Use your antibodies-online credentials, if available.
No Products on your Comparison List.
Your basket is empty.
Find out more
Show all species
Show all synonyms
Select your species
Findings suggest that both tricellular tight junctions proteins TRIC and LSR have crucial roles for the differentiated cochlear cell survival.
Tricellulin is a specific redox sensor and sealing element at 3-cell contacts and may compensate as a redox mediator for occludin (show OCLN ELISA Kits) loss at 2-cell contacts in vivo and in vitro.
GFP-tagged angulin-1/LSR, in which serine 288 was substituted by alanine, was observed to be dispersed to bicellular junctions, indicating that phosphorylation of Ser288 is crucial for the exclusive localization of angulin-1/LSR and tricellulin at tTJs.
localization of angulin-1/LSR and tricellulin at tricellular contacts of brain and retinal endothelial cells in vivo
Loss of tricellulin prevented the coalition of the strands of the bicellular junction with the central element of the tricellular junction in the inner ear epithelia.
The findings show the heterogeneity of the molecular organization of tTJs in terms of the content of LSR, ILDR1 (show ILDR1 ELISA Kits) or ILDR2, and suggest that ILDR1 (show ILDR1 ELISA Kits)-mediated recruitment of tricellulin to TCs is required for hearing.
The tricellulin may be a component to maintain the integrity for PNS myelin function and morphology.
marvelD3, occludin (show OCLN ELISA Kits), and tricellulin define the tight junction-associated MARVEL protein family
In this study, we identify tricellulin, the first integral membrane protein that is concentrated at the vertically oriented TJ strands of tricellular contacts.
In the inner ear, tricellulin is concentrated at the tricellular tight-junctions in cochlear and vestibular epithelia, including the structurally complex and extensive junctions between supporting and hair cells.
Tricellulin-dependent macromolecule passage was comparably regulated in leaky and tight epithelia, but relative and absolute ion permeabilities of the tricellular tight junction (tTJ) were different.
Data show that the E3 ubiquitin ligase Itch forms a complex with tricellulin and thereby enhances its ubiquitination.
we demonstrated that PLG functions as a molecular bridge between tricellulin and streptococcal surface enolase (SEN). The wild type strain efficiently translocated across the epithelial monolayer, accompanied by cleavage of transmembrane junctional proteins.
The expressions of MARVELD2, CLDN1 (show CLDN1 ELISA Kits) and CLDN3 (show CLDN3 ELISA Kits) mRNA were significantly lower in cholesteatoma tissue and may be involved in epithelium permeability.
High tricellulin expression is associated with hepatocellular carcinoma.
MARVELD2 variants are responsible for about 1.5 % (95 % CI 0.8-2.6) of non-syndromic hearing loss in our cohort of 800 Pakistani families. The c.1331+2T>C allele is recurrent.
This study reveals the presence and subcellular distribution of tricellulin in brain endothelial cells.
The dynamic behavior of tricellulin during the destruction and formation of tight junctions (TJ) under various extracellular calcium conditions seems to be closely associated with the barrier and fence functions of TJs.
DFNB49 is an important cause of non-syndromic deafness in Czech Roma patients but not in the general Czech population.
The protein encoded by this gene is a membrane protein found at the tight junctions between epithelial cells. The encoded protein helps establish epithelial barriers such as those in the organ of Corti, where these barriers are required for normal hearing. Defects in this gene are a cause of deafness autosomal recessive type 49 (DFNB49). Two transcript variants encoding different isoforms have been found for this gene.
MARVEL (membrane-associating) domain containing 2
, MARVEL domain-containing protein 2