货号 | 3806T |
同种亚型 | Rabbit IgG |
反应种属 | Human,Mouse,Monkey, |
来源宿主 | Rabbit |
应用 | WB |
目标/特异性 | Phospho-Rictor (Thr1135) (D30A3) Rabbit mAb detects endogenous levels of rictor protein only when phosphorylated at Thr1135. |
使用方法 | WB(1:1000) |
供应商 | CST |
灵敏度 | Endogenous |
背景 | Cell growth is a fundamental biological process whereby cells accumulate mass and increase in size. The mammalian TOR (mTOR) pathway regulates growth by coordinating energy and nutrient signals with growth factor-derived signals (1). mTOR is a large protein kinase with two different complexes. One complex contains mTOR, GβL and raptor, which is a target of rapamycin. The other complex, insensitive to rapamycin, includes mTOR, GβL, Sin1, and rictor (1). The mTOR-rictor complex phosphorylates Ser473 of Akt/PKB in vitro (2). This phosphorylation is essential for full Akt/PKB activation. Furthermore, an siRNA knockdown of rictor inhibits Ser473 phosphorylation in 3T3-L1 adipocytes (3). This complex has also been shown to phosphorylate the rapamycin-resistant mutants of S6K1, another effector of mTOR (4).Phosphorylation of Thr1135 on rictor was identified at Cell Signaling Technology (CST) using PhosphoScan®, CSTs LC-MS/MS platform for phosphorylation site discovery (5). Additional research indicates that rictor is phosphorylated at Thr1135 by p70 S6K, which negatively regulates mTORC2 protein complex as part of a negative feedback mechanism controlling Akt activity (6-8). |
存放说明 | -20C |
计算分子量 | 200 |
参考文献 | 1 . Sarbassov, D.D. et al. (2004) Curr. Biol. 14, 1296-1302. 2 . Sarbassov, D.D. et al. (2005) Science 307, 1098-101. 3 . Hresko, R.C. and Mueckler, M. (2005) J. Biol. Chem. 280, 40406-40416. 4 . Ali SM and Sabatini DM (2005) J Biol Chem 280, 19445–8 5 . Dibble, C.C. et al. (2009) Mol Cell Biol 29, 5657-70. 6 . Julien, L.A. et al. (2010) Mol Cell Biol 30, 908-21. 7 . Rush, J. et al. (2005) Nat Biotechnol 23, 94-101. 8 . Treins, C. et al. (2010) Oncogene 29, 1003-16. |