Phospho-Rictor (Thr1135) (D30A3) Rabbit Antibody

INQUIRY

CAT. NO.: AMA-0001

Target Information
UniProt ID	Q6R327

Product Details
Size	20 μL/100 μL/300 μL
Reactivity	Human, Monkey, Mouse
Host	Rabbit
Source/Isotype	Rabbit IgG
Storage	Store at -20°C.
Purification	Monoclonal antibody is produced by immunizing animals with a synthetic phosphopeptide corresponding to the sequence surrounding Thr1135 of human Rictor protein.

Usage
Application	WB
Product Usage Information Dilution	Western Blotting (1:1000)
MW (Target)	200 kDa

Background
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, GβL and raptor, which is a target of rapamycin. The other complex, insensitive to rapamycin, includes mTOR, GβL, 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.

Background

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, GβL and raptor, which is a target of rapamycin. The other complex, insensitive to rapamycin, includes mTOR, GβL, 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.

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