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D9945

Sigma-Aldrich

Anti-DOCK1 (C-terminal) antibody produced in rabbit

~1.5 mg/mL, affinity isolated antibody, buffered aqueous solution

Synonym(s):

Anti-DOCK180, Anti-Dedicator of cytokinesis 1, Anti-Downstream of CRK-binding protein, 180-KD

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About This Item

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

mol wt

antigen ~180 kDa

species reactivity

mouse, rat, human

concentration

~1.5 mg/mL

technique(s)

indirect immunofluorescence: 10-20 μg/mL using NIH-3T3 cells
western blot: 2-4 μg/mL using HeLa or PC12 cell lysates

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... DOCK1(1793)
mouse ... Dock1(330662)
rat ... Dock1(309081)

General description

Dedicator of cytokinesis protein 1 (DOCK1), also termed as the DOCK180 gene, is mapped to human chromosome 10q26.2. DOCK1 is a member of a family of guanine nucleotide exchange factors (GEF).

Specificity

Anti-DOCK1 (C-terminal) specifically recognizes human, rat, and mouse DOCK1.

Application

Anti-DOCK1 (C-terminal) antibody produced in rabbit may be used in immunoblotting and immunofluorescence.

Biochem/physiol Actions

Dedicator of cytokinesis protein 1 (DOCK1) is involved in cytoskeletal reorganization and cell migration and acts as an activator of Rac. DOCK1 has been found to undergo ubiquitination and proteasome-dependent degradation, a process enhanced in response to epidermal growth factor (EGF), adapter molecule (Crk) and adhesion-dependent signals. DOCK1 forms a complex with engulfment and cell motility protein 1 (ELMO1) which also inhibits ubiquitylation of DOCK1. By activating the β1 and αvβ5 integrins, DOCK1 regulates cell motility, filopodia formation, and phagocytosis. DOCK1 has been suggested to play a central role in netrin signaling during neuronal development by mediating the attractive responses by neurons to netrin-1. It mediates morphological changes such as integrin-mediated cell spreading and nerve growth factor (NGF)-induced neurite outgrowth. In mammalian cells, the CrkII-ELMO1-DOCK1 complex has been shown to promote phagocytosis.

Physical form

Solution in 0.01 M phos­phate buffered saline, pH 7.4, containing 15 mM sodium azide.

Storage and Stability

Store at –20 °C. For continuous use, the product may be stored at 2–8 °C for up to one month. For extended storage, freeze in working aliquots at –20 °C. Repeated freezing and thawing, or storage in “frost-free” freezers, is not recommended. If slight turbidity occurs upon prolonged storage, clarify the solution by centrifugation before use. Working dilutions should be discarded if not used within 12 hours.

Disclaimer

Unless otherwise stated in our catalog, 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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Certificates of Analysis (COA)

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Rapid aneuploidy diagnosis of partial trisomy 7q (7q34? qter) and partial monosomy 10q (10q26. 12? qter) by array comparative genomic hybridization using uncultured amniocytes
Chen CP, et al.
Taiwanese Journal of Obstetrics & Gynecology, 51(1), 93-99 (2012)
Etsuko Kiyokawa et al.
Cell adhesion & migration, 3(3), 281-284 (2009-05-22)
DOCK180 is an atypical guanine nucleotide exchange factor of Rac1 identified originally as one of the two major proteins bound to the SH3 domain of the Crk adaptor protein. DOCK180 induces tyrosine phosphorylation of p130(Cas), and recruits the Crk-p130(Cas) complex
Yoshinori Makino et al.
Journal of cell science, 119(Pt 5), 923-932 (2006-02-24)
Dock180, a member of the CDM family of proteins, plays roles in biological processes such as phagocytosis and motility through its association with the signalling adaptor protein Crk. Recently, the complex formation between Dock180 and Elmo1 was reported to function

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