Technical Data
C2069-43D
Catenin alpha1 (CTNNA1, Catenin (Cadherin-associated Protein), alpha 1, 102kDa, HGNC:2509, CAP102, FLJ36832, alpha 1 (102kD), alpha-E-Catenin, alpha-Catenin, alphaE-Catenin)
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:
Can be used for Western Blot, Immunoprecipitation and Immunofluorescence.

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

Storage and Stability:
May be stored at 4C for short-term only. For long-term storage and to avoid repeated freezing and thawing, aliquot and add glycerol (40-50%). Store at -20C or colder. Aliquots are stable for at least 12 months at -20C. 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.
TypeIsotypeCloneGrade
MabIgG16A489Affinity Purified
SizeStorageShippingSourceHost
100ug-20CBlue IceHumanMouse
Concentration:
~0.1mg/ml
Immunogen:
alpha-catenin, bacterial fusion protein
Purity:
Purified by Protein G affinity chromatography.
Form
Supplied as a liquid in PBS, containing 0.02% sodium azide and 0.1% BSA.
Specificity:
Reacts with 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.