mouse monoclonal IgG2a; c-Myc Antibody (C-8) is an IgG2a κ mouse monoclonal c-Myc antibody (also designated c-Myc antibody or Myc antibody) that detects c-Myc p67 and c-Myc tagged fusion proteins of mouse, rat and human origin by WB, IP, IF and ELISA. c-Myc Antibody (C-8) is available as the non-conjugated anti-c-Myc antibody form, as well as multiple conjugated forms of anti-c-Myc antibody, including agarose, HRP, PE, FITC and multiple Alexa Fluor® conjugates. c-Myc-, N-Myc- and L-Myc-encoded proteins function in cell proliferation, differentiation and neoplastic disease. Amplification of the c-Myc gene has been found in several types of human tumors including lung, breast and colon carcinomas. The presence of three sequence motifs in the c-Myc COOH terminus, including the leucine zipper, the helix-loop-helix and a basic region, provided initial evidence for a sequence-specific binding function. A basic region helix-loop-helix leucine zipper motif (bHLH-Zip) protein, designated Max, specifically associates with c-Myc, N-Myc and L-Myc proteins. The Myc-Max complex binds to DNA in a sequence-specific manner under conditions where neither Max nor Myc exhibits appreciable binding. Max can also form heterodimers with at least two additional bHLH-Zip proteins, Mad 1 and Mxi1, and Mad 1-Max dimers have been shown to repress transcription through interaction with mSin3.