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Several of the SNF and SWI genes of Saccharomyces cerevisiae encode proteins that are involved in the regulation of transcriptional activation. One of these proteins, SNF2/SWI2, has both . The human Brm protein has been reported to be a 180 kDa nuclear factor that acts as a transcriptional activator when fused to a heterologus DNA binding domain. Transfected Brm, expressed in cells lacking endogenous protein, can cooperate with the glucocorticoid receptor (GR) in transcriptional activation. The cooperation between Brm and GR requires the DNA binding domain of GR and the helicase domain and the P/Q-charged domain of Brm. However, Brm does not affect on several other transcription factors. The retinoblastoma protein, Rb, stimulates the transcription of a number of genes. Like Brm, Rb up-regulates glucocorticoid-receptor-mediated transcription. Brm and Rb interact in vitro and in vivo , requiring the Rb-pocket domain and the consensus Rb-binding motif of Brm. This antibody is routinely tested by western blot analysis. Other applications were tested at BD Biosciences Pharmingen during antibody development only or reported in the literature.
