Anti-SIN1

0.5 mg/ml with 0.1 mg/ml BSA (US sourced), 0.05% sodium azide. mTOR, or Mammalian target of rapamycin, a large protein kinase, is a regulator of cell growth and survival via its mTORC1 (mTOR + GBL + Raptor) and mTORC2 (mTOR + GBL + SIN1 + Rictor) complexes. SIN1 is an essential component of mTORC2, which activates Akt by phosphorylating Ser473. Phosphorylation of SIN1 at Thr86/398 causes its dissociation from the mTORC2 complex, inhibiting mTORC2s kinase activity. Protein function: Subunit of mTORC2, which regulates cell growth and survival in response to hormonal signals. mTORC2 is activated by growth factors, but, in contrast to mTORC1, seems to be nutrient- insensitive. mTORC2 seems to function upstream of Rho GTPases to regulate the actin cytoskeleton, probably by activating one or more Rho-type guanine nucleotide exchange factors. mTORC2 promotes the serum-induced formation of stress-fibers or F-actin. mTORC2 plays a critical role in AKT1 'Ser-473' phosphorylation, which may facilitate the phosphorylation of the activation loop of AKT1 on 'Thr-308' by PDK1 which is a prerequisite for full activation. mTORC2 regulates the phosphorylation of SGK1 at 'Ser-422'. mTORC2 also modulates the phosphorylation of PRKCA on 'Ser-657'. Within mTORC2, MAPKAP1 is required for complex formation and mTORC2 kinase activity. MAPKAP1 inhibits MAP3K2 by preventing its dimerization and autophosphorylation. Inhibits HRAS and KRAS signaling. Enhances osmotic stress-induced phosphorylation of ATF2 and ATF2-mediated transcription. Involved in ciliogenesis, regulates cilia length through its interaction with CCDC28B independently of mTORC2 complex. [The UniProt Consortium]