Cell Signaling Technology

Product Pathways - Translational Control

Phospho-mTOR (Ser2448) Antibody #2971

Applications Reactivity MW (kDa) Source
W H M R Mk 289 Rabbit

Applications Key:  W=Western Blotting
Reactivity Key:  H=Human  M=Mouse  R=Rat  Mk=Monkey
Species enclosed in parentheses are predicted to react based on 100% sequence homology. Species cross-reactivity is determined by Western blot.

Specificity / Sensitivity

Phospho-mTOR (Ser2448) Antibody detects endogenous levels of mTOR only when phosphorylated at Ser2448.

Source / Purification

Polyclonal antibodies are produced by immunizing rabbits with a synthetic phospho-peptide (KLH-coupled) corresponding to residues surrounding Ser2448 of human mTOR. Antibodies are purified by protein A and peptide affinity chromatography.

Western Blotting

Western Blotting

Western blot analysis of extracts from 293 cells (starved for 16 hours) untreated or EGF-treated (100 ng/ml), using Phospho-mTOR (Ser2448) Antibody (upper) or control mTOR Antibody #2972 (lower).

Background

The mammalian target of rapamycin (mTOR, FRAP, RAFT) is a Ser/Thr protein kinase (1-3) that functions as an ATP and amino acid sensor to balance nutrient availability and cell growth (4,5). When sufficient nutrients are available, mTOR responds to a phosphatidic acid-mediated signal to transmit a positive signal to p70 S6 kinase and participate in the inactivation of the eIF4E inhibitor, 4E-BP1 (6). These events result in the translation of specific mRNA subpopulations. mTOR is phosphorylated at Ser2448 via the PI3 kinase/Akt signaling pathway and autophosphorylated at Ser2481 (7,8). mTOR plays a key role in cell growth and homeostasis and may be abnormally regulated in tumors. For these reasons, mTOR is currently under investigation as a potential target for anti-cancer therapy (9).

  1. Sabers, C.J. et al. (1995) J. Biol. Chem. 270, 815-822.
  2. Brown, E.J. et al. (1994) Nature 369, 756-758.
  3. Sabatini, D.M. et al. (1994) Cell 78, 35-43.
  4. Gingras, A.C. et al. (2001) Genes Dev. 15, 807-826.
  5. Dennis, P.B. et al. (2001) Science 294, 1102-1105.
  6. Fang, Y. et al. (2001) Science 294, 1942-1945.
  7. Nave, B.T. et al. (1999) Biochem. J. 344 Pt 2, 427-431.
  8. Peterson, R.T. et al. (2000) J. Biol. Chem. 275, 7416-7423.
  9. Huang, S. and Houghton, P.J. (2003) Curr. Opin. Pharmacol. 3, 371-377.

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