Phospho-GADS (Thr262) (E8L3B) Rabbit mAb #78972
- WB
Supporting Data
| REACTIVITY | H |
| SENSITIVITY | Endogenous |
| MW (kDa) | 40 |
| Source/Isotype | Rabbit IgG |
Application Key:
- WB-Western Blotting
Species Cross-Reactivity Key:
- H-Human
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
| Simple Western™ | 1:50 - 1:250 |
Storage
Protocol
Specificity / Sensitivity
Phospho-GADS (Thr262) (E8L3B) Rabbit mAb recognizes endogenous levels of GADS protein only when phosphorylated at Thr262.
Species Reactivity:
Human
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Thr262 of human GADS protein.
Background
GRB2-related adaptor downstream of Shc (GADS) belongs to the GRB2 family of adaptor proteins. It is a hematopoietic cell-specific signaling adaptor protein that harbors amino- and carboxy-terminal SH3 domains, a central SH2 domain, and a unique linker region that is rich in proline and glutamine residues (1). The presence of SH2 and SH3 domains within GADS strongly suggest that it functions in signal transduction cascades by facilitating protein-protein interactions. In the context of T cells, research studies have demonstrated that GADS interacts with LAT and SLP-76 signaling complexes to facilitate NFAT activation downstream of TCR engagement (2-4). Given its role as a fundamental mediator of TCR signaling, GADS is subject to multiple modes of negative regulation to limit TCR signal strength. For example, research studies have demonstrated that HPK1 directly phosphorylates GADS at Thr262 within its linker region, a modification that promotes 14-3-3 binding and dissociation of signaling complexes nucleated by LAT, SLP-76, and GADS (5). The linker region of GADS is also subject to caspase-mediated cleavage, which separates its SH2 and SH3 domains and thus impairs the ability of GADS to bridge LAT and SLP-76 signaling complexes for transduction of faithful TCR signals (6,7).
- Hámori, J. et al. (1978) Neuroscience 3, 403-12.
- Liu, S.K. et al. (1999) Curr Biol 9, 67-75.
- Law, C.L. et al. (1999) J Exp Med 189, 1243-53.
- Asada, H. et al. (1999) J Exp Med 189, 1383-90.
- Lasserre, R. et al. (2011) J Cell Biol 195, 839-53.
- Berry, D.M. et al. (2001) Oncogene 20, 1203-11.
- Yankee, T.M. et al. (2001) Proc Natl Acad Sci USA 98, 6789-93.
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