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Tight junctions represent one mode of cell-to-cell adhesion in epithelial or endothelial cell sheets, forming continuous seals around cells and serving as a physical barrier to prevent solutes and water from passing freely through the paracellular space. Additionally we are shipping JAM3 Antibodies (99) and JAM3 Proteins (13) and many more products for this protein.
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interaction between Jamb (show JAM2 ELISA Kits) and Jamc expressed by neighbouring cells is essential for fusion. jamc is ectopically expressed in prdm1a (show PRDM1 ELISA Kits) mutant slow muscle precursors, which inappropriately fuse with other myocytes.
JAM-B (show JAM2 ELISA Kits)/JAM-C mediated interaction between endothelial cells and stellate cells stabilizes vessel walls and may control the sinusoidal diameter.
Study provides evidence that JAM-C downregulation may contribute to acute pancreatitis-associated lung injury via reverse transendothelial migration of neutrophils.
Endothelial-specific deletion of JAM-C promoted endothelial cell sprouting, and consequently vessel normalisation and revascularisation of the hypoxic retina without altering pathologic neovascularisation.
JAM-C blockade can finely-tune the innate cell migration and accelerate the consequent immune response to L. major without changing the type of the T helper cell response.
Function of Jam-B (show JAM2 ELISA Kits)/Jam-C interaction in homing and mobilization of human and mouse hematopoietic stem and progenitor cells.
These findings provide evidence for a role for endothelial cell JAM-C in tumor growth and aggressiveness as well as recruitment of pericytes to newly formed blood vessels in a model of ovarian cancer.
JAM-C might be involved in the final steps of trafficking and transmigration of antigen-specific autoaggressive T-cells to the islets of Langerhans.
study suggests that JAM-C(-/-) C57BL/6 mice model the important role for JAM-C in brain development and CSF (show CSF2 ELISA Kits) homeostasis as recently observed in humans with a loss-of-function mutation in JAM-C
Data show that junctional adhesion molecule-B (JAM-B (show JAM2 ELISA Kits)) expressed by endothelial cells contributes to murine B16 melanoma cells metastasis through its interaction with junctional adhesion molecule-C (JAM-C) on tumor cells.
Results indicate that in vivo JAM-C shows enrichment at the apical surface and therefore is asymmetrically distributed during cell divisions.
The role of JAM-C in the engraftment of human lymphoma B cells in mice was investigated. The binding of anti-JAM-C antibodies inhibited the phosphorylation of ERK1/2 (show MAPK1/3 ELISA Kits), without affecting other signaling pathways, identifying for the first time the intracellular MAPK (show MAPK1 ELISA Kits) cascade as the JAM-C-driven signaling pathway in JAM-C(+) B cells.
blocking JAM-C can reduce the number of atherogenic monocytes/macrophages in plaques by emigration.
Palmitoylation of JAM-C promotes its localization to tight junctions and inhibits transwell migration of A549 lung cancer cells.
Suggest JAM3-M4 methylation as a biomarker for diagnosis of preneoplastic and neoplastic lesions of the cervix.
JAM-C inactivation in endothelial cells resulted in increased spreading on fibronectin and enhanced sprouting in vitro in a manner dependent on beta1-integrin and on the activation of the small GTPase RAP1.
indicate that JAM-C may be a therapeutic target for preventing and treating lymphatic metastases
Our study confirms the importance of JAM3 as a component of the junctional complexes and its deficiency leading to a distinctive and catastrophic neonatal presentation of cataracts and hemorrhagic destruction of the brain.
Tight junctions represent one mode of cell-to-cell adhesion in epithelial or endothelial cell sheets, forming continuous seals around cells and serving as a physical barrier to prevent solutes and water from passing freely through the paracellular space. The protein encoded by this immunoglobulin superfamily gene member is localized in the tight junctions between high endothelial cells. Unlike other proteins in this family, the this protein is unable to adhere to leukocyte cell lines and only forms weak homotypic interactions. The encoded protein is a member of the junctional adhesion molecule protein family and acts as a receptor for another member of this family. A mutation in an intron of this gene is associated with hemorrhagic destruction of the brain, subependymal calcification, and congenital cataracts. Alternative splicing results in multiple transcript variants.
junctional adhesion molecule 3
, JAM-C-like protein
, junction cell adhesion molecule 3
, junction cell adhesion molecule C
, junctional adhesion molecule C