SRP5171
Catenin α, GST tagged human
recombinant, expressed in baculovirus infected Sf9 cells, ≥70% (SDS-PAGE), buffered aqueous glycerol solution
Sinonimo/i:
CAP102, CTNNA1, FLJ36832
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About This Item
Prodotti consigliati
Origine biologica
human
Ricombinante
expressed in baculovirus infected Sf9 cells
Saggio
≥70% (SDS-PAGE)
Stato
buffered aqueous glycerol solution
PM
~123 kDa
N° accesso NCBI
applicazioni
cell analysis
Condizioni di spedizione
dry ice
Temperatura di conservazione
−70°C
Informazioni sul gene
human ... CTNNA1(1495)
Descrizione generale
Catenin α is a novel actin-binding and -bundling protein. Catenin α is responsible for organizing and tethering actin filaments at the zones of E-cadherin-mediated cell-cell contact. Monomeric Catenin α can bind strongly to E-Cadherin-β-Catenin, whereas the dimer preferentially binds actin filaments. Different molecular conformations are associated with these different binding states, indicating that Catenin α is an allosteric protein. Catenin α directly regulates actin-filament organization by suppressing Arp2/3-mediated actin polymerization, likely by competing with the Arp2/3 complex for binding to actin filaments
Stato fisico
Supplied in 50mM Tris-HCl, pH 7.5, 150mM NaCl, 10mM glutathione, 0.1mM EDTA, 0.25mM DTT, 0.1mM PMSF, 25% glycerol.
Nota sulla preparazione
after opening, aliquot into smaller quantities and store at -70 °C. Avoid repeating handling and multiple freeze/thaw cycles
Codice della classe di stoccaggio
10 - Combustible liquids
Classe di pericolosità dell'acqua (WGK)
WGK 1
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Frauke Drees et al.
Cell, 123(5), 903-915 (2005-12-06)
Epithelial cell-cell junctions, organized by adhesion proteins and the underlying actin cytoskeleton, are considered to be stable structures maintaining the structural integrity of tissues. Contrary to the idea that alpha-catenin links the adhesion protein E-cadherin through beta-catenin to the actin
D L Rimm et al.
Proceedings of the National Academy of Sciences of the United States of America, 92(19), 8813-8817 (1995-09-12)
Calcium-dependent homotypic cell-cell adhesion, mediated by molecules such as E-cadherin, guides the establishment of classical epithelial cell polarity and contributes to the control of migration, growth, and differentiation. These actions involve additional proteins, including alpha- and beta-catenin (or plakoglobin) and
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