Apoptosis and Autophagy
Phospho-Bim (Ser69) (D7E11) Rabbit mAb
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| CSTコード |
包装 |
希望納入価格 (円) |
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| #4585S | 100 μL | 57,000 | |
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Bim抗体製品一覧
4585 の推奨プロトコール
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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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4585:
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Immunoprecipitation
Western Blotting
| 用途(希釈倍率) | |
| ウエスタンブロッティング(1:1,000)、免疫沈降(1:50) |
| 特異性・感度 | |
| 内在性レベルのSer69 がリン酸化されたBim タンパク質を検出します。 |
| 使用抗原 | |
| ヒトのBim タンパク質のSer69 周辺領域(合成リン酸化ペプチド) |
| ※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 Raji cells, untreated or TPA-treated for 30 min, using Phospho-Bim (Ser69) (D7E11) Rabbit mAb (upper) or total Bim (C34C5) Rabbit mAb #2933 (lower).
Bim/Bod is a pro-apoptotic protein belonging to the BH3-only group of Bcl-2 family members including Bad, Bid, Bik, Hrk and Noxa that contain a BH3 domain but lack other conserved BH1 or BH2 domains (1,2). Bim induces apoptosis by binding to and antagonizing anti-apoptotic members of the Bcl-2 family. Interactions have been observed with Bcl-2, Bcl-xL, Mcl-1, Bcl-w, Bfl-1 and BHRF-1 (1,2). Bim functions in regulating apoptosis associated with thymocyte negative selection and following growth factor withdrawal, during which Bim expression is elevated (3-6). Three major isoforms of Bim are generated by alternative splicing: BimEL, BimL and BimS (1). The shortest form, BimS, is the most cytotoxic and is generally only transiently expressed during apoptosis. The BimEL and BimL isoforms may be sequestered to the dynein motor complex through an interaction with the dynein light chain and released from this complex during apoptosis (7). Apoptotic activity of these longer isoforms may be regulated by phosphorylation (8,9). Environmental stress triggers Bim phosphorylation by JNK and results in its dissociation from the dynein complex and increased apoptotic activity.
ERK 1/2-dependent phosphorylation of BimEL at Ser69 (Ser65 in mouse and rat) in response to growth factor stimulation can promote its proteasome-mediated degradation and enhance cell survival (6,10,11).
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Hsu, S.Y. et al. (1998) Mol Endocrinol 12, 1432-40.
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Bouillet, P. et al. (2002) Nature 415, 922-6.
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Whitfield, J. et al. (2001) Neuron 29, 629-43.
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Dijkers, P.F. et al. (2000) Curr Biol 10, 1201-4.
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Ley, R. et al. (2003) J Biol Chem 278, 18811-6.
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Puthalakath, H. et al. (1999) Mol Cell 3, 287-96.
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Lei, K. and Davis, R.J. (2003) Proc Natl Acad Sci U S A 100, 2432-7.
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Putcha, G.V. et al. (2003) Neuron 38, 899-914.
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Luciano, F. et al. (2003) Oncogene 22, 6785-93.
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Marani, M. et al. (2004) Oncogene 23, 2431-41.