B42 Background Information The GAL4 protein of Saccharomyces cerevisiae is one of the most thoroughly characterized transcriptional activators. Since the N-terminal 147 amino acid residues of GAL4 are sufficient to mediate specific and strong binding to DNA, but are incapable of efficient transcriptional activation, this protein fragment has frequently been used to confer specific DNA binding in experiments examining transcriptional activation functions of heterologous proteins. This approach is facilitated by the finding that higher eukaryotes lack endogenous proteins that enhance transcription from the consensus GAL4-binding site. Fusions between GAL4 (aa 1-147) and activating domains from a variety of transcriptional regulatory proteins can activate transcription in yeast, plant, insects and mammalian cells. A unique “two-hybrid” system has been developed using GAL4 fusions in yeast to identify specific protein-protein interactions. Another “two-hybrid” system has been developed using the DNA binding domain (DBD) of the E.Coli protein Lex A and the transcriptional activation domain (TAD) of the bacterially-derived B42 protein.
B42 (Q-19) Product Citations
See how others have used B42 (Q-19): sc-8606 antibody and or B42 (Q-19) antibody conjugates.
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B42 (Q-19)
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Western blot analysis of full-length B42 fusion protein, sc-4269 WB (A,B). Antibodies tested include B42 (Q-19): sc-8606 (A) and B42 (C-20): sc-8607 (B).