The Drosophila segment polarity gene armadillo is required for pattern formation within embryonic segments and imaginal discs. We have found that armadillo is highly conserved during evolution; it is 63% identical to human plakoglobin, a protein found in adhesive junctions joining epithelial and oth …
catenin complex, cell-cell adherens junction, desmosome, nucleus, atrioventricular valve morphogenesis, cell adhesion, heart development, negative regulation of Wnt signaling pathway, negative regulation of Wnt signaling pathway involved in heart development
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Complete information for JUP gene (Protein Coding), Junction Plakoglobin, including: function, proteins, disorders, pathways, orthologs, and expression. GeneCards - The Human Gene Compendium
View Jup/Jup Tg(Myh6-cre)2182Mds/0 involves: 129 * C57BL/6J: phenotypes, images, diseases, and references.
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Plakoglobin interacts with both classical and desmosomal cadherins. It is closely related to Drosophila aramadillo (arm) gene product; arm acts in the wingless (wg)-signaling pathway to establish segment polarity. In Xenopus, homologs of wg--i.e., wnts, can produce anterior axis duplications by inducing dorsal mesoderm. Studies in Drosophila suggest that wnt acts by increasing the level of cytoplasmic armadillo protein (arm). To test whether simply increasing the level of plakoglobin mimics the effects of exogenous wnts in Xenopus, we injected fertilized eggs with RNA encoding an epitope-tagged form of plakoglobin; this induced both early radial gastrulation and anterior axis duplication. Exogenous plakoglobin accumulates in the nuclei of embryonic cells. Plakoglobin binds to the tail domain of the desmosomal cadherin desmoglein 1. When RNA encoding the tail domain of desmoglein was coinjected with plakoglobin RNA, both the dorsalizing effect and nuclear accumulation of plakoglobin were ...
4709 Plakoglobin (γ-catenin) and β-catenin are pivotal components of cell-cell adherent junctions, linking cadherin receptors to the actin cytoskeleton. Unlike β-catenin overexpression, which is implicated in proliferation and tumor formation, high levels of plakoglobin suppress cell growth and tumorigenicity, whereas reduction of plakoglobin expression was found in highly invasive and metastatic tumors. We studied the expression of β-catenin and plakoglobin in 5 alveolar (ARMS) and 4 embryonal (ERMS) rhabdomyosarcoma (RMS) cell lines and 11 RMS tumor biopsies, 4 ARMS carrying the translocation t(2;13)(q35;q14), 2 ARMS without translocation and 3 ERMS. We found a consistent and homogeneous β-catenin expression in all of the cell lines and tumors tested, while plakoglobin, detectable in ERMS, was absent or almost undetectable in ARMS. These findings were confirmed by semi-quantitative RT-PCR assay at the RNA level. Immunocytochemical analysis of RMS cell lines showed membrane and cytoplasmic ...
Introduction The majority of deaths from breast cancer are a total result of metastases; nevertheless, small is definitely recognized about the hereditary modifications root their starting point. had been scored by cell keeping track of, circulation cytometry, and scuff and Boyden Holding chamber assays. For in vivo tests, plakoglobin knockdown and control cells had been inoculated into mammary extra fat parts of rodents, and growth development, dropping of growth cells into the blood stream, and proof of metastatic bone tissue lesions had been supervised with caliper dimension, circulation cytometry, and microcomputed tomography (CT), respectively. Outcomes Plakoglobin and -catenin appearance had been decreased by even more than 80% in all knockdown Trifolirhizin supplier cell lines utilized but had been unaltered after transfection with the scrambled series. Decreased plakoglobin lead in considerably improved in MCF7 and Capital t47D cell expansion in vitro and in vivo, likened with control, ...
Astrid F. Nottebaum, Giuseppe Cagna, Mark Winderlich, Alexander C. Gamp, Ruth Linnepe, Christian Polaschegg, Kristina Filippova, Ruth Lyck, Britta Engelhardt, Olena Kamenyeva, Maria Gabriele Bixel, Stefan Butz, Dietmar Vestweber ...
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Cadherins are calcium-dependent, cell surface glycoproteins involved in cell-cell adhesion. To function in cell-cell adhesion, the transmembrane cadherin molecule must be associated with the cytoskeleton via cytoplasmic proteins known as catenins. Three catenins, alpha-catenin, beta-catenin, and gamma-catenin (also known as plakoglobin), have been identified. The domain of the cadherin molecule important for its interaction with the catenins has been mapped to the COOH-terminal 70 amino acids, but less is known about regions of the catenins that allow them to associate with one another or with the cadherin molecule. In this study we have transfected carboxyl-terminal deletions of plakoglobin into the human fibrosarcoma HT-1080 and used immunofluorescence localization and co-immunoprecipitation to map the regions of plakoglobin that allow it to associate with N-cadherin and with alpha-catenin. Plakoglobin is an armadillo family member containing 13 weakly similar internal repeats. These data show ...
Cadherins are calcium-dependent, cell surface glycoproteins involved in cell-cell adhesion. To function in cell-cell adhesion, the transmembrane cadherin molecule must be associated with the cytoskeleton via cytoplasmic proteins known as catenins. Three catenins, alpha-catenin, beta-catenin, and gamma-catenin (also known as plakoglobin), have been identified. The domain of the cadherin molecule important for its interaction with the catenins has been mapped to the COOH-terminal 70 amino acids, but less is known about regions of the catenins that allow them to associate with one another or with the cadherin molecule. In this study we have transfected carboxyl-terminal deletions of plakoglobin into the human fibrosarcoma HT-1080 and used immunofluorescence localization and co-immunoprecipitation to map the regions of plakoglobin that allow it to associate with N-cadherin and with alpha-catenin. Plakoglobin is an armadillo family member containing 13 weakly similar internal repeats. These data show ...
Cadherins are calcium-dependent, cell surface glycoproteins involved in cell-cell adhesion. To function in cell-cell adhesion, the transmembrane cadherin molecule must be associated with the cytoskeleton via cytoplasmic proteins known as catenins. Three catenins, alpha-catenin, beta-catenin, and gamma-catenin (also known as plakoglobin), have been identified. The domain of the cadherin molecule important for its interaction with the catenins has been mapped to the COOH-terminal 70 amino acids, but less is known about regions of the catenins that allow them to associate with one another or with the cadherin molecule. In this study we have transfected carboxyl-terminal deletions of plakoglobin into the human fibrosarcoma HT-1080 and used immunofluorescence localization and co-immunoprecipitation to map the regions of plakoglobin that allow it to associate with N-cadherin and with alpha-catenin. Plakoglobin is an armadillo family member containing 13 weakly similar internal repeats. These data show ...
The canonical Wnt signaling pathway plays key roles in stem-cell maintenance, progenitor cell expansion, and lineage decisions. Transcriptional responses induced by Wnt depend on the association of either beta-catenin or gamma-catenin with lymphoid enhancer factor/T cell factor transcription factors. Here we show that hematopoiesis, including thymopoiesis, is normal in the combined absence of beta- and gamma-catenin. Double-deficient hematopoietic stem cells maintain long-term repopulation capacity and multilineage differentiation potential. Unexpectedly, 2 independent ex vivo reporter gene assays show that Wnt signal transmission is maintained in double-deficient hematopoietic stem cells, thymocytes, or peripheral T cells. In contrast, Wnt signaling is strongly reduced in thymocytes lacking TCF-1 or in nonhematopoietic cells devoid of beta-catenin. These data provide the first evidence that hematopoietic cells can transduce canonical Wnt signals in the combined absence of beta- and gamma-catenin.
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Naxos disease (also known as Diffuse non-epidermolytic palmoplantar keratoderma with woolly hair and cardiomyopathy, Diffuse palmoplantar keratoderma with woolly hair and arrhythmogenic right ventricular cardiomyopathy firstly described in Naxos island by Dr Nikos Protonotarios, and Naxos disease) is a cutaneous condition characterized by a palmoplantar keratoderma. The prevalence of the syndrome is about 1 person in 1000 in the Hellenic islands. It has been associated with mutations in the genes encoding desmoplakin and plakoglobin. Olmsted syndrome List of cutaneous conditions List of conditions caused by problems with junctional proteins Rapini, Ronald P.; Bolognia, Jean L.; Jorizzo, Joseph L. (2007). Dermatology: 2-Volume Set. St. Louis: Mosby. ISBN 1-4160-2999-0. McKoy G, Protonotarios N, Crosby A, et al. (June 2000). Identification of a deletion in plakoglobin in arrhythmogenic right ventricular cardiomyopathy with palmoplantar keratoderma and woolly hair (Naxos disease). Lancet. ...
The cadherin-catenin complex is important for mediating homotypic, calcium-dependent cell-cell interactions in diverse tissue types. Although proteins of this complex have been identified, little is known about their interactions. Using a genetic assay in yeast and an in vitro protein-binding assay, we demonstrate that beta-catenin is the linker protein between E-cadherin and alpha-catenin and that E-cadherin does not bind directly to alpha-catenin. We show that a 25-amino acid sequence in the cytoplasmic domain of E-cadherin and the amino-terminal domain of alpha-catenin are independent binding sites for beta-catenin. In addition to beta-catenin and plakoglobin, another member of the armadillo family, p120 binds to E-cadherin. However, unlike beta-catenin, p120 does not bind alpha-catenin in vitro, although a complex of p120 and endogenous alpha-catenin could be immunoprecipitated from cell extracts. In vitro protein-binding assays using recombinant E-cadherin cytoplasmic domain and ...
The Sonic hedgehog (Shh) signaling pathway is critical for cell growth and differentiation. Impairment of this pathway can result in both birth defects and cancer. Despite its importance in cancer development, the Shh pathway has not been thoroughly investigated in tumorigenesis of brain tumors. In this study, we sought to understand the regulatory roles of GLI1, the immediate downstream activator of the Shh signaling pathway on its downstream target genes PTCH1, Cyclin D2, Plakoglobin, NKX2.2 and PAX6 in medulloblastoma and astrocytic tumors. We silenced GLI1 expression in medulloblastoma and astrocytic cell lines by transfection of siRNA against GLI1. Subsequently, we performed RT-PCR and quantitative real time RT-PCR (qRT-PCR) to assay the expression of downstream target genes PTCH1, Cyclin D2, Plakoglobin, NKX2.2 and PAX6. We also attempted to correlate the pattern of expression of GLI1 and its regulated genes in 14 cell lines and 41 primary medulloblastoma and astrocytoma tumor samples. We also
Synapses are fundamental building blocks of neural circuits. Synapse formation requires complex regulation involving cell adhesion molecules, secreted molecules, transcription factors and so forth. For cell adhesion molecules, ...
Free Online Library: Anaesthesia in Naxos disease: first case report.(Clinical report) by Bosnian Journal of Basic Medical Sciences; Biological sciences Anesthesia Case studies Methods Keratodermas Care and treatment
The α-catenin molecule links E-cadherin/ β-catenin or E-cadherin/plakoglobin complexes to the actin cytoskeleton. We studied several invasive human colon carcinoma cell lines lacking α-catenin. They showed a solitary and rounded morphotype that correlated with increased invasiveness. These round cell variants acquired a more normal epithelial phenotype upon transfection with an α-catenin expression plasmid, but also upon treatment with the protein kinase C (PKC) activator 12-O-tetradecanoyl-phorbol-13-acetate (TPA). Video registrations showed that the cells started to establish elaborated intercellular junctions within 30 min after addition of TPA. Interestingly, this normalizing TPA effect was not associated with α-catenin induction. Classical and confocal immunofluorescence showed only minor TPA-induced changes in E-cadherin staining. In contrast, desmosomal and tight junctional proteins were dramatically rearranged, with a conversion from cytoplasmic clusters to obvious concentration at ...
RDI-PRO10704 Cadherin E 6F9 1ml €350.00. RDI-PRO10028 Cadherin E 5H9 1ml €350.00. RDI-TRK5C5 Caldesmon 12B5 1mg €300.00. RDI- Calmodulin RDI- Calpain (u and m reactive antibodies). RDI- Calpastatin 200ul €350.00. RDI-Catenins Catenins (see specs for monoclonals against. alpha-catenin, beta-catenin and gamma-catenin/plakoglobin) RDI-CHYMOTabm Chymotrypsin CHYMOT 62 1mg €375.00. RDI-PRO61018 Complement C3a H13 50ug €300.00. RDI-PRO61019 Complement C3b-alpha H206 50ug €300.00. RDI-PRO61020 Complement C3b-beta H11 50ug €300.00. RDI-PRO61021 Complement C5 HCC 5.1 50ug €300.00. RDI-CBL192 Complement 5b neoepitope HC5b.1 50ug €300.00. RDI-TRK4C7- Corticoliberin 2 clones 1mg €300.00. RDI-TRK4C28- Cross Reactive Protein (CRP) 7 clones 1mg €300.00 each. RDI-CYCLIND- Cyclin D1, D2 & D3 antibodies 3+ clones & polyclonals. RDI-TRK3C13 Cyclosporine A CSZ.22 1mg €300.00. RDI-PRO65192 Desmocollin 1 DSC1-U100 5ml €300.00. RDI-PRO610120 Desmocollin 2 rabbit polyclonal 100ul ...
NKX3.1 and β-catenin expression variations might be related to macrophage infiltration in tissues consequent to inflammation.Tissues adjacent to the sections w
Levels of β-catenin and phospho-β-catenin (p-β-catenin), and their subcellular localization.In HB1.F3, β-catenin is mainly localized in nucleus (A), and p-
gamma-catenin Antibody (F-2) is a monoclonal anti-γ-catenin antibody that detects m, r, and h γ-catenin by WB, IP, IF and ELISA.
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β-Catenin is essential for embryonic development and required for cell renewal/regeneration in adult life. Cellular β-catenin exists in three different pools: membranous, cytoplasmic and nuclear. In...
TY - JOUR. T1 - No major role for rare plectin variants in arrhythmogenic right ventricular cardiomyopathy. AU - Hoorntje, Edgar T. AU - Posafalvi, Anna. AU - Syrris, Petros. AU - van der Velde, K Joeri. AU - Bolling, Marieke C. AU - Protonotarios, Alexandros. AU - Boven, Ludolf G. AU - Amat-Codina, Nuria. AU - Groeneweg, Judith A. AU - Wilde, Arthur A. AU - Sobreira, Nara. AU - Calkins, Hugh. AU - Hauer, Richard N W. AU - Jonkman, Marcel F. AU - McKenna, William J. AU - Elliott, Perry M. AU - Sinke, Richard J. AU - van den Berg, Maarten P. AU - Chelko, Stephen P. AU - James, Cynthia A. AU - van Tintelen, J Peter. AU - Judge, Daniel P. AU - Jongbloed, Jan D H. PY - 2018/8/30. Y1 - 2018/8/30. N2 - AIMS: Likely pathogenic/pathogenic variants in genes encoding desmosomal proteins play an important role in the pathophysiology of arrhythmogenic right ventricular cardiomyopathy (ARVC). However, for a substantial proportion of ARVC patients, the genetic substrate remains unknown. We hypothesized that ...
TY - JOUR. T1 - Abnormal expression and function of the E-cadherin-catenin complex in gastric carcinoma cell lines. AU - Jawhari, A. U.. AU - Noda, M.. AU - Farthing, M. J.G.. AU - Pignatelli, M.. PY - 1999/1/1. Y1 - 1999/1/1. N2 - Dysfunction of the cadherin-catenin complex, a key component of adherens junctions, is thought to confer invasive potential to cells. The aim of this study is to examine the expression and function of the E-cadherin/catenin complex in gastric carcinoma cell lines. Expression of E-cadherin, α, β and γ-catenin and p120(ctn), and of the adenomatous polyposis coil protein (APC), together with function of the cadherin-catenin complex was examined in a panel of gastric carcinoma cell lines, using immunocytochemistry, Western blotting and a cell-cell aggregation assay. Protein interactions were examined by sequential immunoprecipitation and immunoblotting with antibodies to E-cadherin, α, β and γ-catenin, p120(ctn) and APC. Abnormalities of E-cadherin, α- and ...
Arrhythmogenic right ventricular cardiomyopathy (ARVC) is an inherited heart muscle disease that may result in arrhythmia, heart failure, and sudden death. The hallmark pathological findings are progressive myocyte loss and fibrofatty replacement, with a predilection for the right ventricle. A number of genetic studies have identified mutations in various components of the cardiac desmosome that have important roles in the pathogenesis of ARVC. Disruption of desmosomal function by defective proteins might lead to death of myocytes under mechanical stress. The myocardial injury may be accompanied by inflammation. Since regeneration of cardiac myocytes is limited, repair by fibrofatty replacement occurs. Several studies have implicated that desmosome dysfunction results in the delocalization and nuclear translocation of plakoglobin. As a result, competition between plakoglobin and beta-catenin will lead to the inhibition of Wnt/beta-catenin signaling, resulting in a shift from a myocyte fate ...
ARVC or arrhythmogenic right ventricular cardiomyopathy is a rare illness. The occurrence of the same makes it impossible for an individual to recover completely.
Background: Mutations in plakoglobin (PG) gene have been identified in arrhythmogenic right ventricular cardiomyopathy (ARVC) patients. However, mechanisms underlying PG dysfunction involved in the pathogenesis of ARVC remain poorly understood. PG is a component of both desmosomes and adherens junctions located at intercalated disc (ICD) of cardiomyocytes where it functions to link cadherins to the cytoskeleton. In addition, PG is thought to function as a signaling protein via its ability to modulate Wnt signaling pathway.. Methods: We generated an inducible cardiac-restricted knockout (CKO) of the PG gene in mice, and performed a series of experiments to examine the role of PG in the heart, and compared with WT.. Results: The PG CKO mice exhibited progressive loss of cardiac myocytes, extensive inflammatory infiltration, fibrous tissue replacement and cardiac dysfunction similar to ARVC patients. Desmosomal proteins were decreased from the ICD consistent with the reduced number and length of ...
The catenins are polypeptides that bind to the conserved cytoplasmic tail of cadherins and are required for cadherin function. α-Catenin is related to vinculin and seems to be required for the interaction of cadherins with the actin cytoskeleton. β-Catenin is homologous to armadillo, a segment polarity gene in Drosophila that participates in developmental signaling. Recent findings indicate that β-catenin also participates in developmental signaling and embryonic patterning in Xenopus laevis. At least a portion of the electrophoretic band migrating at the position of γ-catenin consists of plakoglobin, a desmosomal and zonula adherens protein that has high sequence similarity to β-catenin and armadillo. The catenins may be involved in the regulation of cadherin function during tissue morphogenesis and tumorigenesis. ...
Canine Multifocal Retinopathy (CMR) Type 1 and Type 2 is an eye disorder that affects various breeds. Animal Genetics UK offers DNA testing for CMR1 and CMR2.
Hatzfeld, M., Green, K.J., and Sauter, H. (2003). Targeting of p0071 to desmosomes and adherens junctions is mediated by different protein domains. J Cell Sci 116, 1219-1233. 2002 Jaulin-Bastard, F., Arsanto, J.P., Le Bivic, A., Navarro, C., Vely, F., Saito, H., Marchetto, S., Hatzfeld, M., Santoni, M.J., Birnbaum, D., and Borg, J.P. (2002). Interaction between Erbin and a Catenin-related Protein in Epithelial Cells. J Biol Chem 277, 2869-2875. 2001 Bornslaeger, E.A., Godsel, L.M., Corcoran, C.M., Park, J.K., Hatzfeld, M., Kowalczyk, A.P., and Green, K.J. (2001). Plakophilin 1 interferes with plakoglobin binding to desmoplakin, yet together with plakoglobin promotes clustering of desmosomal plaque complexes at cell-cell borders. J Cell Sci 114, 727-738. 2000 Hatzfeld, M., C. Haffner, K. Schulze, and U. Vinzens. (2000). The function of plakophilin 1 in desmosome assembly and actin filament organization. J. Cell Biol. 149. 1999 Kowalczyk, A.P., Hatzfeld, M., Bornslaeger, E.A., Kopp, D.S., ...
Original kegg element: gene;3;hsa:10368 hsa:10369 hsa:27091 hsa:27092 hsa:55799 hsa:59283 hsa:59284 hsa:59285 hsa:775 hsa:776 hsa:778 hsa:779 hsa:781 hsa:782 hsa:783 hsa:784 hsa:785 hsa:786 hsa:9254 hsa: ...
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Generation of this architectural and functional diversity is a complex process comprising cell type-specific transcription and/or splicing of the components combined with selective transport of mRNAs and even site-specific translation. These events must be interconnected and regulated tightly, and several proteins are known that are involved in either one or several of these steps. A cross-talk between cytoskeletal components of adhesive junctions and gene transcription has been demonstrated for β-catenin (Ben Zeev and Geiger, 1998), actin (Scheer et al., 1984; Gonsior et al., 1999; Rando et al., 2000), zyxin (Nix and Beckerle, 1997), and the desmosomal plaque proteins plakophilin-1a and -1b (Schmidt et al., 1997), plakophilin-2 (Mertens et al., 2001), and plakophilin-3 (Bonne et al., 1999; Schmidt et al., 1999). Differential RNA splicing resulting in junctional diversity may be executed by protein components of the heterogeneous nuclear RNPs (hnRNPs)* like the polypyrimidine tract binding ...
TGF-β1 has been previously reported to promote tyrosine phosphorylation of β-catenin (Tian and Phillips, 2002), although the specific site of phosphorylation and its functional significance in TGF-β1 signaling has been unknown. Our finding of integrin-dependent tyrosine phosphorylation of Y654-β-catenin is important because phosphorylation of β-catenin at Y654 is known to promote both dissociation of β-catenin from E-cadherin and stabilization of β-catenin from ubiquitination and degradation (Brembeck et al., 2006). Therefore, independently of Wnt signaling, our findings indicate that TGF-β1 can promote a pathway of cross talk with β-catenin by generating stable pY654-β-catenin-Smad complexes. The data indicate that only a fraction of the β-catenin is phosphorylated, and presumably, this reflects, at least in part, the pool internalized with E-cadherin and TGF-βR1 after TGF-β1 stimulation. However, internalization alone does not appear to be sufficient, as α3-null cells, even ...
Arrhythmogenic Right Ventricular Cardiomyopathy (ARVC) is an inherited condition characterized by life threatening heart racing, presenting with palpitations, cardiac arrest (collapse requiring an ambulance) or sudden death. The disease affects the right ventricle, the part of the heart that pumps blood to the lungs. ARVC is diagnosed with a wide range of tests that focus on the pumping function and the electrical signals from the right ventricle. There are a number of methods used to diagnose ARVC: ECG, echocardiogram, Holter Monitoring, signal averaged ECG, stress testing, cardiac MRI, right ventricular angiography, electroanatomic mapping and rarely tissue biopsy. These tools can detect an abnormal electrical signal from the involved muscle tissue, or structural abnormalities. The variable presentation typically leads the physician to perform broad testing, since no single test is a gold standard for the diagnosis. Test results, and personal and family history are the basis of the ARVC Task ...
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Desmocollin 2小鼠多克隆抗体(ab72792)可与人样本反应并经WB实验严格验证,被1篇文献引用。所有产品均提供质保服务,中国75%以上现货。
14-3-3ζ has been found to associate with β-catenin (Tian et al., 2004). Later, it was found that Akt phosphorylates β-catenin at serine 552, which appears to enhance its interaction with 14-3-3ζ (Fang et al., 2007). In both cases, ectopic expression of 14-3-3ζ resulted in a moderate activation (two- to fourfold) of β-catenin-dependent transcription in TopFlash assays. We found that 14-3-3ζ enhances, whereas 14-3-3η and ε isoforms repress, β-catenin activation of the TopFlash reporter (Fig. 5 A). One possible explanation for this observation is that 14-3-3 overexpression exerts complex biological effects, which makes our interpretation of the TopFlash results difficult. In fact, 14-3-3 proteins have been shown to interact with a plethora of target proteins ranging from transcription factors to various signaling molecules (Dougherty and Morrison, 2004; Pozuelo Rubio et al., 2004). However, it is interesting to note that, consistent with our results (Fig. 7 C), ectopic expression of ...
Polyclonal antibody for ALPHA 1 CATENIN/CTNNA1 detection. Host: Rabbit.Size: 100μg/vial. Tested applications: IHC-P. Reactive species: Human. ALPHA 1 CATENIN/CTNNA1 information: Molecular Weight: 100071 MW; Subcellular Localization: Isoform 1: Cytoplasm,
Mutations in the Wnt/-catenin pathway occur in most colorectal cancers (CRCs), and these mutations lead to increased nuclear accumulation of the -catenin transcriptional co-activator. element within the first intron of the gene to drive expression in CRC cells. As such, reducing -catenin expression in CRC cells using shRNAs leads to decreased mRNA and protein levels. …Read More. ...
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