		Technical Data
C2096-59	Catenin, beta

Description:
b-Catenin (~92kD) shares 70% amino acid identity with both plakoglobin (g-catenin) and the product of the Drosophila segment polarity gene armadillo. b-catenin, plakoglobin (g-catenin), and p120 cas are homologous but distinct proteins which contain between 10-13 copies of a 42-44 amino acid motif rst identi ed in the armadillo protein and referred to as armadillo repeats. These armadillo repeats mediate b-catenin’s interaction with the tumor suppressor protein APC (Adenomatous Polyposis Coli).

Applications:
Suitable for use in Immunohistochemistry. Other applications not tested.

Recommended Dilution:
Immunohistochemistry: Frozen and formalin-fixed, paraffin embedded tissue sections. Epitope retrieval required.
Optimal dilutions to be determined by the researcher.

Recommended Positive Control Tissue:
Non-neural epithelial tissue

Expected Staining Pattern: Membrane and cytoplasmic
Epitope Retrieval: Required
Enzyme Digestion: Not required

Storage and Stability:
May be stored at 4°C for short-term only. For long-term storage, aliquot and store at -20°C. Aliquots are stable for at least 12 months at -20°C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.

Type	Isotype	Clone	Grade
Mab	IgG1,k	3G67	Purified

Size		Storage	Shipping	Source	Host
1ml		-20°C	Blue Ice	Chicken	Mouse

Concentration:

~0.25mg/ml

Immunogen:

Recombinant protein corresponding to the C-terminus of chicken b-catenin.

Purity:

Puri ed from mouse ascites

Form

Supplied as a liquid in PBS, pH 7.4, 1% BSA, 0.1% sodium azide.

Specificity:

Recognizes chicken b-catenin (~92kD) and does not crossreact with the related plakoglobin (~83kD) protein. Species Crossreactivity: human, mouse.

Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.

1. Knudsen, K.A., et al; J. Cell. Biol. 18:671–679 (1992). 2. McCrea, P.D., et al; J. Biol. Chem. 266:4514–4520 (1991). 3. McCrea, P.D., et al; Science 25:1359–1361 (1991). 4. Peifer, M., et al; Cell 63:1167–1178 (1990). 5. Daniel, J.M., et al; Mol. Cell. Biol. 270:4819–4824 (1995). 6. Peifer, M., et al; Cell 76:789–791 (1994). 7. Rubinfeld, B., et al; Science 262:1731–1734 (1993). 8. Su, L.-K., et al; Science 262:1734–1737 (1993). 9. Peifer, M., et al; Science 262:1667–1668 (1993). 10. Sparks, A.B. et al. Cancer Research. 58:1130–1134, (1998). 11. Rubinfeld, B. et al. Science. 275:1790–1792, (1997).. 12. Geiger, B., et al; Curr. Opin. Cell Biol. 1:103–109 (1989). 13. Takeichi, M., et al. Science 51:1451–1455, (1991). 14. Johnson, K.R., et al; Exp. Cell Res. 207:252–260 (1993). 15. Hinck, L, et al; J. Cell. Biol. 125:1327–1340 (1994). 16. Ozawa, M., et al; Proc. Natl Acad. Sci. USA. 87:4246–4250 (1990). 17. Knudsen, K.A., et al; J. Biol. Chem. 130:67–77 (1995). 18. Croons A.H. et al. 1941. Proceed. Soc. Experim. Med. 47: 200–202. 19. Nakane P.K. and Pierce G.B. J. Histo. Cyto. 22:1084–1091, (1966). 20. Sternberger L.A. Mikroskopie 25:346–361, (1969). 21. Sternberger L.A. J. Histochem. Cytochem. 18:315–333, (1970). 22. Hsu S.M. J. Histochem. Cytochem. 29:577–580, (1981). 23. Elias J.M. Am. J. Clin. Path. 92:62–67, (1989). 24. Shi Z.R. et al. J Histochem Cytochem 36(3):317–322, (1988).