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TJP2 encodes a zonula occluden that is a member of the membrane-associated guanylate kinase homolog family. Zusätzlich bieten wir Ihnen TJP2 Antikörper (106) und TJP2 Kits (7) und viele weitere Produktgruppen zu diesem Protein an.
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Biochemistry and microscopy approaches in T cells confirmed SNX27 (zeige SNX27 Proteine)/ZO-2 PDZ-dependent interaction, and demonstrated its role controlling the dynamic localization of ZO-2 at the IS
A likely causal mutation was identified in the majority (61%), spanning many genes including ones that have only rarely been reported to cause cholestatic liver disease, e.g. TJP2 and VIPAS39 (zeige VIPAR Proteine)
Patients with a confirmed ABCB11 (zeige ABCB11 Proteine) or tight junction protein 2 gene mutation (n = 7) had a minimally detectable THBA proportion (0.23-2.99% of total BAs). Three patients with an ATP8B1 (zeige ATP8B1 Proteine) mutation had an elevated THBA proportion (7.51-37.26%).
Studies indicate the modular and supramodular organization of zonula occludens protein 2 (ZO-2) that allows it to interact with a wide variety of molecules, including cell-cell adhesion proteins, cytoskeletal components, and nuclear factors.
Data identified two Disease-causing Genes TJP2 and GJB2 (zeige GJB2 Proteine) in a Chinese Family with Unconditional Autosomal Dominant Nonsyndromic Hereditary Hearing Impairment.
TJP2 deficiency may predispose to hepatocellular carcinoma in early childhood
Claudin-19 (zeige CLDN19 Proteine), the most abundant claudin in myelin, exhibited no binding to ZO2.
JAM-A (zeige F11R Proteine) regulates epithelial permeability via association with ZO-2, afadin, and PDZ-GEF1 (zeige RAPGEF2 Proteine) to activate Rap2c (zeige RAP2C Proteine) and control contraction of the apical cytoskeleton.
Protein-truncating mutations in the tight junction protein 2 gene cause failure of protein localization and disruption of tight-junction structure, leading to severe cholestatic liver disease.
demonstrated that ZO-2 inhibition increases invasive and migrative capacities of invasive tumor cells. This was associated with an increase of MT1-MMP (zeige MMP14 Proteine)
In the present study, we found that the protein level of ZO-2, a scaffolding tight junction protein (zeige OCLN Proteine), decreased in the bladder of OVX mice indicating a possible role in overactive bladder.
Expression of Podocalyxin (zeige PODXL Proteine), which positively regulates the formation of microvilli and the apical membrane, is repressed in embryoid bodies lacking both ZO-1 (zeige TJP1 Proteine) and ZO-2 and this correlates with an aberrant submembranous localization of Ezrin (zeige EZR Proteine).
SNX27 (zeige SNX27 Proteine) associates with ZO-2 and modulates the epithelial tight junction.
ZO-2 protects against podocyte dysfunction induced by adreiamycin. This action is regulated by ZO-2-mediated inhibition of the Wnt (zeige WNT2 Proteine)/beta-catenin (zeige CTNNB1 Proteine) signaling pathway
the first PDZ domain of ZO-2 interacts with YAP2 to form complex; ZO-2 facilitates both nuclear translocation of YAP2 & pro-apoptotic function of YAP2; these activities of ZO-2 are PDZ-domain-dependent
Male ZO-2 chimeras show reduced fertility and pathological changes in the testis. Lanthanum tracer experiments show a compromised blood-testis barrier.
nuclear ZO-2 is present in epithelial and endothelial cells, particularly in response to environmental stress conditions
ZO-1 (zeige TJP1 Proteine) and ZO-2 function redundantly to some extent in junction formation/epithelial polarization but they are not functionally identical
These findings indicate that ZO-1 (zeige TJP1 Proteine) and ZO-2 can independently determine whether and where claudins are polymerized.
These results suggest novel roles for ZO proteins as Src (zeige SRC Proteine)/Csk (zeige CSK Proteine) scaffolds potentially involved in the regulation of Src (zeige SRC Proteine) transformation.
analysis of tissue distribution and developmental expression of tjp1/zo-1 (zeige TJP1 Proteine), tjp2/zo-2 and tjp3/zo-3 (zeige TJP3 Proteine) in the zebrafish, Danio rerio
This gene encodes a zonula occluden that is a member of the membrane-associated guanylate kinase homolog family. The encoded protein functions as a component of the tight junction barrier in epithelial and endothelial cells and is necessary for proper assembly of tight junctions. Mutations in this gene have been identified in patients with hypercholanemia, and genomic duplication of a 270 kb region including this gene causes autosomal dominant deafness-51. Alternatively spliced transcripts encoding multiple isoforms have been observed for this gene.
Friedreich ataxia region gene X104 (tight junction protein ZO-2)
, tight junction protein ZO-2
, zona occludens 2
, zonula occludens protein 2
, tight junction protein 2 (zona occludens 2)
, Tight junction protein ZO-2 (Zonula occludens 2 protein) (Zona occludens 2 protein) (Tight junction protein 2)
, zona occludens protein 2
, tight junction protein 2 L homeolog
, tight junction protein 2b