Phospho-Raptor (Ser792) Antibody

• 产品编号：CST-2083P      品牌：Cell Signaling Technology       原厂货号：2083P
• 产品分类：抗体 > 一抗 > 磷酸化抗体
• 应用分类：

描述：

Phospho-Raptor (Ser792) Antibody能够检测内源性的Ser792位点磷酸化的raptor蛋白。这个抗体也可能检测到不同分子量的非特异性信号。该多克隆抗体是由合成的人源的针对raptor蛋白Ser792位点磷酸化肽段免疫动物而生产的。

mTOR的调控关联蛋白（Raptor）被认为是mTOR的结合伴侣并能够调节其信号通路下游靶点（1,2）。Raptor通过4E-BP1和p70 S6激酶等mTOR的底物的TOR信号基序与它们结合，为mTOR介导的这些底物的磷酸化所必需（3,4）。FKBP12-rapamycin复合物和mTOR结合可以抑制mTOR与raptor的相互作用，可能是rapamycin抑制mTOR信号的作用机制（5）。mTOR与raptor的相互作用及营养物质和/或rapamycin对它的调控依赖于GβL蛋白（6）。GβL也是mTOR和rictor（mTOR的rapamycin不敏感的组分）之间的rapamycin不敏感复合物的一部分，并可能调节rictor-mTOR信号通路下游像PKCα这些靶点（7）。此外，rictor-mTOR复合物被认为是以前不明了的PDK2，负责Akt / PKB Ser473位点磷酸化，促进PDK1调节的Akt / PKB Thr308位点磷酸化，最终充分激活Akt / PKB（8）。最近raptor被证实是AMP活化的蛋白激酶（AMPK）的直接底物（9）。AMPK磷酸化raptord的Ser722/792（9）。这种磷酸化对于抑制含raptor的mTOR复合物1（mTORC1）的活性并在细胞能量匮乏时诱导细胞周期阻滞是必不可少的（9）。这些结果表明，raptor是调控细胞周期进程和能量状态一个关键节点。

1. Hara, K. et al. (2002) Cell 110, 177-189.
2. Kim, D. et al. (2002) Cell 110, 163-175.
3. Beugnet, A. et al. (2003) J. Biol. Chem. 278, 40717-40722.
4. Nojima, H. et al. (2003) J. Biol. Chem. 278, 15461-15464.
5. Oshiro, N. et al. (2004) Genes Cells 9, 359-366.
6. Kim, D. H. et al. (2003) Mol. Cell 11, 895-904.
7. Sarbassov, D. et al. (2004) Curr. Biol. 14, 1296-1302.
8. Sarbassov, D.D. et al. (2005) Science 307, 1098-1101.
9. Gwinn, D.M. et al. (2008) Mol Cell 30, 214-26.

原厂资料：

Specificity / Sensitivity

Phospho-Raptor (Ser792) Antibody detects endogenous levels of raptor protein only when phosphorylated at Ser792. The antibody may also detect non-specific signals of various molecular weights.

Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to the sequence surrounding Ser792 of human raptor. Antibodies are purified by peptide affinity chromatography.

Background

The regulatory associated protein of mTOR (Raptor) was identified as an mTOR binding partner that mediates mTOR signaling to downstream targets (1,2). Raptor binds to mTOR substrates, including 4E-BP1 and p70 S6 kinase, through their TOR signaling (TOS) motifs and is required for mTOR-mediated phosphorylation of these substrates (3,4). Binding of the FKBP12-rapamycin complex to mTOR inhibits the mTOR-raptor interaction, suggesting a mechanism for rapamycin's specific inhibition of mTOR signaling (5). This mTOR-raptor interaction and its regulation by nutrients and/or rapamycin is dependent on a protein called GβL (6). GβL is also part of the rapamycin-insensitive complex between mTOR and rictor (rapamycin-insensitive companion of mTOR), and may mediate rictor-mTOR signaling to downstream targets including PKCα (7). Furthermore, the rictor-mTOR complex has been identified as the previously elusive PDK2 responsible for the phosphorylation of Akt/PKB on Ser473, facilitating phosphorylation of Akt/PKB on Thr308 by PDK1 and required for the full activation of Akt/PKB (8). 
 
 Recently raptor has been identified as a direct substrate of the AMP-activated protein kinase (AMPK) (9). AMPK phosphorylates raptor on Ser722/Ser792 (9). This phosphorylation is essential for inhibition of the raptor-containing mTOR complex 1 (mTORC1) and induces cell cycle arrest when cells are stressed for energy (9). These findings suggest that raptor is a critical switch that correlates cell cycle progression with energy status.

1. Hara, K. et al. (2002) Cell 110, 177-189.
2. Kim, D. et al. (2002) Cell 110, 163-175.
3. Beugnet, A. et al. (2003) J. Biol. Chem. 278, 40717-40722.
4. Nojima, H. et al. (2003) J. Biol. Chem. 278, 15461-15464.
5. Oshiro, N. et al. (2004) Genes Cells 9, 359-366.
6. Kim, D. H. et al. (2003) Mol. Cell 11, 895-904.
7. Sarbassov, D. et al. (2004) Curr. Biol. 14, 1296-1302.
8. Sarbassov, D.D. et al. (2005) Science 307, 1098-1101.
9. Gwinn, D.M. et al. (2008) Mol Cell 30, 214-26.

注意事项：

For Research Use Only. Not For Use In Diagnostic Procedures.

Storage: Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM
NaCl, 100 µg/ml BSA and 50% glycerol. Store at –20°C.
Do not aliquot the antibody