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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 Proteins (12) and JAM3 Kits (8) and many more products for this protein.
Showing 10 out of 76 products:
Human Monoclonal JAM3 Primary Antibody for ELISA - ABIN394998
Bailey, Xie, Do, Montpetit, Diaz, Mohan, Keavney, Yusuf, Gerstein, Engert, Anand: Variation at the NFATC2 locus increases the risk of thiazolidinedione-induced edema in the Diabetes REduction Assessment with ramipril and rosiglitazone Medication (DREAM) study. in Diabetes Care 2010
Show all 5 references for ABIN394998
Human Polyclonal JAM3 Primary Antibody for WB - ABIN1882171
Arrate, Rodriguez, Tran, Brock, Cunningham: Cloning of human junctional adhesion molecule 3 (JAM3) and its identification as the JAM2 counter-receptor. in The Journal of biological chemistry 2001
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Human Monoclonal JAM3 Primary Antibody for Func, IHC (fro) - ABIN2475176
Matsuo, Aoki, Kawagoe, Kogure: [Pathophysiology of cerebral ischemia]. in Tanpakushitsu kakusan koso. Protein, nucleic acid, enzyme 1992
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Human Monoclonal JAM3 Primary Antibody for EIA, IHC (fro) - ABIN1107891
Aurrand-Lions, Duncan, Ballestrem, Imhof: JAM-2, a novel immunoglobulin superfamily molecule, expressed by endothelial and lymphatic cells. in The Journal of biological chemistry 2001
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Mouse (Murine) Polyclonal JAM3 Primary Antibody for ELISA - ABIN2000989
Mandicourt, Iden, Ebnet, Aurrand-Lions, Imhof: JAM-C regulates tight junctions and integrin-mediated cell adhesion and migration. in The Journal of biological chemistry 2007
interaction between Jamb (show JAM2 Antibodies) and Jamc expressed by neighbouring cells is essential for fusion. jamc is ectopically expressed in prdm1a (show PRDM1 Antibodies) mutant slow muscle precursors, which inappropriately fuse with other myocytes.
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 Antibodies)/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 Antibodies) 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 Antibodies)) 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.
Data indicate deletion of JAM-C in deletion of JAM-C in Schwann cells (SCs (show TWIST1 Antibodies)) (JAM-C SC KO) mice showed electrophysiological defects, muscular weakness, and hypersensitivity to mechanical stimuli.
Endothelial cell JAM-C has a key role in supporting luminal-to-abluminal migration of neutrophils in vivo, suggsting that reverse transepithial cell migration of neutrophils can contribute to the dissemination of systemic inflammation.
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.
These data brought new evidences for the role of JAM2 (show JAM2 Antibodies) and JAM3 in progression of gastric adenocarcinoma
In the present study, we investigated the role of JAM-C in homing of human B cells, using a xenogeneic nonobese diabetic/severe combined immunodeficient mouse model.
JAM-C expression was identified in human and murine melanoma cell lines, in human malignant melanoma, as well as in metastatic melanoma including melanoma lung metastasis
Our results suggest that JAM3 is essential for maintaining the integrity of the cerebrovascular endothelium as well as for normal lens development in humans
Soluble JAM-C mediates facets of angiogenesis in vitro and contributes the angiogenic potential of rheumatoid arthritis synovial fluid.
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