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CTNNA1 Antibody (Internal)

Goat Polyclonal Antibody

     
  • IHC - CTNNA1 Antibody (Internal) ALS13431
    Anti-CTNNA1 antibody IHC of human prostate.
    detail
  • IHC - CTNNA1 Antibody (Internal) ALS13431
    Anti-CTNNA1 antibody IHC of human uterus.
    detail
  • SPECIFICATION
  • CITATIONS
  • PROTOCOLS
  • BACKGROUND
  • detail
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, IHC-P, E
Primary Accession P35221
Reactivity Human, Mouse, Rat, Rabbit, Hamster, Monkey, Chicken, Horse, Xenopus, Bovine, Dog
Host Goat
Clonality Polyclonal
Calculated MW 100kDa
Dilution ELISA (1:32000), IHC-P (3.75 µg/ml), WB (1-3 µg/ml)
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 Human CTNNA1.
Reconstitution & Storage Store at -20°C. Minimize freezing and thawing.
PrecautionsCTNNA1 Antibody (Internal) is for research use only and not for use in diagnostic or therapeutic procedures.
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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Discontinued
Cat# ALS13431
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