|
ORF cDNA clones
|
CRISPR / TALEN
|
Lentivirus
|
AAV
|
TALE-TF
|
ORF knockin clones
|
|
Antibody
|
Proteins
|
miRNA target clones
|
qPCR primers
|
shRNA clones
|
miRNA products
|
Promoter clones
|
Validated All-in-One™ qPCR Primer for F11R(NM_016946.6) Search again
By default, qPCR primer pairs are designed to measure the expression level of the splice variant (accession number) you selected for this gene WITHOUT consideration of other possible variants of this gene. If this gene has multiple variants, and you would like to measure the expression levels of one particular variant, multiple variants, or all variants, please contact us for a custom service project at inquiry@genecopoeia.com.
Summary
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 an important regulator of tight junction assembly in epithelia. In addition, the encoded protein can act as (1) a receptor for reovirus, (2) a ligand for the integrin LFA1, involved in leukocyte transmigration, and (3) a platelet receptor.
Gene References into function
- F11 receptor (F11R) was discovered by Kornecki, 1990 (JBC, 265:10042) on platelets. A 100% homology exists between the platelet F11R and human JAM at the protein level.
- The F11 receptor (F11R) was discovered in 1990 (Kornecki et al.), partially sequenced (1995) and cloned (Sobocka, et al) by this group. A 100% homology exists between platelet F11R and JAM.
- Two domains in the N-terminus and 1st Ig-fold of F11R were found, through which M.Ab.F11 triggers platelet aggregation. These 2 regions form an active site within the conformation of this cell adhesion molecule.
- Effect of gene on proliferation arrest in a non-small cell bronchopulmonary cancer line.
- platelets adhere specifically to F11R of cytokine- (TNF-alpha, INF-gamma) stimulated vascular endothelial cells
- signaling through JAM-1 and alphavbeta3 is necessary for bFGF-induced angiogenesis.
- JAM-1 is required for basic fibroblast growth factor-induced extracellular signal-related kinase activation that leads to endothelial cell migration on vitronectin.
- homodimer formation may be important for localization of JAM1 at tight junctions and for regulation of epithelial barrier function
- JAM1 structure, role and tissue distribution (review)
- analysis of F11R dimerization, phosphorylation and complex formation with the integrin GPIIIa in human platelets
- JAM1 regulates epithelial cell morphology and beta1 integrin expression by modulating activity of the small GTPase Rap1.
- functional contribution of JAM-A to atherogenesis
- JAM-A transgene is prominently expressed in embryonic vasculature and the epithelial components of several organ systems of transgenic mice and may have an important role in their development
- signaling through JAM-A is necessary for alpha(v)beta(3)-dependent endothelial cells migration and implicate JAM-A in the regulation of vascular function.
- Data show that reovirus engages JAM-A monomers via residues found on beta-strands of the dimer and suggest that the distinct disease phenotypes produced by different strains of reovirus are in part due to differences in contacts with JAM-A.
- Junctional adhesion molecule-A is critical for the formation of pseudocanaliculi and modulates E-cadherin expression in hepatic cells
- the apparent occurrence of an unusual TG 3' splice site in intron 3 is discussed
- Examine JAM-1 expression in normal/inflammed lymphatic endothelium.
- Detection of JAM-A in human sperm proteins indicates that its role may be conserved in sperm motility.
- JAM-A plays a role in intestinal homeostasis by regulating epithelial permeability, inflammation, and proliferation
- Single nucleotide polymorphisms (SNPs) in the F11 receptor gene (F11R) are associated with hypertension and obesity in Hong Kong Chinese.
- JAM-A is essential for the development of polarity in cultured hepatic cells
- JAM-1 is expressed by human corneal epithelial and endothelial cells, but not by keratocytes, although its expression is induced in corneal myofibroblasts.
- results that an immunoglobulin superfamily cell adhesion protein, JAM-A, expressed at tight junctions could serve as a key negative regulator of breast cancer cell invasion and possibly metastasis.
- nonredundant and novel role of JAM-A in controlling mucosal homeostasis by regulating the integrity and permeability of epithelial barrier function
- These data indicate that JAM-A is required for the correct internalization and recycling of integrins during cell migration.
