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When compared with SAP, the other single SH2 domain protein in human, EAT2 shows similar binding energies to unphosphorylated ligands. This is inconsistent to the previous data showing low affinity of EAT2 toward unphosphorylated peptides compared to SAP which shows high affinity
Data indicate that Ewing's sarcoma-associated transcript-2 (EAT-2) over-expression increased the anti-tumor activity of NK cells against K562 tumor cell. targets.
EAT-2 mediates its effects in natural killer cells by linking SLAM family receptors to phospholipase Cgamma, calcium fluxes, and Erk kinase.
NTB-A-mediated IFN-gamma production was greatly reduced in the absence of SLAM-associated protein (SAP), demonstrating that cytokine production and cytotoxicity are differentially dependent on SAP and possibly EAT-2
By binding phosphotyrosines through its free SRC (MIM 190090) homology-2 (SH2) domain, EAT2 regulates signal transduction through receptors expressed on the surface of antigen-presenting cells (Morra et al., 2001
, EWS/FLI1-activated transcript 2
, SH2 domain-containing molecule EAT2
, SH2 domain-containing protein 1B
, SH2 domain containing 1B
, SH2 domain protein 1B1