mouse monoclonal IgG2a; GAL4 Antibody (DBD) is an IgG2a κ mouse monoclonal GAL4 antibody (also designated GAL4 DNA binding domain antibody, GAL4 DBD Upstream Activation Sequence system antibody, GAL4 UAS system antibody, or yeast GAL4 DBD antibody) that detects the GAL4 protein. GAL4 Antibody (DBD) is available as both the non-conjugated anti-GAL4 antibody form, as well as multiple conjugated forms of anti-GAL4 antibody, including agarose, HRP, PE, FITC and multiple Alexa Fluor® conjugates. 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.