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Anti-α1-Catenin (Tyr-148), Phosphospecific Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
| Primary Accession | P35221 |
|---|---|
| Reactivity | Bovine, Chicken |
| Host | Rabbit |
| Clonality | Rabbit Polyclonal |
| Isotype | IgG |
| Calculated MW | 100071 Da |
| Gene ID | 1495 |
|---|---|
| Other Names | alphaE-catenin, catenin alpha1, catenin |
| Target/Specificity | α-catenins are cadherin interacting proteins with homology to vinculin. Three α-catenin genes have been described including α1-catenin (αE-Catenin), α2-catenin (αN-catenin), and α3-catenin (αT-catenin). α1-catenin has 81% homology with α2-catenin and 60% homology with α3-catenin. These α-catenin isoforms may have similar roles since each binds cadherins. However, their expression patterns are both overlapping and distinct. α1-catenin was identified in epithelial cells, and is expressed in various cell types. α2-catenin is enriched in the nervous system, and α3-catenin is expressed highest in testis and heart. Phosphorylation may regulate the activity of α1-catenin, since tyrosine phosphorylation of Tyr-148 occurs during intercellular adhesion. This site is dephosphorylated by SHP2, which inhibits α1-catenin binding to β-catenin and translocation to the plasma membrane. Phosphorylation of α1-catenin at Tyr-148 may be important for inhibition of cell transformation, and dephosphorylation of this site may be important during SHP2-mediated cell transformation. |
| Format | Antigen Affinity Purified |
| Storage | Maintain refrigerated at 2-8°C for up to 6 months. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
| Precautions | Anti-α1-Catenin (Tyr-148), Phosphospecific Antibody is for research use only and not for use in diagnostic or therapeutic procedures. |
| Shipping | Blue Ice |
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Background
α-catenins are cadherin interacting proteins with homology to vinculin. Three α-catenin genes have been described including α1-catenin (αE-Catenin), α2-catenin (αN-catenin), and α3-catenin (αT-catenin). α1-catenin has 81% homology with α2-catenin and 60% homology with α3-catenin. These α-catenin isoforms may have similar roles since each binds cadherins. However, their expression patterns are both overlapping and distinct. α1-catenin was identified in epithelial cells, and is expressed in various cell types. α2-catenin is enriched in the nervous system, and α3-catenin is expressed highest in testis and heart. Phosphorylation may regulate the activity of α1-catenin, since tyrosine phosphorylation of Tyr-148 occurs during intercellular adhesion. This site is dephosphorylated by SHP2, which inhibits α1-catenin binding to β-catenin and translocation to the plasma membrane. Phosphorylation of α1-catenin at Tyr-148 may be important for inhibition of cell transformation, and dephosphorylation of this site may be important during SHP2-mediated cell transformation.
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