Key Spec Table
|Species Reactivity||Key Applications||Host||Format||Antibody Type|
|H, M, R||WB, IH(P)||Rb||Purified||Monoclonal Antibody|
|Description||Anti-phospho-LAT (Tyr191) Antibody, rabbit monoclonal|
|Presentation||100 μL of rabbit monoclonal IgG in 60% storage buffer (50mM Tris-Glycine (pH 7.4), 0.15M NaCl, 0.01% sodium azide and 0.05% BSA) and 40% glycerol.|
|Safety Information according to GHS|
|Material Size||100 µL|
|Reference overview||Application||Pub Med ID|
|Beta-catenin inhibits T cell activation by selective interference with linker for activation of T cells-phospholipase C-γ1 phosphorylation.|
Driessens, G; Zheng, Y; Locke, F; Cannon, JL; Gounari, F; Gajewski, TF
Journal of immunology (Baltimore, Md. : 1950) 186 784-90 2011
Despite the defined function of the β-catenin pathway in thymocytes, its functional role in peripheral T cells is poorly understood. We report that in a mouse model, β-catenin protein is constitutively degraded in peripheral T cells. Introduction of stabilized β-catenin into primary T cells inhibited proliferation and cytokine secretion after TCR stimulation and blunted effector cell differentiation. Functional and biochemical studies revealed that β-catenin selectively inhibited linker for activation of T cells phosphorylation on tyrosine 136, which was associated with defective phospholipase C-γ1 phosphorylation and calcium signaling but normal ERK activation. Our findings indicate that β-catenin negatively regulates T cell activation by a previously undescribed mechanism and suggest that conditions under which β-catenin might be inducibly stabilized in vivo would be inhibitory for T cell-based immunity.
|Molecular cloning of the cDNA encoding pp36, a tyrosine-phosphorylated adaptor protein selectively expressed by T cells and natural killer cells|
Weber, J R, et al
J Exp Med, 187:1157-61 (1998) 1998
|LAT: the ZAP-70 tyrosine kinase substrate that links T cell receptor to cellular activation.|
Zhang, W, et al.
Cell, 92: 83-92 (1998) 1998
Despite extensive study, several of the major components involved in T cell receptor-mediated signaling remain unidentified. Here we report the cloning of the cDNA for a highly tyrosine-phosphorylated 36-38 kDa protein, previously characterized by its association with Grb2, phospholipase C-gamma1, and the p85 subunit of phosphoinositide 3-kinase. Deduced amino acid sequence identifies a novel integral membrane protein containing multiple potential tyrosine phosphorylation sites. We show that this protein is phosphorylated by ZAP-70/Syk protein tyrosine kinases leading to recruitment of multiple signaling molecules. Its function is demonstrated by inhibition of T cell activation following overexpression of a mutant form lacking critical tyrosine residues. Therefore, we propose to name the molecule LAT-linker for activation of T cells.