The activation of T lymphocytes by antigens is mediated by the T cell receptor (TCR), which is a multisubunit complex assembled from at least six different genes (1,2). The TCR subunits include the Ti a and b chains, the CD3 g , d and e chains and a z -containing homodimer or heterodimer (1,2). The protein tyrosine kinase ZAP-70 binds to the phosphorylated immunoreceptor tyrosine-base activation motifs (ITAMs) of the TCR z chain through two src-homology (SH2) domains (3,4). This binding results in the phosphorylation of ZAP-70 on multiple tyrosine residues, including Tyr292 and Tyr319 (4). ZAP-70 is autophosphorylated on Tyr292, which is thought to negatively regulate ZAP-70 function in lymphocytes (5,6). Alternatively, ZAP-70 is positively regulated by phosphorylation on Tyr319, which mediates the SH2-dependent interaction between Lck and ZAP-70 (5,6).
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIPIFELISA
recommended for detection of Tyr 493 phosphorylated ZAP-70 of mouse, rat and human origin by WB, IP, IF and ELISA
Species Reactivity
HumanMouseRat
Concentration
1mg/ml
Purification
Affinity purified
Target Information
Alternative Names
epitope corresponding to phosphorylated Tyr 493 of ZAP-70 of human origin
Tissue Specificity
epitope corresponding to phosphorylated Tyr 493 of ZAP-70 of human origin