Purification and Quality Control The Flag-tag recombinant protein is purified by affinity chromatography in combination with FPLC columns. The purified MAX is greater than 90% homogeneous based on SDS-PAGE analysis.
Unit Definition (Activity) 1 unit equals 1 nanogram of purified protein.
Applications MAX can be applied to DNA binding, proliferation, differentiation, and apoptosis research studies.
Formulation and Storage The protein is in 20mM Tris-HCl pH7.9,100mM NaCl, 0.2mM EDTA, 1mM DTT and 20% glycerol. Stored at -70°C before use. Avoid repeated freeze thaw cycles.
Background The MAX gene encodes a protein that interacts specifically with the Myc protein to form a heterodimer with high affinity for the specific cognate DNA-binding site of Myc. The protein encoded by this gene is a member of the basic helix-loop-helix leucine zipper (bHLHZ) family of transcription factors. It is able to form homodimers and heterodimers with other family members, which include MAD, MXI1 and Myc (1). 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 provides a complex system of transcriptional regulation. Substantial evidence has been accumulated over the last years that support the model that Myc/MAX/MAD proteins affect different aspects of cell behavior, including proliferation, differentiation, and apoptosis, by modulating distinct target genes. The unbalanced expression of these genes, e.g. in response to deregulated Myc expression, is most likely an important aspect of Myc`s ability to stimulate tumor formation (2). It is reported that In vivo transactivation assays suggest that Myc-MAX and MAD-MAX complexes have opposing functions in transcription and that MAX plays a central role in this network of transcription factors (3). High levels of MAX and stress-induced NFkappaB activation may result in elevated expression of Fas ligand in human lung cancer cells and possibly contribute to Fas ligand-associated immune escape mechanisms (4).
