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HCST encodes a transmembrane signaling adaptor that contains a YxxM motif in its cytoplasmic domain. Additionally we are shipping HCST Kits (8) and HCST Proteins (5) and many more products for this protein.
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Human Polyclonal HCST Primary Antibody for ELISA, WB - ABIN547785
Upshaw, Arneson, Schoon, Dick, Billadeau, Leibson: NKG2D-mediated signaling requires a DAP10-bound Grb2-Vav1 intermediate and phosphatidylinositol-3-kinase in human natural killer cells. in Nature immunology 2006
These results suggest that NKG2D-DAP10 endocytosis represents a means to decrease cell surface receptor abundance, as well as to control signaling outcome in cytotoxic lymphocytes.
findings indicate that the functional interaction between RAGE and DAP10 coordinately regulates S100A8/A9-mediated survival and/or apoptotic response of keratinocytes
TGF-beta1 may reduce the expression of NKG2D/DAP10 and 2B4/SAPin patients with hepatitis B.
HMBOX1 negatively regulates the expression of NKG2D and the activation of the NKG2D/DAP10 signaling pathway in NK cells.
Other gamma(c) cytokines act similarly to IL-2 in up-regulating DAP10 expression and NKG2D-DAP10 surface expression.
TGF-BETA1 down-modulates surface NKG2D expression by controlling the transcriptional and translational levels of DAP10.
A transgenic mouse model demonstrates that induction of tolerance in Ly49H-positive natural killer (NK) cells by chronic exposure to virus-encoded ligand m157 requires signaling through the Ly49H adaptor protein DAP12, not the DAP10 adaptor protein.
NKG2D-DAP10 triggers human NK cell-mediated killing via a Syk-independent regulatory pathway.
both activated and expanded CD8+ T cells and NK cells use DAP10 for cytolysis
Downstream targets of DAP10 and DAP12 are constitutively activated in large granular lymphocyte leukemia cells, and expression of dominant-negative DAP10 and DAP12 dramatically reduces their lytic capacity.
the rapid degradation of NKG2D/DAP10 observed coincident with recruitment of the receptor to the cytotoxic immune synapse may explain the loss of NKG2D receptor expression after chronic exposure to NKG2D ligands
Adoptive transfer of murine T cells expressing a chimeric-PD1-Dap10 receptor may induce a preferential cytokine profile and T-cell differentiation phenotype for anti-lymphoma therapies.
Rat and mouse CD94/NKG2C heterodimers bind efficiently to both DAP12 and DAP10; this binding is critically dependent on the transmembrane lysine residue of CD94.
contributes to CD8(+) T cell-mediated cytotoxic effector mechanisms during Mycobacterium tuberculosis infection
demonstrate a previously uncharacterized interaction of SHIP1 with DAP12 that limits TREM2- and DAP12-dependent signaling and identify a mechanism through which SHIP1 regulates key ITAM-containing receptors by blocking the binding and activation of PI3K
selective associations with DAP10 determine stimulatory versus costimulatory activity of NKG2D
Differential requirements for Vav proteins in DAP10- and ITAM-mediated NK cell cytotoxicity.
The importance of Fcgr3/Cd3z, Hcst, and Tyrobp in the activation of NK cells in the uterus of pregnant mice is reported.
Review of immune reactions against syngeneic tumors reveals an important physiological role of DAP10 adapter protein signaling in maintaining tolerance to self, by controlling the development and activation threshold of autoreactive T cells.
DAP10 signaling is involved in adjusting the activation threshold and generation of natural killer T cells and regulatory T cells to avoid autoreactivity, but it also modulates antitumor mechanisms.
improved rejection of B16 melanomas in DAP10-deficient mice
these data demonstrate that DAP10 does associate with Ly49H and Ly49D in primary NK cells.
MDL-1 associates with both DAP12 and DAP10 in osteoclasts and bone marrow-derived macrophages, where DAP10 association depends almost entirely on DAP12, suggesting a formation of MDL-1-DAP12/DAP10 trimolecular complexes.
Optimal natural killer cell-mediated immunity to cytomegalovirus depends on Ly49H signaling through DAP10 and DAP12.
cloning, sequencing, and cell surface expression pattern
The structure of the adaptor protein dap10 has been identified in the zebrafish genome.
This gene encodes a transmembrane signaling adaptor that contains a YxxM motif in its cytoplasmic domain. The encoded protein may form part of the immune recognition receptor complex with the C-type lectin-like receptor NKG2D. As part of this receptor complex, this protein may activate phosphatidylinositol 3-kinase dependent signaling pathways through its intracytoplasmic YxxM motif. This receptor complex may have a role in cell survival and proliferation by activation of NK and T cell responses. Alternative splicing results in two transcript variants encoding different isoforms.
DNAX-activation protein 10
, kinase assoc pro of ~10kDa
, kinase assoc protein
, membrane protein DAP10
, phosphoinositide-3-kinase adaptor protein
, transmembrane adapter protein KAP10
, immunoreceptor DAP10
, hematopoietic cell signal transducer
, putative membrane adaptor molecule
, hematopoietic cell signal transducer A
, hematopoietic cell signal transducer L homeolog
, signal subunit, signaling transmembrane co-receptor