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Human Polyclonal CTNNA1 Primary Antibody für WB - ABIN4948305
Yamada, Pokutta, Drees, Weis, Nelson: Deconstructing the cadherin-catenin-actin complex. in Cell 2005
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Polyclonal CTNNA1 Primary Antibody für WB - ABIN4948297
Drees, Pokutta, Yamada, Nelson, Weis: Alpha-catenin is a molecular switch that binds E-cadherin-beta-catenin and regulates actin-filament assembly. in Cell 2005
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Human Polyclonal CTNNA1 Primary Antibody für IHC (fro), IHC (p) - ABIN3043818
Lin, Wu, Li, Wu, Zheng: Prognostic and clinicopathological features of E-cadherin, alpha-catenin, beta-catenin, gamma-catenin and cyclin D1 expression in human esophageal squamous cell carcinoma. in World journal of gastroenterology 2005
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Human Polyclonal CTNNA1 Primary Antibody für FACS - ABIN5693090
Ren, Qiu, Lü, Ru, Li, Xiang, Yu, Zhang: TALENs-directed knockout of the full-length transcription factor Nrf1α that represses malignant behaviour of human hepatocellular carcinoma (HepG2) cells. in Scientific reports 2017
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Human Monoclonal CTNNA1 Primary Antibody für FACS, IF - ABIN2191997
Nieman, Kim, Johnson, Wheelock: Mechanism of extracellular domain-deleted dominant negative cadherins. in Journal of cell science 1999
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Dog (Canine) Polyclonal CTNNA1 Primary Antibody für ELISA, WB - ABIN547674
Lynch, Grady, Suriano, Huntsman: Gastric cancer: new genetic developments. in Journal of surgical oncology 2005
loss of AJs in alpha-catenin-knockout (KO) EpH4 epithelial cells altered the lipid composition of the plasma membrane (PM) and led to endocytosis of claudins, a major component of Tight junctions (TJs). Sphingomyelin with long-chain fatty acids and cholesterol were enriched in the TJ-containing PM fraction. Depletion of cholesterol abolished the formation of TJs.
The combination of CTNB1, XPO2, and CAPG achieved 95% sensitivity and 96% specificity for the discrimination of these subtypes. We developed two uterine aspirate-based signatures to diagnose Endometrial cancer and classify tumors in the most prevalent histologic subtypes. This will improve diagnosis and assist in the prediction of the optimal surgical treatment
These findings provide mechanistic insight into the WNT-mediated regulation of the DNA damage response and suggest a novel role for the alpha-catenin-beta-catenin complex in the nucleus.
pseudogene CTNNAP1 is a potential tumor suppressor participating in CRC pathogenesis by competing with the parent gene CTNNA1 for microRNA-141.
Hypermethylation of the CTNNA1 promoter was associated with unfavorable karyotype, and possessed the higher frequency of coexisting with ASXL1 and RUNX1 mutations.
The results of this study demonstrate that causative variants identified in the CTNNA1 and CYP4V2 genes are also associated with Leber Congenital Amaurosis.
alpha- and beta-catenins may be important in the early stages of phyllodes tumours development, while E-cadherin may be required for malignant development
This work identified alpha-catenin as another molecule in addition to E- and P-cadherin that were targeted to inactivate homotypic cell-in-cell structures formation in human tumor cells.
Progressive loss of e-cadherin/alpha-catenin expression is associated with an aggressive phenotype (low differentiation, increased metastatic activity/advanced stage) in thyroid carcinomas.
study identifies CTNNA1 gene variants as a cause of macular dystrophy, indicates that CTNNA1 is involved in maintaining RPE integrity
The results demonstrate a Fas-mediated apoptotic signaling pathway that is enhanced by the age-dependent loss of alpha(E)-catenin in renal tubule epithelial cells.
Actin-dependent CTNNA1 clustering is a unique molecular mechanism mediating both integrity and reassembly of the cell-cell adhesive interface formed through weak cis- and trans-intercadherin interactions.
alpha-catenin is a reversible, stretch-activatable sensor that mechanically links cadherin complexes and actin and is an indispensable player in cadherin-specific mechanotransduction at intercellular junctions.
alpha-catenin functions as a tumor suppressor in E-cadherin-negative basal like breast cancer cells by inhibiting NF-kappaB signaling.
CTNNA1 hypermethylation was detected in three out of four with isolated del(5q), one with trisomy 11, one with monosomy 7, one out of four with del(20q), and one out of seven with complex abnormalities, but in none with trisomy 8.
CTNNA1 methylation is a recurrent event but has no influence on prognosis in acute myeloid leukemia
CTNNA1 expression is specifically downregulated in basal-like breast cancer subtype, correlates with clinical outcome and inversely correlates with TNF and RELB expression.
A germline truncating allele of alpha-E-catenin (CTNNA1) was identified that was present in two family members with invasive diffuse gastric cancer and four in which intramucosal signet ring cells were detected as part of endoscopic surveillance.
A discrete trimeric complex of beta-catenin, alpha-catenin and the tumor suppressor APC, forms in the cytoplasm in response to Wnt signaling.
Data show that E-cadherin and alpha-catenin were predominantly expressed in the cell membranes, whereas beta- and gamma-catenin were found both in the cell membrane and cytoplasm.
alphaE-catenin knockout caused heart failure, the upregulation of hypertrophic genes, and the dysregulation of fatty acid metabolism via the transcriptional activity of Yap and beta-catenin.
alphaE-catenin is essential for inhibiting nuclear YAP localization and cell proliferation. This function of alphaE-catenin is required for formation of the tooth signalling centre, the enamel knot (EK), which maintains dental mesenchymal condensation and epithelial invagination. alphaE-catenin restricts YAP/TAZ activity to establish a group of non-dividing and specialized cells that constitute a signalling centre.
Catna1 functions as a positive regulator of pancreatic islet cell lineage differentiation by repressing the sonic hedgehog pathway.
alpha-catenins regulate intercalated disc maturation and actomyosin contractility, which, in turn, control Yap subcellular localization, thus providing an explanation for the loss of proliferative capacity in the newborn mammalian heart.
In this study, the authors revealed how alpha-catenin retains its activated state while avoiding unfolding under tension.
cadherin 2 (CDH2) and CDH4 cooperate to regulate radial migration in mouse brain via the protein tyrosine phosphatase 1B (PTP1B) and alpha- and beta-catenins.
alphaT-catenin is a constitutively active actin-binding protein that can physically couple the cadherin.catenin complex to F-actin in the absence of tension.
Two Dtna interactors, alpha-catulin (phosphorylation independent) and Grb2 (phosphorylation dependent) are localized to neuromuscular junctions in vivo, and are required for proper organization of neurotransmitter receptors on myotubes.
alphaE-catenin inhibits beta4 integrin-mediated activation of SRC tyrosine kinase
E-cadherin/alphaE-catenin chimeras used previously do not mimic alphaE-catenin in the native CCC, and imply that both CCC-bound monomer and cytosolic homodimer alphaE-catenin are required for strong cell-cell adhesion.
Loss of alpha-catenin elicits a cholestatic response and impairs liver regeneration
alphaE-catenin binding to filamentous actin favors assembly of unbranched filament bundles that are protected from severing over more dynamic, branched filament arrays.
Fusing VE-cadherin to alpha-catenin presents a mutation, which leads to embryonic lethality, due to a lack of fetal liver hematopoiesis and severe lymphedema but no detectable defects in blood vessel formation and remodeling.
alphaE-catenin recruits vinculin to adherens junctions more effectively than alphaN-catenin, partly because of its higher affinity for actin filaments.
our results show that alpha-catenin-mediated cell adhesion and cell organization are important for the fissure closure in mice, and further suggest that genes that regulate cell adhesion may underlie certain coloboma cases in humans
alpha-Catenin and vinculin cooperate to promote high E-cadherin-based adhesion strength
alpha-catenin, previously implicated in tumor suppression and cell density sensing in the skin, is an upstream negative regulator of Yap1; alpha-catenin controls Yap1 activity and phosphorylation by modulating its interaction with 14-3-3 and PP2A phosphatase.
Data show that alphaE-catenin D3 binds strongly to vinculin, whereas larger fragments and full-length alphaE-catenin bind approximately 1,000-fold more weakly.
An E-cadherin-alpha-catenin fusion protein (Ealpha) restored full cell-adhesion function and organized the actin-based cytoskeleton and ZO-1, an actin filament binding protein, in F9 cells lacking all endogenous cadherin-catenin complex components.
An evolutionarily conserved PTEN-C/EBPalpha-CTNNA1 axis controls myeloid development and transformation.
alpha-Catenin controls actomyosin dynamics by stabilising and promoting the formation of actomyosin foci, and also stabilises DE-Cadherin (Drosophila E-Cadherin, also known as Shotgun) at the cell membrane, suggesting that medioapical actomyosin contractility regulates junction stability.
Increased Rap1 activity restricts epithelial invagination in an alpha-catenin-dependent manner.
alpha-Cat mutant phenotype can be rescued by the expression of a DE-cadherin::alpha-Catenin fusion protein, which argues against an essential cytosolic, cadherin-independent role of Drosophila alpha-Catenin
alpha-catenin and p120(ctn) are key players in a mechanism of recruiting Rho1 to its sites of action.
Depletion of alphaE-catenin caused a defect in radial intercalation that was associated with decreased cell-cell adhesion, in a similar manner to E-cadherin depletion. Depletion of alphaE-catenin also caused deep cells to have plasma membrane blebbing.
These data suggest that the interactions of beta-catenin with alpha-catenin and GSK-3beta exert opposing effects on the terminal projections of ventral optic axons.
Associates with the cytoplasmic domain of a variety of cadherins. The association of catenins to cadherins produces a complex which is linked to the actin filament network, and which seems to be of primary importance for cadherins cell-adhesion properties. Can associate with both E- and N-cadherins. Originally believed to be a stable component of E-cadherin/catenin adhesion complexes and to mediate the linkage of cadherins to the actin cytoskeleton at adherens junctions. In contrast, cortical actin was found to be much more dynamic than E-cadherin/catenin complexes and CTNNA1 was shown not to bind to F-actin when assembled in the complex suggesting a different linkage between actin and adherens junctions components. The homodimeric form may regulate actin filament assembly and inhibit actin branching by competing with the Arp2/3 complex for binding to actin filaments. May play a crucial role in cell differentiation.
, cadherin-associated protein,102kDa
, catenin alpha-1
, renal carcinoma antigen NY-REN-13
, 102 kDa cadherin-associated protein
, alpha E catenin
, cadherin associated protein
, catenin alpha 1
, catenin (cadherin associated protein), alpha 1
, catenin, alpha 1
, alpha catenin
, catenin alpha 1 subunit
, catenin (cadherin-associated protein), alpha 1, 102kDa
, catenin alpha-1-like
, catenin alpha 1 S homeolog
, LOW QUALITY PROTEIN: catenin alpha-1