Anti-MLX / Max-like protein X, clone PCRP-MLX-1G8

0.2 mg/ml in 1X PBS with 0.1 mg/ml BSA (US sourced), 0.05% sodium azide. Max is a nuclear localized bHLH-Zip protein that forms homodimers or heterodimers with Myc family members, including Myc, Mad1, Mad3, Mad4, Mxi1 and Mnt (or Rox). These dimers bind to the E-box sequence CACGTG in order to regulate cell growth, proliferation and apoptosis. Mlx (Max-like protein X) is a bHLH-Zip protein that is structurally and functionally related to Max. Like Max, Mlx is broadly expressed in many tissues and has a long half-life. Mlx also forms homodimers or heterodimers with members of the Myc family, specifically Mad1, Mad4 and Rox, and members of the Mondo family, to repress or activate transcription from CACGTG E-boxes. MondoA forms weak homodimers and preferentially forms heterodimers with Mlx. The MondoA/Mlx complex is primarily localized to the cytoplasm, but will translocate to the nucleus in response to leptomycin B. Mlx can also dimerize with WBSCR14, a protein involved in Williams-Beuren syndrome (WBS), to repress E-box transcription, which provides further evidence that Mlx is a critical element in a transcription factor network. Protein function: Transcription regulator. Forms a sequence-specific DNA- binding protein complex with MAD1, MAD4, MNT, WBSCR14 and MLXIP which recognizes the core sequence 5'-CACGTG-3'. The TCFL4-MAD1, TCFL4-MAD4, TCFL4-WBSCR14 complexes are transcriptional repressors. Plays a role in transcriptional activation of glycolytic target genes. Involved in glucose-responsive gene regulation. [The UniProt Consortium]