Phospho-Threonine/Tyrosine Antibody #9381
- WB
- IP
Supporting Data
| REACTIVITY | All |
| SENSITIVITY | Endogenous |
| MW (kDa) | |
| SOURCE | Rabbit |
Application Key:
- WB-Western Blotting
- IP-Immunoprecipitation
Species Cross-Reactivity Key:
- All-All Species Expected
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| Immunoprecipitation | 1:50 |
| Peptide ELISA (DELFIA) | 1:2000 |
Storage
Protocol
Specificity / Sensitivity
Species Reactivity:
Source / Purification
Background
General protein modification antibodies are designed to react with modified amino acid residues (e.g. phospho-threonine, phospho-tyrosine, acetyl-lysine, nitro-tyrosine) independently of the sequence in which they are embedded. This ability to recognize modified residues in a "context-independent" fashion gives these antibodies broad reactivities, presumably conferring upon them the ability to react with hundreds of distinct proteins. This broad pattern of reactivity makes these antibodies especially valuable in multiplex analyses and target discovery programs.
Protein kinases are among the most abundant eukaryotic regulatory proteins; over 500 separate kinase genes are encoded in mammalian genomes (5,6). In spite of the importance of kinases in eukaryotic biology, relatively few of their physiological targets are known. Phospho-Threonine Antibody (P-Thr-Polyclonal) #9381 and Phospho-Threonine (42H4) mAb #9386 provide powerful tools for discovering targets of serine/threonine kinases, for monitoring and characterizing in vitro threonine phosphorylation reactions as well as for high throughput Ser/Thr kinase drug discovery.
- Yaffe, M.B. and Elia, A.E. (2001) Curr Opin Cell Biol 13, 131-8.
- Appella, E. and Anderson, C.W. (2001) Eur J Biochem 268, 2764-72.
- Jenuwein, T. and Allis, C.D. (2001) Science 293, 1074-80.
- Krishna, R.G. and Wold, F. (1993) Adv Enzymol Relat Areas Mol Biol 67, 265-98.
- Venter, J.C. et al. (2001) Science 291, 1304-51.
- Manning, G. et al. (2002) Science 298, 1912-34.
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