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Mouse (Murine) CD83 ELISA Kit for Sandwich ELISA - ABIN425143
Kreiser, Eckhardt, Kuhnt, Stein, Krzyzak, Seitz, Tucher, Knippertz, Becker, Günther, Steinkasserer, Lechmann: Murine CD83-positive T cells mediate suppressor functions in vitro and in vivo. in Immunobiology 2014
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Our findings indicate that CD83 homotypic interactions regulate DC activation and promote mucosal homeostasis.
CD83(+) T cells share important features with regulatory T cells, identifying CD83 as a novel lineage marker to discriminate between different T cell populations.
CD83 differentially modulates follicular and marginal zone B cell responses
Dendritic cells co-cultivated with antigen-specific induced Tregs expressed lower levels of CD83. A major suppressive mechanism of DC function by iTregs is secondary to the effects of IL-10 (show IL10 ELISA Kits) on MARCH1 & CD83 expression.
activated T cells induce CD83 on B cells via CD40 engagement but independent of TCR/MHC binding and thus independent of antigen-specificity of B cells.
found that the transmembrane domain of CD83 enhances MHC class II and CD86 expression by blocking MHC class II association with the ubiquitin ligase MARCH1
Data strongly suggest that CD83 is expressed by B cells upon activation and contributes to the regulation of B cell function.
Cd36 (show CD36 ELISA Kits), Cd44 (show CD44 ELISA Kits) and Cd83 might play a role in specific neural circuits and present functions other than those attributed to leukocyte biology and these surface proteins, or their associated mRNA, could be used to label neurons in specific circuits/regions
Soluble CD83-Ig fusion protein is immunosuppressive, costimulatory when coimmobilized with anti-CD3 (show CD3E ELISA Kits), and by interacting with its ligand(s) is involved in regulation of immune response to tumor.
CD83 expression influences CD4 (show CD4 ELISA Kits)+ T cell development in the thymus.
Crystal structure of human CD83 reveals that its surface domain consists of an Ig-like domain only.CD83 exerts its immunological activity by mixed homotypic and heterotypic interactions as typically observed for proteins present in the immunological synapse.
this study shows that dendritic cells from rheumatoid arthritis patients have low expression levels of CD83
Triple costimulation via CD80 (show CD80 ELISA Kits), 4-1BB (show TNFRSF9 ELISA Kits), and CD83 ligand elicits the long-term growth of Vgamma9Vdelta2 T cells in low levels of IL-2 (show IL2 ELISA Kits).
nonspreading Rift Valley fever virus infection of monocyte-derived immature denditic cells results in incomplete maturation, associated with gradual downregulation of CD83.
Sustained expression of CD83 was observed when CD4 (show CD4 ELISA Kits)+ T cells were induced by transforming growth factor-beta to differentiate into CD4 (show CD4 ELISA Kits)+CD25 (show IL2RA ELISA Kits)+ forkhead box P3 (show FOXP3 ELISA Kits)+ regulatory T (iTreg) cells.
These results suggest that HTLV-I induces CD83 expression on T cells via Tax1 (show CNTN2 ELISA Kits) -mediated NF-kappaB (show NFKB1 ELISA Kits) activation, which may promote HTLV-I infection in vivo.
GRASP55 (show GORASP2 ELISA Kits) interacts with CD83 shortly after induction of dendritic cells maturation and that this interaction plays a role in CD83 glycosylation as well as in surface expression of CD83 on dendritic cells.
IDO (show IDO1 ELISA Kits) and CD83 are expressed differently in human epidermal Langerhans cells
HSV-1 ICP0 alone induces CD83 degradation independent of its E3 ubiquitin ligase function and of the ubiquitin machinery.
The protein encoded by this gene is a single-pass type I membrane protein and member of the immunoglobulin superfamily of receptors. The encoded protein may be involved in the regulation of antigen presentation. A soluble form of this protein can bind to dendritic cells and inhibit their maturation. Three transcript variants encoding different isoforms have been found for this gene.
, B-cell activation protein
, CD83 antigen
, CD83 antigen (activated B lymphocytes, immunoglobulin superfamily)
, cell surface protein HB15
, cell-surface glycoprotein