Application Note
*Optimal dilutions/concentrations should be determined by the researcher.
Application |
Recommended Dilution |
1:500-1:10000 |
1:100-1:1000 |
Assay dependent |
Not tested in other applications.
Calculated MW
Positive Control
Mouse brain , rat brain
Predict Reactivity
Zebrafish, Rabbit, Bovine, Xenopus laevis, Rhesus Monkey(>80% identity)
Form
Liquid
Buffer
PBS, 20% Glycerol
Preservative
0.025% ProClin 300
Storage
Store as concentrated solution. Centrifuge briefly prior to opening vial. For short-term storage (1-2 weeks), store at 4ºC. For long-term storage, aliquot and store at -20ºC or below. Avoid multiple freeze-thaw cycles.
Concentration
1.11 mg/ml (Please refer to the vial label for the specific concentration.)
Antigen Species
Human
Immunogen
Recombinant protein encompassing a sequence within the center region of human alpha 1 Catenin. The exact sequence is proprietary.
Purification
Purified by antigen-affinity chromatography.
Conjugation
Unconjugated
RRID
AB_1950059
Note
For laboratory research use only. Not for any clinical, therapeutic, or diagnostic use in humans or animals. Not for animal or human consumption.
Purchasers shall not, and agree not to enable third parties to, analyze, copy, reverse engineer or otherwise attempt to determine the structure or sequence of the product.
Synonyms
catenin alpha 1 , CAP102 , MDPT2
Cellular Localization
Cytoplasm , cytoskeleton , Cell junction , adherens junction , Cell membrane
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 adherence 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.
Database
Research Area