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Validated All-in-One™ qPCR Primer for TJP1(NM_003257.4) Search again
Product ID:
HQP110674
(click here to view gene annotation page)
Powered by BiozSpecies:
Human
Symbol:
Alias:
ZO-1
Gene Description:
tight junction protein 1
Target Gene Accession:
NM_003257.4(click here to view gene page)
Estimated Delivery:
Approximately 1-3 weeks, but may vary. Please email sales@genecopoeia.com or call 301-762-0888 to confirm ETA.
Important Note:
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.
Validated result:
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| A | B |
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Each All-in-One™ qPCR Primer is experimentally validated to yield a single dissociation curve peak and to generate a single amplification of the correct size for the targeted gene. A cDNA Pool, containing reverse transcript products of 8 different human tissue total RNA(Liver, Testis,Muscle,Thyroid,Brain,Spleen,Stomach,Small Intestine)),was used as the qPCR validation template. qPCR was performed using 0.2 µM primer with 2XAll-in-One™ qPCR Mix (Catalog#: QP001,QP002,QP004,QP005). Reactions were incubated for 10min. at 95°C, followed by 40 cycles of 95°C for 10 sec.; 60°C, 20 sec. and 72°C, 15sec. using Bio-Rad iQ5™ Instrument. At the end of the last cycle, temperature was increased from 72 to 95°C to produce a melting curve. Panel A: Validated Result for Amplification Curve; Panel B: Validated Result for Melting Curve. |
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Summary
This gene encodes a protein located on a cytoplasmic membrane surface of intercellular tight junctions. The encoded protein may be involved in signal transduction at cell-cell junctions. Two transcript variants encoding distinct isoforms have been identified for this gene. [provided by RefSeq].
Gene References into function
- Data show that connexin 43 (cx43) binds alpha-tubulin equally well as beta-tubulin, and that ZO-1 binds directly to Cx43.
- oxidative stress induces tyrosine phosphorylation and cellular redistribution of occludin-ZO-1 and E-cadherin-beta-catenin complexes by a tyrosine-kinase-dependent mechanism
- Tyrosine phosphorylation of ZO-1 leads to down-regulation of the function of ZO-1 and dedifferentiation of the glands in colorectal cancers. These phenomena contribute to liver metastases, & redifferentiation of the glands occurs in the liver metastases.
- dedifferentiation and a decreased expression of E-cadherin and ZO-1 are closely related to liver metastasis
- Modulatory role of VIPergic submucosal neuronal pathways on intestinal epithelial barrier permeability and ZO-1 expression.
- Interactions with ZO-1 and ZO-2, in particular, may mediate recruitment of armadillo repeat gene deletes in velocardiofacial syndrome protein to the plasma membrane and the nucleus
- The ZO-1 present in the tight junctions in HepG2 cells cultured in the presence or absence of retinoic acid.
- The scaffolding protein ZO-1 co-localizes with transient receptor potential channel 4 protein TRPC4 in resting astrocytes at the cell membrane.
- Activation of PKC by the phorbol ester TPA induced ZO-1 and occludin transcription, whereas PKC inhibition lead to decreased expression levels
- Increased ZO-1 in melanoma contributes to oncogenic behavior. Protein products of genes such as ZO-1 can function in either pro- or anti-oncogenic manner when expressed in different cellular contexts.
- Rsults show that ZO-1 can intervene in signaling events promoting tumor cell invasion.
- Structural analyses reveal that the differences between Erbin PDZ domain and the first PDZ domain of ZO-1 in specificity can be accounted for by two key differences in primary sequence.
- two ZO-1 complexes may coordinate two important S1P-mediated functions, i.e. migration and barrier integrity, in vascular endothelial cells
- I human intestinal epithelium, ZO-1 was localized to the apical pole of cells neighboring a shedding event (shedding of epithelial cells).
- Variants in TJP1 do not appear to be major determinants for albuminuria in the San Antonio Family Diabetes/Gallbladder Study.
- findings show that zonula occludens-1 is recruited to actin tails and pedestals; it is proposed that certain pathogenic bacteria create particular actin-rich structures that attract ZO-1 through a signal generated by WASP-related molecules
- Sertoli cells associated with carcinoma in situ of the testicles show an altered distribution of ZO-1 protein and loss of blood-testis barrier function.
- ZO-1 accumulated at cell-to-cell junctions of the breast neoplasm cell line.
- Triglyceride rich lipoprotein lipolysis products regulate ZO-1 expression at endothelial cell tight junctions to alter permeability.
- Helicobacter pylori infected gastric epithelial cells showed altered ZO-1 distribution.
- the interaction between Cx43 and ZO-1 is regulated by the proteasome
- It is concluded that in patients with heart failure, down-regulation of ZO-1 matches the diminished expression levels of connexin 43, suggesting that ZO-1 plays an important role in gap junction formation and gap junction plaque stability.
- analysis of the structure of the second of the three PDZ domains of ZO-1, which is known to promote dimerization as well as bind to C-terminal sequences on connexins
- Reduced claudin-1 expression correlates with loss of differentiation in thyroid neoplasms.
- Findings suggest that ZO-1, by interacting with Cx43, plays a role in the down-regulation and decreased size of Cx43 gap junctions in congestive heart failure.
- The aims of our study were: (i) to investigate the effect of alcohol on miRNA-212 (miR-212) and on expression of its predicted target gene, ZO-1, (ii) to study the potential role of miR-212 in the pathophysiology of ALD in man.
- Hepatocellular carcinomas and metastases are characterized by markedly different protein expression pattern of occludin and ZO-1, which phenomenon might be attributed to the different histogenesis of these tumors.
- Rsults suggest that the lower epithelial alpha-catenin, E-cadherin and (or) ZO-1 expression in patients with atopic asthma contributes to a defective airway epithelial barrier and a higher influx of eosinophils in the epithelium.
- These data demonstrate that the tight junction undergoes constant remodeling and suggest that this dynamic behavior may contribute to tight junction assembly and regulation.
- JunD is a biological suppressor of ZO-1 expression in intestinal epithelial cells and plays a critical role in maintaining epithelial barrier function
- domain-swapped dimerization of zonula occludens-1 PDZ2 generates a distinct interface that functions together with the well-separated canonical carboxyl tail-binding pocket in each PDZ unit in binding to connexin43 (Cx43)
- Targets to gap junction edges independently of several known PDZ2 domain-mediated interactions.
- Hepatocyte tight junctions-associated proteins occludin, claudin-1, and Zonula Occludens protein-1 (ZO-1) disappeared from the borders of adjacent cells in hepatoma cells harboring genomic hepatitis c virus replicons.
- tyrosine phosphorylation of Neph1 mediated by Fyn results in significantly increased Neph1 and ZO-1 binding, suggesting a critical role for Neph1 tyrosine phosphorylation in reorganizing the Neph1-ZO-1 complex.
- a unique motif in the occludin sequence that is involved in the regulation of ZO-1 binding by reversible phosphorylation of specific Tyr residues.
- Muscarinic-induced recruitment of plasma membrane Ca2+-ATPase involves PSD-95/Dlg/Zo-1-mediated interactions.