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Anti-γ-Catenin (Tyr-550), Phosphospecific Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB |
|---|---|
| Primary Accession | P14923 |
| Reactivity | Bovine |
| Host | Rabbit |
| Clonality | Rabbit Polyclonal |
| Isotype | IgG |
| Calculated MW | 81745 Da |
| Gene ID | 3728 |
|---|---|
| Other Names | Plakoglobin, JUP, Desmoplakin III, Desmoplakin-3, catenin gamma1 |
| Target/Specificity | Plakoglobin (γ-Catenin) is a catenin family member identified as a component of desmosomes. γ-Catenin has high homology to β-catenin and, like β-catenin, it can associate with the cadherins, E-cadherin and N-cadherin. One molecule of α-catenin and at least one molecule of β-catenin and γ-Catenin simultaneously bind to a single cadherin molecule. A 19-amino acid sequence of desmoglein was found to be critical for binding of γ-Catenin. Similar catenin-binding domains found in cadherins, suggest a common mechanism for γ-Catenin localization to both adherens junctions and desmosomes. Phosphorylation of tyrosine residues in γ-Catenin can modify its interactions with other proteins. Phosphorylation of tyrosine 644 decreases γ-Catenin association with α-catenin, but increases binding to desmoplakin. Fer kinase can phosphorylate tyrosine 550, which increases γ-Catenin binding to α-catenin. Thus, tyrosine phosphorylation may be important for regulation of γ-Catenin protein-protein interactions within desmosomal complexes. |
| 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-γ-Catenin (Tyr-550), Phosphospecific Antibody is for research use only and not for use in diagnostic or therapeutic procedures. |
| Shipping | Blue Ice |
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Provided below are standard protocols that you may find useful for product applications.
Background
Plakoglobin (γ-Catenin) is a catenin family member identified as a component of desmosomes. γ-Catenin has high homology to β-catenin and, like β-catenin, it can associate with the cadherins, E-cadherin and N-cadherin. One molecule of α-catenin and at least one molecule of β-catenin and γ-Catenin simultaneously bind to a single cadherin molecule. A 19-amino acid sequence of desmoglein was found to be critical for binding of γ-Catenin. Similar catenin-binding domains found in cadherins, suggest a common mechanism for γ-Catenin localization to both adherens junctions and desmosomes. Phosphorylation of tyrosine residues in γ-Catenin can modify its interactions with other proteins. Phosphorylation of tyrosine 644 decreases γ-Catenin association with α-catenin, but increases binding to desmoplakin. Fer kinase can phosphorylate tyrosine 550, which increases γ-Catenin binding to α-catenin. Thus, tyrosine phosphorylation may be important for regulation of γ-Catenin protein-protein interactions within desmosomal complexes.
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