Technical Data
C2069-40J
Catenin alpha1 (alpha-1 Catenin, CTNNA1, Catenin (Cadherin-associated Protein) alpha 1 102kDa, Catenin alpha, alpha-Catenin, alpha-E-Catenin, alphaE-Catenin, CAP102, FLJ36832, FLJ52416, HGNC:2509, NY-REN-13 Antigen, Renal Carcinoma Antigen NY-REN-13)
Description:
Alpha-catenin belongs together with beta and gamma-catenin to the catenin family. Catenins comprise a large family of Ca2+-dependent, homotypic cell-cell adhesion molecules that play important roles in development, epithelial cell polarity and tumor progression. Cadherins are single pass, type I transmembrane proteins that are localized in the adherens junction. To be fully functional, the cadherin cytoplasmic domain must be linked to the actin cytoskeleton through a group of proteins termed catenins: alpha-catenin, beta-catenin and plakoglobin. Alpha catenin interacts with the cadherin indirectly via interactions with beta-catenin or plakoglobin.

Applications:
Suitable for use in Immunofluorescence, Western Blot and Immunoprecipitation. Other applications not tested.

Recommended Dilution:
Immunofluorescence: 1:10
Western Blot: 1:10
Optimal dilutions to be determined by the researcher.

Storage and Stability:
May be stored at 4C for short-term only. Aliquot to avoid repeated freezing and thawing. Store at -20C. Aliquots are stable for at least 12 months. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap.
TypeIsotypeCloneGrade
MabIgG11G5Affinity Purified
SizeStorageShippingSourceHost
100ug-20CBlue IceHumanMouse
Concentration:
~0.1mg/ml
Immunogen:
Human alpha-catenin.
Purity:
Purified by Protein G affinity chromatography.
Form
Supplied as a liquid in PBS, 0.1% BSA, 0.02% sodium azide.
Specificity:
Recognizes human alpha-catenin.
Intended for research use only. Not for use in human, therapeutic, or diagnostic applications.
1. Nieman, M et al; Mechanism of extracellular domain-deleted dominant negative cadherins. J. Cell Science 1999, 112: 1621 2) Johnson, K et al; P- and E-cadherin are in separate complexes in cells expressing both cadherins. Exp Cell Res 1993, 207: 252.