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Merck

SAB4200372

Sigma-Aldrich

Anti-WASH1 antibody produced in rabbit

~1.0 mg/mL, affinity isolated antibody

別名:

Anti-FAM39E, Anti-WAS protein family homolog 1, Anti-WASH

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About This Item

UNSPSCコード:
12352203
NACRES:
NA.41

由来生物

rabbit

品質水準

結合体

unconjugated

抗体製品の状態

affinity isolated antibody

抗体製品タイプ

primary antibodies

クローン

polyclonal

フォーム

buffered aqueous solution

分子量

antigen ~72 kDa

化学種の反応性

human, rat, mouse

濃度

~1.0 mg/mL

テクニック

immunoprecipitation (IP): 5-10 μg using lysates of rat NRK cells.
western blot: 2-4 μg/mL using whole extracts of HEK-293T cells over-expressing mouse WASH1.

輸送温度

dry ice

保管温度

−20°C

ターゲットの翻訳後修飾

unmodified

遺伝子情報

詳細

WASH1 (Wiskott-Aldrich Syndrome Protein and SCAR Homolog) is a new member of the WASP family. Similar to other WASP family members, it contains a C-terminal for ′WH2, connecting and acidic′ (WCA) domain that binds to Actin related protein 2/actin related protein 3 (Arp2/3). In addition, WASH1 also contains a short proline-rich region, a unique N-terminal domain termed WASH-homology domain (WAHD1), and a tubulin-binding region.

免疫原

synthetic peptide corresponding to an internal region of human WASH1, conjugated to KLH. The corresponding sequence differs by one amino acid in mouse and rat.

アプリケーション

Anti-WASH1 antibody produced in rabbit has been used in western blotting and immunoprecipitation.

生物化学的/生理学的作用

WASH1 (Wiskott-Aldrich Syndrome Protein and SCAR Homolog), is a nucleation-promoting factor at the surface of endosomes. It recruits and activates the Arp2/3 complex to induce actin polymerization, playing a key role in the fission of endosomes. WASH1 forms part of a multiprotein complex composed of FAM21, KIAA1033 strumpellin and WASH-interacting protein (SWIP) and coiled coil domain containing 53 (CCDC53). It associates with tubulin and localizes to early and recycling endosomes, where together with the Arp2/3 complex and actin, it is required for maintaining the shape of the endosomal compartment and the regulation of the retrograde transport.

物理的形状

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

免責事項

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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保管分類コード

10 - Combustible liquids

引火点(°F)

Not applicable

引火点(℃)

Not applicable


適用法令

試験研究用途を考慮した関連法令を主に挙げております。化学物質以外については、一部の情報のみ提供しています。 製品を安全かつ合法的に使用することは、使用者の義務です。最新情報により修正される場合があります。WEBの反映には時間を要することがあるため、適宜SDSをご参照ください。

Jan Code

SAB4200372-200UL:
SAB4200372-BULK:
SAB4200372-VAR:
IXO14136:


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Lot/Batch Number

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以前この製品を購入いただいたことがある場合

文書ライブラリで、最近購入した製品の文書を検索できます。

文書ライブラリにアクセスする

Missense variant in CCDC22 causes X-linked recessive intellectual disability with features of Ritscher-Schinzel/3C syndrome
Kolanczyk M, et al.
European Journal of Human Genetics, 23(5), 633-633 (2015)
DNAJC13 p. Asn855Ser, implicated in familial parkinsonism, alters membrane dynamics of sorting nexin 1
Follett J, et al.
Neuroscience Letters, 706(5), 114-122 (2019)
Mateusz Kolanczyk et al.
European journal of human genetics : EJHG, 23(5), 633-638 (2014-06-12)
Ritscher-Schinzel syndrome (RSS)/3C (cranio-cerebro-cardiac) syndrome (OMIM#220210) is a rare and clinically heterogeneous developmental disorder characterized by intellectual disability, cerebellar brain malformations, congenital heart defects, and craniofacial abnormalities. A recent study of a Canadian cohort identified homozygous sequence variants in the
WASH and the Arp2/3 complex regulate endosome shape and trafficking
Duleh SN and Welch MaD
Cytoskeleton (Hoboken, N.J.), 67(3), 193-206 (2010)
A FAM21-containing WASH complex regulates retromer-dependent sorting
Gomez TS and Billadeau DD
Developmental Cell, 17(5), 699-711 (2009)

ライフサイエンス、有機合成、材料科学、クロマトグラフィー、分析など、あらゆる分野の研究に経験のあるメンバーがおります。.

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