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Product Includes Quantity Applications Reactivity MW(kDa) Isotype
α-E-Catenin (23B2) Rabbit mAb 3240 40 µl
Western Blotting Immunoprecipitation
H M Mk 100 Rabbit IgG
β-Catenin (D10A8) XP® Rabbit mAb 8480 40 µl
Western Blotting Immunoprecipitation Immunohistochemistry Immunofluorescence Flow Cytometry Chromatin Immunoprecipitation
H M R Mk 92 Rabbit IgG
γ-Catenin Antibody 2309 40 µl
Western Blotting Immunoprecipitation Immunohistochemistry Immunofluorescence
H M R Hm Mk 83 Rabbit 
Catenin δ-1 Antibody 4989 40 µl
Western Blotting Flow Cytometry
H M R 100 Rabbit 
Afadin (D1Y3Z) Rabbit mAb 13531 40 µl
Western Blotting Immunoprecipitation
H M R Mk Dg 205 Rabbit IgG
Anti-rabbit IgG, HRP-linked Antibody 7074 100 µl
Western Blotting
All Goat 

Product Description

The Adherens Junction Antibody Sampler Kit provides an economical means of detecting the protein components of adherens junctions. The kit includes enough antibody to perform four western blot experiments per primary antibody.


Specificity / Sensitivity

Each antibody in this kit detects endogenous levels of total protein for the specified target and does not cross-react with other family members unless indicated. The α-E-Catenin (23B2) Rabbit mAb may cross-react with neuronal α-N-catenin. The γ-Catenin Antibody does not cross-react with β-catenin. Based on sequence homology, the Afadin (D1Y3Z) Rabbit mAb is expected to recognize all isoforms of afadin.


Source / Purification

Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to the carboxy terminus of human γ-catenin protein, or the sequence of human catenin δ-1 protein. Polyclonal antibodies are purified by protein A and peptide affinity chromatography. Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to the amino-terminal sequence of human α-E-catenin, Arg1117 of human afadin protein, or to residues surrounding Pro714 of human β-catenin protein.

Adherens junctions are dynamic structures that form cell-cell contacts and are important in development, differentiation, tissue integrity, morphology and cell polarity. They are composed of the transmembrane proteins, cadherins, which bind cadherins on adjacent cells in a calcium-dependent manner. On the cytoplasmic side of adherens junctions, the classic model states that cadherins are linked to the cytoskeleton through β- and α-catenin. α-E-catenin is ubiquitously expressed, α-N-catenin is expressed in neuronal tissue, and α-T-catenin is primarily expressed in heart tissue. Research studies have demonstrated that loss of E-cadherin and α-E-catenin occurs during the progression of several human cancers, indicating that the breakdown of adherens junctions is important in cancer progression (reviewed in 1).

Research studies also suggest that, rather than acting as a static link between cadherins and actin, α-catenin regulates actin dynamics directly, possibly by competing with the actin nucleating arp2/3 complex (2,3). α-catenin also plays a role in regulating β-catenin-dependent transcriptional activity, affecting differentiation and response to Wnt signaling. α-catenin binds to β-catenin in the nucleus, preventing it from regulating transcription, and levels of both proteins appear to be regulated via proteasome-dependent degradation (4).


Afadin has two splice variants: l-afadin, which is ubiquitously expressed, and s-afadin, which is expressed predominantly in neural tissue. s-afadin is a shorter form lacking one of the three proline-rich regions found in l-afadin, as well as the carboxyl-terminal F-actin binding region (5). Human s-afadin is identical to AF-6, the ALL-1 fusion partner involved in acute myeloid leukemias (6). Recent research has also shown that afadin is involved in controlling the directionality of cell movement when it is localized at the leading edge of moving cells (7,8).


1.  Kobielak, A. and Fuchs, E. (2004) Nat Rev Mol Cell Biol 5, 614-25.

2.  Yamada, S. et al. (2005) Cell 123, 889-901.

3.  Drees, F. et al. (2005) Cell 123, 903-15.

4.  Hwang, S.G. et al. (2005) J Biol Chem 280, 12758-65.

5.  Mandai, K. et al. (1997) J Cell Biol 139, 517-28.

6.  Prasad, R. et al. (1993) Cancer Res 53, 5624-8.

7.  Miyata, M. et al. (2009) J Cell Sci 122, 4319-29.

8.  Miyata, M. et al. (2009) J Biol Chem 284, 24595-609.


Entrez-Gene Id 4301, 1495, 1499, 1500, 3728
Swiss-Prot Acc. P55196, P35221, P35222, O60716, P14923


For Research Use Only. Not For Use In Diagnostic Procedures.
Cell Signaling Technology® is a trademark of Cell Signaling Technology, Inc.
XP® is a trademark of Cell Signaling Technology, Inc.
U.S. Patent No. 5,675,063.