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Thymus development depends on a complex series of interactions between thymocytes and the stromal component of the organ. Additionally we are shipping MPZL2 Antibodies (64) and many more products for this protein.
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CLCA2 (show CLCA2 Proteins) links junctional adhesion molecule (show AMICA1 Proteins) EVA1, to cytosolic signaling proteins that modulate proliferation and differentiation.
Findings highlight Eva1 as a novel regulator of GIC function and also provide new mechanistic insight into the role of noncanonical NF-kappaB (show NFKB1 Proteins) activation in GIC.
EVA (show SLC26A4 Proteins) is expressed in human choroid plexus epithelial cells and CD4 (show CD4 Proteins) T lymphocytes and regulates CD4 (show CD4 Proteins)+ T lymphocyte adhesion to human choroid plexus epithelial cells in vitro. These data suggest a novel mechanism to regulate CNS immune surveillance.
EVA deficiency results in increased experimental autoimmune encephalomyelitis disease severity. EVA-knockout Mice have normal immune system development and choroid plexus morphology.
modulation of Eva1 expression in thymocytes is crucial for lymphocyte physiological developmental progression and stromal differentiation
These results suggest that EVA expressed in choroid plexus cells may regulate the permeability of the blood-CSF (show CSF2 Proteins) barrier.
Thymus development depends on a complex series of interactions between thymocytes and the stromal component of the organ. Epithelial V-like antigen (EVA) is expressed in thymus epithelium and strongly downregulated by thymocyte developmental progression. This gene is expressed in the thymus and in several epithelial structures early in embryogenesis. It is highly homologous to the myelin protein zero and, in thymus-derived epithelial cell lines, is poorly soluble in nonionic detergents, strongly suggesting an association to the cytoskeleton. Its capacity to mediate cell adhesion through a homophilic interaction and its selective regulation by T cell maturation might imply the participation of EVA in the earliest phases of thymus organogenesis. The protein bears a characteristic V-type domain and two potential N-glycosylation sites in the extracellular domain\; a putative serine phosphorylation site for casein kinase 2 is also present in the cytoplasmic tail. Two transcript variants encoding the same protein have been found for this gene.
epithelial V-like antigen 1
, myelin protein zero-like 2
, myelin protein zero-like protein 2