ZAP-70

GWB-5293E6

A synthetic peptide corresponding to residues in C-terminus of human ZAP-70 was used as immunogen.

WB: 1:500IHC: 1:100-250ICC: 1:100-250FC: 1:80IP: 1:50. Zap-70 a Syk-family protein tyrosine kinase plays a critical role in mediating T cell signal transduction in response to T cell receptor (TCR) activation (1). 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 via its tandem SH2 domains. This binding correlates with activation of ZAP-70 a critical event in T cell activation (2). Following TCR engagement ZAP-70 is phosphorylated on several tyrosine residues presumably by two mechanisms: an autophosphorylation and a trans-phosphorylation by the Src-family tyrosine kinase Lck. Phosphorylation of Tyr319 is required for full activation and increased positive downstream regulation by ZAP-70 (3). 1. Chu D. H. et al. The Syk family of protein tyrosine kinases in T-cell activation and development. Immunol. Rev. 165: 1672. Isakov N. et al. ZAP-70 binding specificity to T cell receptor tyrosine-based activation motifs: the tandem SH2 domains of ZAP-70 bind distinct tyrosine-based activation motifs with varying affinity. J Exp Med. 181: 3753. Di Bartolo V. et al. Tyrosine 319 a newly identified phosphorylation site of ZAP-70 plays a critical role in T cell antigen receptor signaling. J Biol Chem. 274: 62854. Manufactured under U. S. Patents No. 5 675 063 and 7 429 487