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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 [PubMed 11689425]).[supplied by OMIM, Mar 2008].. Additionally we are shipping SH2D1B Proteins (5) and many more products for this protein.
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Human Polyclonal SH2D1B Primary Antibody for FACS, IHC (p) - ABIN653070
Morra, Howie, Grande, Sayos, Wang, Wu, Engel, Terhorst: X-linked lymphoproliferative disease: a progressive immunodeficiency. in Annual review of immunology 2001
Show all 2 references for ABIN653070
Human Polyclonal SH2D1B Primary Antibody for EIA, FACS - ABIN954786
Tangye, van de Weerdt, Avery, Hodgkin: CD84 is up-regulated on a major population of human memory B cells and recruits the SH2 domain containing proteins SAP and EAT-2. in European journal of immunology 2002
Show all 2 references for ABIN954786
Human Polyclonal SH2D1B Primary Antibody for ELISA, WB - ABIN408654
Morra, Lu, Poy, Martin, Sayos, Calpe, Gullo, Howie, Rietdijk, Thompson, Coyle, Denny, Yaffe, Engel, Eck, Terhorst: Structural basis for the interaction of the free SH2 domain EAT-2 with SLAM receptors in hematopoietic cells. in The EMBO journal 2001
Human Polyclonal SH2D1B Primary Antibody for EIA, WB - ABIN375193
Clarkson, Simmonds, Puklavec, Brown: Direct and indirect interactions of the cytoplasmic region of CD244 (2B4) in mice and humans with FYN kinase. in The Journal of biological chemistry 2007
When compared with SAP (show APCS Antibodies), 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 (show APCS Antibodies) 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 (show SLAMF1 Antibodies) family receptors to phospholipase Cgamma, calcium fluxes, and Erk (show EPHB2 Antibodies) 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
EAT-2 negatively regulates cytokine production in dendritic cells downstream of SLAM (show SLAMF1 Antibodies) engagement and a genetic polymorphism that disturbs this process promotes the development of lupus.
EAT-2A and EAT-2B act as positive regulators of signaling lymphocyte activation molecule (show SLAMF1 Antibodies) family receptor-specific NK cell functions in C57BL/6 mice.
Taken together, the data suggest that both EAT-2A and EAT-2B are adapters that recruit Src (show SRC Antibodies) kinases to SLAM (show SLAMF1 Antibodies) family receptors using a mechanism that is distinct from that of SAP (show APCS Antibodies).
EAT-2 mediates CRACC (show SLAMF7 Antibodies) function. In the absence of EAT-2, CRACC (show SLAMF7 Antibodies) inhibited natural killer cell function.
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
SH2 domain protein 1B1
, SH2 domain containing 1B
, SH2 domain-containing protein 1B
, EWS/FLI1-activated transcript 2
, SH2 domain-containing molecule EAT2
, EWS/FLI1 activated transcript 2