||Recombinant human MAD was expressed in anE. colisystem and purified by an affinity column in combination with FPLC chromatography. 24 kDa.
||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. The wild-type c-Myc and c-Myc/MADBR proteins have indistinguishable biological activity and target gene recognition in vivo .
||MAD can be applied to DNA binding, proliferation, differentiation, and apoptosis research studies.
||1 unit equals 1 nanogram of purified protein.
||The purified protein is greater than 95% homogeneous based on SDS-PAGE gel analysis.
||1x dilution buffer A: 20 mM Tris-Cl (pH 8.0), 20% Glycerol, 100 mM KCl, 0.2 mM EDTA and 1mM DTT.
||Store at -80°C.