Synthetic phosphopeptide derived from human Rictor around the phosphorylation site of Threonine 1135.
Conjugation:
Unconjugated
Alternative Names:
Rapamycin-insensitive companion of mTOR, AVO3 homolog, hAVO3, RICTOR, KIAA1999
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. mTOR is a large protein kinase with two different complexes. One complex contains mTOR, GbetaL and raptor, which is a target of rapamycin. The other complex, insensitive to rapamycin, includes mTOR, GbetaL, Sin1, and rictor. The mTOR-rictor complex phosphorylates Ser473 of Akt/PKB in vitro. This phosphorylation is essential for full Akt/PKB activation. Furthermore, an siRNA knockdown of rictor inhibits Ser473 phosphorylation in 3T3-L1 adipocytes. This complex has also been shown to phosphorylate the rapamycin-resistant mutants of S6K1, another effector of mTOR. Phosphorylation of Thr1135 on rictor was identified at Cell Signaling Technology (CST) using PhosphoScan, CSTs LC-MS/MS platform for phosphorylation site discovery. 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.
The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).
Form:
Rabbit IgG, 1mg/ml in PBS with 0.02% sodium azide, 50% glycerol, pH7.2
Application Dilute:
WB: 1:500~1:1000 IHC: 1:50~1:200 IF: 1:50~1:200
Application Notes:
Rictor (Phospho-Thr1135) polyclonal antibody detects endogenous levels of Rictor protein only when phosphorylated at Thr1135.
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