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Overview
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MAX Human Recombinant produced in E. Coli is a single, non-glycosylated, polypeptide chain containing 168 amino acids (1-160 a.a.) and having a molecular mass of 19.3kDa. MAX protein is fused to an 8 amino acid His-Tag at C-terminus and purified by standard chromatography. MAX protein is part of the basic helix-loop-helix leucine zipper (bHLHZ) family of transcription factors. MAX forms homodimers and heterodimers with Mad, Mxi1 and Myc. Myc is an oncoprotein implicated in cell proliferation, differentiation and apoptosis. The homodimers and heterodimers compete for a common DNA target site (the E box) and rearrangement among these dimer forms offers a complex system of transcriptional regulation. In contrast to Myc, which is exceedingly regulated throughout progression during the cell cycle, Max is very stable and is much more abundant than Myc.
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- Properties
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Overview