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. Author manuscript; available in PMC: 2019 Aug 16.
Published in final edited form as: Mol Cell. 2018 Aug 2;71(4):554–566.e7. doi: 10.1016/j.molcel.2018.06.040

Figure 2.

Figure 2.

In-solution binding of ERG to BAF complexes in prostate cancer.

(A) Immunoprecipitation using anti-ERG (mouse monoclonal) and anti-BRG1 antibodies (left); IP with an alternate anti-ERG (rabbit polyclonal) antibody (right), in VCaP cell nuclear extracts.

(B) Immunoprecipitation using IgG and anti-ERG antibodies, with or without ethidium bromide (EtBr) treatment (left). Immunoprecipitation using IgG and anti-ERG antibodies with or without treatment of benzonase, presence of plasmid DNA indicated for benzonase treatment control (right).

(C) Immunodepletion studies performed on VCaP cell nuclear extracts using an anti-BRG1 antibody.

(D) Urea denaturation analysis performed on anti-ERG IPs from VCaP nuclear extracts treated with [urea]= 0–2.5M.

(E) Nuclear protein input and anti-ERG IP on nuclear extracts from LNCaP cells in empty and ERG conditions.

(F) Input (left) and anti-V5 IP (right) in HEK-293-T cells transfected with V5-ETV1, V5-ETV4, V5-ETV5 or empty vector.