Cell Signaling Technology

Product Pathways - Tyrosine Kinase / Adaptors

Phospho-Src (Ser17) (D7F2Q) Rabbit mAb #12432

Applications Reactivity Sensitivity MW (kDa) Isotype
W IP H M R Mk Endogenous 60 Rabbit IgG

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

Protocols

Specificity / Sensitivity

Phospho-Src (Ser17) (D7F2Q) Rabbit mAb recognizes endogenous levels of Src protein only when phosphorylated at Ser17.

Source / Purification

Monoclonal antibody is produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser17 of human Src protein.

Western Blotting

Western Blotting

Western blot analysis of extracts from 293T cells, untreated (-) or treated (+) with λ phosphatase and calf intestinal phosphatase (CIP), using Phospho-Src (Ser17) (D7F2Q) Rabbit mAb (upper) or Src (32G6) Rabbit mAb #2123 (lower).

IP

IP

Immunoprecipitation of phospho-Src (Ser17) from 293T cell extracts using Rabbit (DA1E) mAb IgG XP® Isotype Control #3900 (lane 2) or Phospho-Src (Ser17) (D7F2Q) Rabbit mAb (lane 3). Lane 1 is 10% input. Western blot analysis was performed using Phospho-Src (Ser17) (D7F2Q) Rabbit mAb. A light-chain specific antibody was used as a secondary antibody.

Background

The Src family of protein tyrosine kinases, which includes Src, Lyn, Fyn, Yes, Lck, Blk, and Hck, are important in the regulation of growth and differentiation of eukaryotic cells (1). Src activity is regulated by tyrosine phosphorylation at two sites, but with opposing effects. While phosphorylation at Tyr416 in the activation loop of the kinase domain upregulates enzyme activity, phosphorylation at Tyr527 in the carboxy-terminal tail by Csk renders the enzyme less active (2).

Protein kinase A (PKA)-dependent phosphorylation of Src at Ser17 is thought to influence multiple signaling networks (3-5). This site has also been identified in a phospho-proteomic screen for substrates of mTOR (6).

  1. Thomas, S.M. and Brugge, J.S. (1997) Annu. Rev. Cell Dev. Biol. 13, 513-609.
  2. Hunter, T. (1987) Cell 49, 1-4.
  3. Schmitt, J.M. and Stork, P.J. (2002) Mol Cell 9, 85-94.
  4. Abrahamsen, H. et al. (2003) J Biol Chem 278, 17170-7.
  5. Obara, Y. et al. (2004) J Cell Sci 117, 6085-94.
  6. Hsu, P.P. et al. (2011) Science 332, 1317-22.

Application References

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Companion Products

For Research Use Only. Not For Use In Diagnostic Procedures.

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