Anti-phospho-Raptor (Ser863)

In 1X PBS, pH 7.4, with 0.09% sodium azide. Raptor participates in the FRAP1 pathway and associates in a near stoichiometric ratio with FRAP1 to form a nutrient-sensitive complex (NSC). It plays a pivotal role as a scaffold protein in the FRAP1-signaling pathway and this interaction is essential for the catalyzed phosphorylation of EIF4EBP1. It has a positive role in nutrient-stimulated signaling to the downstream effector RPS6KB1. Under nutrient-deprived conditions, raptor serves as a negative regulator of FRAP1 kinase activity. Regulation of the interaction with FRAP1 is a critical mechanism by which cells coordinate the rate of cell growth and maintenance of cell size with different environmental conditions. Protein function: Involved in the control of the mammalian target of rapamycin complex 1 (mTORC1) activity which regulates cell growth and survival, and autophagy in response to nutrient and hormonal signals, functions as a scaffold for recruiting mTORC1 substrates. mTORC1 is activated in response to growth factors or amino acids. Growth factor-stimulated mTORC1 activation involves a AKT1- mediated phosphorylation of TSC1-TSC2, which leads to the activation of the RHEB GTPase that potently activates the protein kinase activity of mTORC1. Amino acid-signaling to mTORC1 requires its relocalization to the lysosomes mediated by the Ragulator complex and the Rag GTPases. Activated mTORC1 up-regulates protein synthesis by phosphorylating key regulators of mRNA translation and ribosome synthesis. mTORC1 phosphorylates EIF4EBP1 and releases it from inhibiting the elongation initiation factor 4E (eiF4E). mTORC1 phosphorylates and activates S6K1 at 'Thr-389', which then promotes protein synthesis by phosphorylating PDCD4 and targeting it for degradation. Involved in ciliogenesis. [The UniProt Consortium]