The mechanisms underlying the neurodevelopmental deficits associated with CHARGE syndrome, which include cerebellar hypoplasia, developmental delay, coordination problems, and autistic features, have not been identified. CHARGE syndrome has been associated with mutations in the gene encoding the ATP-dependent chromatin remodeler
B W Howell et al.
The EMBO journal, 16(1), 121-132 (1997-01-02)
Here, we identify a mouse homolog of the Drosophila Disabled (Dab) protein, mDab1, and show it is an adaptor molecule functioning in neural development. We find that mDab1 is expressed in certain neuronal and hematopoietic cell lines, and is localized
B W Howell et al.
Current biology : CB, 10(15), 877-885 (2000-08-26)
The extracellular protein Reln controls neuronal migrations in parts of the cortex, hippocampus and cerebellum. In vivo, absence of Reln correlates with up-regulation of the docking protein Dab1 and decreased Dab1 tyrosine phosphorylation. Loss of the Reln receptor proteins, apolipoprotein
T Hiesberger et al.
Neuron, 24(2), 481-489 (1999-11-26)
The large extracellular matrix protein Reelin is produced by Cajal-Retzius neurons in specific regions of the developing brain, where it controls neuronal migration and positioning. Genetic evidence suggests that interpretation of the Reelin signal by migrating neurons involves two neuronal
Giampiero Palladino et al.
Journal of molecular neuroscience : MN, 61(3), 359-367 (2016-11-21)
Recent evidence highlights the protective role of reelin against amyloid β (Aβ)-induced synaptic dysfunction and cognitive impairment in Alzheimer disease (AD). In this study, exploiting TgCRND8 mice that overexpress a mutant form of amyloid β precursor protein (AβPP) and display
View All Related Papers

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