|Immunogen||:||A synthetic peptide corresponding to residues in the C-terminus of human ZAP-70 was used as immunogen.|
|Protocol||:||30 min @ RT|
|Control tissue||:||Tonsil Tissue|
ZAP-70(c-term), a Syk-family protein tyrosine kinase, plays a critical role in mediating T cell signal transduction in response to T cell receptor (TCR) activation. TCR-mediated activation of the Src-family kinases, Lck and Fyn, results in tyrosine phosphorylation of the TCR zeta and CD3 chains. These domains serve as targets for binding of ZAP-70(c-term) via its tandem SH2 domains. This binding correlates with activation of ZAP-70(c-term), a critical event in T cell activation. Following TCR engagement, ZAP-70(c-term) is phosphorylated on several tyrosine residues, presumably by two mechanisms: an autophosphorylation and a trans-phosphorylation by the Srcfamily tyrosine kinase, Lck. Phosphorylation of Tyr319 is required for full activation and increased positive downstream regulation by ZAP-70(c-term) .
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