R Recombinant
Recombinant: Superior lot-to-lot consistency, continuous supply, and animal-free manufacturing.
Phospho-Src (Ser17) (D7F2Q) Rabbit mAb #12432
Filter:
- WB
- IP
Supporting Data
| REACTIVITY | H M R Mk |
| SENSITIVITY | Endogenous |
| MW (kDa) | 60 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
- IP-Immunoprecipitation
Species Cross-Reactivity Key:
- H-Human
- M-Mouse
- R-Rat
- Mk-Monkey
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| Immunoprecipitation | 1:50 |
Storage
Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA, 50% glycerol and less than 0.02% sodium azide. Store at –20°C. Do not aliquot the antibody.
Protocol
Specificity / Sensitivity
Phospho-Src (Ser17) (D7F2Q) Rabbit mAb recognizes endogenous levels of Src protein only when phosphorylated at Ser17.
Species Reactivity:
Human, Mouse, Rat, Monkey
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser17 of human Src protein.
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).
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).
- Thomas, S.M. and Brugge, J.S. (1997) Annu Rev Cell Dev Biol 13, 513-609.
- Hunter, T. (1987) Cell 49, 1-4.
- Schmitt, J.M. and Stork, P.J. (2002) Mol Cell 9, 85-94.
- Abrahamsen, H. et al. (2003) J Biol Chem 278, 17170-7.
- Obara, Y. et al. (2004) J Cell Sci 117, 6085-94.
- Hsu, P.P. et al. (2011) Science 332, 1317-22.
限制使用
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For Research Use Only. Not For Use In Diagnostic Procedures.
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