Andersson et al. Nature Communications 2017 describe the validation of thirteen commercial and academic antibodies raised against estrogen receptor beta (ERbeta).
The present antibody worked in the IHC validation step (1:1500 dilution) since it discriminated between ERbeta positive cells and ERbeta negative cells. However, it recognized fewer ERbeta positive cells compared to the best performing antibody (PPZ0506) of the study. Further, it detected ERbeta in a wide range of clinical tissue sections that did not express ERbeta mRNA.
In Western blotting, it recognized a faint band for recombinant ERbeta and a band in ERbeta positive cells, however, band of similar and other sizes was observed also in ERbeta-negative cells. In IP, the antibody showed greater affinity and reproducibility for a different protein, POU2F1, than for ERbeta.
On August 4, 2017 Cecilia Williams, KTH Royal Institute of Technology, Sweden wrote:
Andersson et al. Nature Communications 2017 describe the validation of thirteen commercial and academic antibodies raised against estrogen receptor beta (ERbeta).
The present antibody worked in the IHC validation step (1:1500 dilution) since it discriminated between ERbeta positive cells and ERbeta negative cells. However, it recognized fewer ERbeta positive cells compared to the best performing antibody (PPZ0506) of the study. Further, it detected ERbeta in a wide range of clinical tissue sections that did not express ERbeta mRNA.
In Western blotting, it recognized a faint band for recombinant ERbeta and a band in ERbeta positive cells, however, band of similar and other sizes was observed also in ERbeta-negative cells. In IP, the antibody showed greater affinity and reproducibility for a different protein, POU2F1, than for ERbeta.
See data figure and link to full article above.