Cell Signaling Technology

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BCL9 Antibody #15096

BCL-9   BCL9   Lymphoma   sc-79868  

No. Size Price
15096S 100 µl ( 10 western blots ) ¥3,100.00 现货查询 购买询价
15096 carrier free & custom formulation / quantityemail request
Applications Dilution Species-Reactivity Sensitivity MW (kDa) Isotype
W 1:1000 Human, Endogenous 149 Rabbit

Species cross-reactivity is determined by western blot.

Applications Key: W=Western Blotting,

Homology

Species predicted to react based on 100% sequence homology: Bovine, Horse,

Specificity / Sensitivity

BCL9 Antibody recognizes endogenous levels of total BCL9 protein. The antibody also cross-reacts with an unidentified protein of 21 kDa in some cell lines.

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.

Western Blotting

Western Blotting

Western blot analysis of extracts from various cell lines using BCL9 Antibody. KARPAS cell Line source: Dr Abraham Karpas at the University of Cambridge.

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).

  1. Townsley, F.M. et al. (2004) Nat Cell Biol 6, 626-33.
  2. de la Roche, M. et al. (2008) BMC Cancer 8, 199.
  3. Katoh, M. and Katoh, M. (2007) Clin Cancer Res 13, 4042-5.
  4. Takada, K. et al. (2012) Sci Transl Med 4, 148ra117.
  5. Fiedler, M. et al. (2008) Mol Cell 30, 507-18.
  6. Deka, J. et al. (2010) Cancer Res 70, 6619-28.
  7. Sampietro, J. et al. (2006) Mol Cell 24, 293-300.

Application References

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Protocols

Companion Products


For Research Use Only. Not For Use In Diagnostic Procedures.

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