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Tricellulin Proteins (MARVELD2)

The protein encoded by MARVELD2 is a membrane protein found at the tight junctions between epithelial cells. Additionally we are shipping Tricellulin Antibodies (27) and many more products for this protein.

list all proteins Gene Name GeneID UniProt
Rat MARVELD2 MARVELD2 365657  
MARVELD2 218518 Q3UZP0
MARVELD2 153562 Q8N4S9
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Top Tricellulin Proteins at antibodies-online.com

Showing 5 out of 7 products:

Catalog No. Origin Source Conjugate Images Quantity Supplier Delivery Price Details
HOST_Escherichia coli (E. coli) Human His tag „Crystallography Grade“ protein due to multi-step, protein-specific purification process 1 mg Log in to see 29 to 34 Days
$4,331.68
Details
Insect Cells Human rho-1D4 tag „Crystallography Grade“ protein due to multi-step, protein-specific purification process 0.5 mg Log in to see 49 to 54 Days
$6,041.49
Details
Insect Cells Mouse rho-1D4 tag „Crystallography Grade“ protein due to multi-step, protein-specific purification process 0.25 mg Log in to see 49 to 54 Days
$4,244.78
Details
HOST_Escherichia coli (E. coli) Mouse His tag „Crystallography Grade“ protein due to multi-step, protein-specific purification process 1 mg Log in to see 29 to 34 Days
$4,331.68
Details
HOST_Human Human Un-conjugated   20 μg Log in to see 9 to 11 Days
$785.40
Details

MARVELD2 Proteins by Origin and Source

Origin Expressed in Conjugate
Mouse (Murine) ,
,
Human , ,
,

More Proteins for Tricellulin (MARVELD2) 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. 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.

  2. High tricellulin expression is associated with hepatocellular carcinoma.

  3. 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.

  4. 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.

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

  6. 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.

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

  8. the tricellulin expression profile in normal and neoplastic human pancreas

  9. tricellulin and its role in tight junction formation and maintenance

  10. tricellulin is markedly reduced at all stages of tumor development. In situ hybridization analysis showed no correlation between HPV infection and altered expression of the tight junction proteins.

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.

Gene names and symbols associated with Tricellulin Proteins (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

GENE ID SPECIES
365657 Rattus norvegicus
218518 Mus musculus
153562 Homo sapiens
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