BCL9 Antibody #15096
- WB
Supporting Data
| REACTIVITY | H |
| SENSITIVITY | Endogenous |
| MW (kDa) | 149 |
| SOURCE | Rabbit |
Application Key:
- WB-Western Blotting
Species Cross-Reactivity Key:
- H-Human
Product Information
Product Usage Information
| Application | Dilution |
|---|---|
| Western Blotting | 1:1000 |
Storage
Protocol
Specificity / Sensitivity
Species Reactivity:
The antigen sequence used to produce this antibody shares 100% sequence homology with the species listed here, but reactivity has not been tested or confirmed to work by CST. Use of this product with these species is not covered under our Product Performance Guarantee.
Species predicted to react based on 100% sequence homology:
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding His138 of human BCL9 protein. Antibodies are purified by protein A and peptide affinity chromatography.
Background
B-cell CLL/lymphoma 9 protein (BCL9) is a widely conserved adaptor protein that functions as a transcriptional co-activator in the canonical Wnt signaling pathway (1,2). BCL9 is a core component of a nuclear protein complex (BCL9, LEF/TCF, β-catenin and PYGO) that regulates the transcription of Wnt-dependent target genes (3). Research studies show that disrupting the interaction between BCL9 and β-catenin suppresses oncogenic Wnt signaling, suggesting a potential avenue for therapeutic intervention in Wnt-mediated cancers (4). BCL9 promotes association of PYGO with the tail of histone H3 that has been methylated at lysine 4 (H3K4me), suggesting a specific chromatin remodeling function for BCL9 in the Wnt signaling pathway (5). Research studies in colon epithelium and adenocarcinomas suggest that BCL9 is required to mediate Wnt-dependent stem cell behaviors, such as epithelial-mesenchymal transition (6). Crystallography studies revealed that BCL9 contains a β-catenin binding site that is distinct from the majority of known β-catenin binding partners, making it an attractive target for therapeutic drug development (7).
- Townsley, F.M. et al. (2004) Nat Cell Biol 6, 626-33.
- de la Roche, M. et al. (2008) BMC Cancer 8, 199.
- Katoh, M. and Katoh, M. (2007) Clin Cancer Res 13, 4042-5.
- Takada, K. et al. (2012) Sci Transl Med 4, 148ra117.
- Fiedler, M. et al. (2008) Mol Cell 30, 507-18.
- Deka, J. et al. (2010) Cancer Res 70, 6619-28.
- Sampietro, J. et al. (2006) Mol Cell 24, 293-300.
Limited Uses
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