Protein Folding and Stability
Smurf1 Antibody
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| CSTコード |
包装 |
希望納入価格 (円) |
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| #2174S | 100 μL | 46,000 | |
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2174 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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2174:
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Western Blotting
| 用途 (希釈倍率) | |
| ウェスタンブロッティング (1:1,000) |
| 特異性・感度 | |
| 内在性レベルのSmurf1 タンパク質を検出します。 |
| 使用抗原 | |
| ヒトのSmurf1タンパク質の中心領域 (合成ペプチド) |
Western Blotting
Western blot analysis of extracts from various cell lines using Smurf1 Antibody.
Bone morphogenetic proteins (BMPs) constitute a large family of signaling molecules that regulate a wide range of critical processes including morphogenesis, cell-fate determination, proliferation, differentiation, and apoptosis (1,2). BMP receptors are members of the TGF-β family of Ser/Thr kinase receptors. Ligand binding induces multimerization, autophosphorylation, and activation of these receptors (3-5). They subsequently phosphorylate Smad1 at Ser463 and Ser465 in the carboxy-terminal motif SSXS, as well as Smad5 and Smad8 at their corresponding sites. These phosphorylated Smads dimerize with the coactivating Smad4 and translocate to the nucleus, where they stimulate transcription of target genes (5).MAP kinases and CDKs 8 and 9 phosphorylate residues in the linker region of Smad1, including Ser206. The phosphorylation of Ser206 recruits Smurf1 to the linker region and leads to the degradation of Smad1 (6). Phosphorylation of this site also promotes Smad1 transcriptional action by recruiting YAP to the linker region (7).
Smurf1, a member of the HECT family of E3 ubiquitin ligases, selectively interacts with BMP pathway Smad effectors, leading to Smad protein ubiquitination and degradation (6). In addition, Smurf1 interacts with the inhibitor Smad, Smad7, the bone-specific transcription factor Runx2/Cbfa1, RhoA and MEKK2 (7-10). Smurf1 negatively regulates osteoblast differentiation and bone formation in vivo (10,11). A related protein, Smurf2, acts more promiscuously, interacting with both BMP and TGF-β pathway Smad proteins (12).
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Hogan, B.L. et al. (1996) Genes Dev. 10, 1580-1594.
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Hoodless, P.A. et al. (1996) Cell 85, 489-500.
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Klemm, J.D. et al. (1998) Annu. Rev. Immunol. 16, 569-592.
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Kretzschmar, M. et al. (1997) Genes Dev. 11, 984-995.
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Whitman, M. (1998) Genes Dev. 12, 2445-2462.
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Sapkota, G. et al. (2007) Mol Cell 25, 441-54.
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Alarcón, C. et al. (2009) Cell 139, 757-69.
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Zhu, H. et al. (1999) Nature 400, 687-693.
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Ebisawa, T. et al. (2001) J. Biol. Chem. 276, 12477-12480.
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Zhao, M. et al. (2003) J. Biol. Chem. 278, 27939-27944.
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Wang, H.R. et al. (2003) Science 302, 1775-1779.
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Yamashita, M. et al. (2005) Cell 121, 101-113.
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Zhao, M. et al. (2004) J. Biol. Chem. 279, 12854-12859.
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Zhang, Y. et al. (2001) Proc. Natl. Acad. Sci. U S A 98, 974-979.
PhosphoSitePlus®：
SMURF1