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ZAP-70 is a tyrosine kinase that mediates T cell receptor (TCR) signaling.1 It is composed of two tandem Src homology 2 (SH2) domains, which are critical for TCR-mediated intracellular signal transduction, a linker region containing numerous tyrosine residues subject to phosphorylation, and a kinase domain. ZAP-70 is expressed mainly by T cells and natural killer (NK) cells but is also expressed by certain subsets of malignant B cells.2 Following TCR stimulation, ZAP-70 is recruited from the cytoplasm to phosphorylated TCR ζ chain immunoreceptor tyrosine-based activation motifs (ITAMs), where it is phosphorylated and activated by the tyrosine kinase LCK.1,3 ZAP-70 phosphorylates the adaptor proteins LAT and SLP-76, which activate a variety of intracellular signaling pathways that lead to T cell activation, proliferation, and differentiation.1,3 ZAP70 loss-of-function mutations are associated with ZAP-70 deficiency, a SCID characterized by the absence of functional T cells and recurrent infections.1,4 Cayman's ZAP-70 (N-Term) Rabbit Monoclonal Antibody (RM408) can be used for immunohistochemistry (IHC) and Western blot (WB) applications.
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4. Clinical, immunological, and genetic features in 49 patients with ZAP-