Purification and Quality Control The Flag-tag recombinant protein is purified by affinity chromatography in combination with FPLC columns. The purified MAD is greater than 90% homogeneous based on SDS-PAGE analysis.
Unit Definition (Activity) 1 unit equals 1 nanogram of purified protein.
Applications MAD 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 MAX dimerization protein belongs to a subfamily of MAX-interacting proteins. This protein competes with MYC for binding to MAX to form a sequence-specific DNA-binding complex, acting as a transcriptional repressor (while MYC appears to function as an activator) and is a candidate tumor suppressor. Both Myc and Mad, as well as the more recently described Mnt and Mga proteins, form heterodimers with Max, permitting binding to specific DNA sequences. These DNA-bound heterodimers recruit coactivator or corepressor complexes that generate alterations in chromatin structure, which in turn modulate transcription (1). The wild-type c-Myc and c-Myc/MadBR proteins have indistinguishable biological activity and target gene recognition in vivo (2).
References: 1. Grandori,C., et al. Annu. Rev. Cell Dev. Biol. 16, 653-699 (2000) 2. Nikiforov,M.A., et al. J. Biol. Chem. 278 (13), 11094-11099 (2003)
DISCLAIMER
This products is recommended For RESEARCH USE ONLY and is Not qualified for Use in Diagnostic or Therapeutic Procedures.
