Vesicle Trafficking
GM130 Antibody
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イイネ！(2)
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| CSTコード |
包装 |
希望納入価格 (円) |
国内在庫  |
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| #2296S | 100 μL | 46,000 | |
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2296 の推奨プロトコール
最適な結果を得るために：Cell Signaling Technology (CST) 社は、各製品の推奨プロトコールを使用することを強くお薦めいたします。
推奨プロトコールはCST社内試験の徹底的なバリデーションに基づいて作成されておりますので、正確かつ再現性の高い結果が得られます。
注：各製品に最適化されたプロトコールをリンクしています。
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2296:
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Immunoprecipitation
Western Blotting
| 用途 (希釈倍率) | |
| ウェスタンブロッティング (1:1,000)、免疫沈降 (1:25) |
| 特異性・感度 | |
| 内在性レベルのGM130 タンパク質を検出します。 |
| 使用抗原 | |
| ヒトのGM130 タンパク質のN末端の配列 (合成ペプチド) |
| ※括弧付きの動物種は、配列が100%相同であるため反応すると推定されます。 |
Western Blotting
Western blot analysis of extracts from HeLa, ZR-75 and MCF-7 cells, using GM130 Antibody.
The Golgi apparatus functions in the modification, organization and transport of proteins and membranes targeted to other parts of the cell, such as the plasma membrane, lysosomes and endosomes. This regulated transport is important for appropriate protein localization, secretion and signal transduction. Members of the Golgin family of proteins, including GM130, Giantin, p115 and GRASP65, are defined by their presence in the Golgi matrix and by their long coiled coil domains. Golgin function, which is regulated in part by small GTPases of the Rab and Arl families, includes establishing and maintaining Golgi structure as well as transport (reviewed in 1). The Golgi cisternae are stacked and linked laterally to form a ribbon. GRASP65 and GM130 are required for membrane fusion events that mediate ribbon formation during Golgi assembly. These lateral fusion events allow for uniform distribution of Golgi enzymes (2). GM130 and Giantin interact with the transport factor p115 to facilitate endoplasmic reticulum (ER)-Golgi transport (3). GM130 is also involved in the transport of the Ether-a-go-go-Related (hERG) potassium ion channel, whose inappropriate localization may be an underlying cause in long Q-T syndrome, a hereditary and potentially fatal cardiac arrhythmia (4). Further, GM130 was implicated in signal transduction regulating invasion, migration and cell polarization via its interaction with and activation of serine/threonine kinases YSK1 and MST4 (5).
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Barr, F.A. and Short, B. (2003) Curr. Opin. Cell Biol. 15, 405-413.
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Puthenveedu, M.A. et al. (2006) Nat. Cell Biol. 8, 238-248.
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Alvarez, C. et al. (2001) J. Biol. Chem. 276, 2693-2700.
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Roti, E.C. et al. (2002) J. Biol. Chem. 277, 47779-47785.
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Preisinger, C. et al. (2004) J. Cell Biol. 164, 1009-1020.
PhosphoSitePlus®：
GM130