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Catenin alpha 1/2 Antibody

Purified Rabbit Polyclonal Antibody (Pab)

     
  • WB - Catenin alpha 1/2 Antibody AP51125
    All lanes : Anti-Catenin alpha 1/2 Antibody at 1:1000 dilution Lane 1: Hela whole cell lysates Lane 2: SH-SY5Y whole cell lysates Lysates/proteins at 20 µg per lane. Secondary Goat Anti-Rabbit IgG, (H+L),Peroxidase conjugated at 1/10000 dilution Predicted band size : 100 kDa Blocking/Dilution buffer: 5% NFDM/TBST.
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Product Information
Application
  • Applications Legend:
  • WB=Western Blot
  • IHC=Immunohistochemistry
  • IHC-P=Immunohistochemistry (Paraffin-embedded Sections)
  • IHC-F=Immunohistochemistry (Frozen Sections)
  • IF=Immunofluorescence
  • FC=Flow Cytopmetry
  • IC=Immunochemistry
  • ICC=Immunocytochemistry
  • E=ELISA
  • IP=Immunoprecipitation
  • DB=Dot Blot
  • CHIP=Chromatin Immunoprecipitation
  • FA=Fluorescence Assay
  • IEM=Immunoelectronmicroscopy
  • EIA=Enzyme Immunoassay
WB
Primary Accession P35221
Reactivity Human, Mouse, Rat
Host Rabbit
Clonality Polyclonal
Calculated MW 102 KDa
Antigen Region 841 - 900 aa
Additional Information
Gene ID 1495
Other Names Catenin alpha-1, Alpha E-catenin, Cadherin-associated protein, Renal carcinoma antigen NY-REN-13, CTNNA1
Target/Specificity KLH conjugated synthetic peptide derived from human Catenin alpha 1/2
Dilution WB~~ 1:1000
Format 0.01M PBS, pH 7.2, 0.09% (W/V) Sodium azide, Glycerol 50%
StorageStore at -20 °C.Stable for 12 months from date of receipt
Protein Information
Name CTNNA1
Function 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. Involved in the regulation of WWTR1/TAZ, YAP1 and TGFB1- dependent SMAD2 and SMAD3 nuclear accumulation (By similarity). May play a crucial role in cell differentiation.
Cellular Location [Isoform 1]: Cytoplasm, cytoskeleton. Cell junction, adherens junction. Cell membrane; Peripheral membrane protein; Cytoplasmic side. Cell junction. Note=Found at cell-cell boundaries and probably at cell-matrix boundaries
Tissue Location Expressed ubiquitously in normal tissues.
Research Areas
Citations (0)
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Background

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.

References

Furukawa Y.,et al.Cytogenet. Cell Genet. 65:74-78(1994).
Oda T.,et al.Biochem. Biophys. Res. Commun. 193:897-904(1993).
Rimm D.L.,et al.Biochem. Biophys. Res. Commun. 203:1691-1699(1994).
Kask M.,et al.Biochem. Biophys. Res. Commun. 411:56-61(2011).
Nollet F.H.,et al.Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.

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$ 350.00
Cat# AP51125
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