Phospho-p44/42 MAPK (Erk1) (Tyr204)/(Erk2) (Tyr187) (D1H6G) Mouse mAb #5726
- WB
- IF
- F
Supporting Data
| REACTIVITY | H M R Mk |
| SENSITIVITY | Endogenous |
| MW (kDa) | 42, 44 |
| Source/Isotype | Mouse IgG2a |
Application Key:
- WB-Western Blotting
- IF-Immunofluorescence
- F-Flow Cytometry
Species Cross-Reactivity Key:
- H-Human
- M-Mouse
- R-Rat
- Mk-Monkey
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| Immunofluorescence (Immunocytochemistry) | 1:200 |
| Flow Cytometry (Fixed/Permeabilized) | 1:400 - 1:1600 |
Storage
For a carrier free (BSA and azide free) version of this product see product #89967.
Protocol
Specificity / Sensitivity
Species Reactivity:
The antigen sequence used to produce this antibody shares 100% sequence homology with the species listed here, but reactivity has not been tested or confirmed to work by CST. Use of this product with these species is not covered under our Product Performance Guarantee.
Species predicted to react based on 100% sequence homology:
Source / Purification
Background
The "activation loop" of MAPK family members contains two phosphorylation sites, typically a threonine and a tyrosine separated by a single amino acid, designated the T-x-Y motif. Phosphorylation on both residues has been shown to be required for full activation of kinase activity, but it has been appreciated for some time that mono-phosphorylation of the T-x-Y motif occurs, resulting in partial activation of catalytic acitvity and priming for subsequent, dual-phosphorylation (11,12). The crystal structures of non-, mono-, and dual-phospho MAPK/Erk demonstrate that each phospho-isomer assumes an independent conformation (13). In addition, mono-phosphorylation of MAPK/Erk2 at Tyr187 reveals that phosphorylation at this site serves to configure the ATP binding site, while phosphorylation of both Tyr and Thr residues is required to completely stabilize the substrate binding site (14). Furthermore, T-x-Y mutational analysis of members of the Erk and p38 MAP kinases appears to suggest that mono-phosphorylation of the T-x-Y motif confers differential activity and substrate preference (15,16). Taken together, these data suggest an important and underappreciated role for Thr- and Tyr- mono-phosphorylation of the T-x-Y motif among MAP kinases.
- Roux, P.P. and Blenis, J. (2004) Microbiol Mol Biol Rev 68, 320-44.
- Baccarini, M. (2005) FEBS Lett 579, 3271-7.
- Meloche, S. and Pouysségur, J. (2007) Oncogene 26, 3227-39.
- Roberts, P.J. and Der, C.J. (2007) Oncogene 26, 3291-310.
- Rubinfeld, H. and Seger, R. (2005) Mol Biotechnol 31, 151-74.
- Murphy, L.O. and Blenis, J. (2006) Trends Biochem Sci 31, 268-75.
- Dalby, K.N. et al. (1998) J Biol Chem 273, 1496-505.
- Marais, R. et al. (1993) Cell 73, 381-93.
- Kortenjann, M. et al. (1994) Mol Cell Biol 14, 4815-24.
- Owens, D.M. and Keyse, S.M. (2007) Oncogene 26, 3203-13.
- Seger, R. et al. (1991) Proc Natl Acad Sci U S A 88, 6142-6.
- Robbins, D.J. et al. (1993) J Biol Chem 268, 5097-106.
- Kinoshita, T. et al. (2008) Biochem Biophys Res Commun 377, 1123-7.
- Prowse, C.N. et al. (2001) J Biol Chem 276, 40817-23.
- Zhou, B. and Zhang, Z.Y. (2002) J Biol Chem 277, 13889-99.
- Zhang, Y.Y. et al. (2008) J Biol Chem 283, 26591-601.
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