Browse our Tricellulin Proteins (MARVELD2)

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Tricellulin Proteins (MARVELD2)
On are 7 Tricellulin (MARVELD2) Proteins from 2 different suppliers available. Additionally we are shipping Tricellulin Antibodies (30) and Tricellulin Kits (1) and many more products for this protein. A total of 40 Tricellulin products are currently listed.
BC003296, DFNB49, MARVD2, MRVLDC2, Tric, Trica, Tricb, Tricc
list all proteins Gene Name GeneID UniProt
Rat MARVELD2 MARVELD2 365657  
MARVELD2 218518 Q3UZP0
MARVELD2 153562 Q8N4S9

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Tricellulin Proteins (MARVELD2) by Origin

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More Proteins for Tricellulin Interaction Partners

Mouse (Murine) Tricellulin (MARVELD2) interaction partners

  1. Tricellulin is a specific redox sensor and sealing element at 3-cell contacts and may compensate as a redox mediator for occludin (show OCLN Proteins) loss at 2-cell contacts in vivo and in vitro.

  2. 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.

  3. localization of angulin-1/LSR and tricellulin at tricellular contacts of brain and retinal endothelial cells in vivo

  4. 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.

  5. The findings show the heterogeneity of the molecular organization of tTJs in terms of the content of LSR, ILDR1 (show ILDR1 Proteins) or ILDR2, and suggest that ILDR1 (show ILDR1 Proteins)-mediated recruitment of tricellulin to TCs is required for hearing.

  6. The tricellulin may be a component to maintain the integrity for PNS myelin function and morphology.

  7. marvelD3 (show MARVELD3 Proteins), occludin (show OCLN Proteins), and tricellulin define the tight junction-associated MARVEL protein family

  8. In this study, we identify tricellulin, the first integral membrane protein that is concentrated at the vertically oriented TJ strands of tricellular contacts.

  9. 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.

  10. Knockdown of occludin (show OCLN Proteins) caused mislocalization of tricellulin to bTJs, implying that occludin (show OCLN Proteins) supports tricellular localization of tricellulin by excluding tricellulin from bicellular tight junctions.

Human Tricellulin (MARVELD2) interaction partners

  1. 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.

  2. Data show that the E3 ubiquitin ligase (show MUL1 Proteins) Itch forms a complex with tricellulin and thereby enhances its ubiquitination.

  3. 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.

  4. The expressions of MARVELD2, CLDN1 (show CLDN1 Proteins) and CLDN3 (show CLDN3 Proteins) mRNA were significantly lower in cholesteatoma tissue and may be involved in epithelium permeability.

  5. High tricellulin expression is associated with hepatocellular carcinoma.

  6. 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.

  7. The findings show the heterogeneity of the molecular organization of tTJs in terms of the content of LSR, ILDR1 (show ILDR1 Proteins) or ILDR2, and suggest that ILDR1 (show ILDR1 Proteins)-mediated recruitment of tricellulin to TCs is required for hearing.

  8. This study reveals the presence and subcellular distribution of tricellulin in brain endothelial cells.

  9. 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.

  10. DFNB49 is an important cause of non-syndromic deafness in Czech Roma patients but not in the general Czech population.

Tricellulin (MARVELD2) Protein Profile

Protein Summary

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.

Alternative names and synonyms associated with Tricellulin (MARVELD2)

  • MARVEL domain containing 2 (Marveld2)
  • MARVEL (membrane-associating) domain containing 2 (Marveld2)
  • MARVEL domain containing 2 (MARVELD2)
  • BC003296 protein
  • DFNB49 protein
  • MARVD2 protein
  • MRVLDC2 protein
  • Tric protein
  • Trica protein
  • Tricb protein
  • Tricc protein

Protein level used designations for Tricellulin Proteins (MARVELD2)

MARVEL (membrane-associating) domain containing 2 , MARVEL domain-containing protein 2 , tricellulin

365657 Rattus norvegicus
218518 Mus musculus
153562 Homo sapiens
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