| 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. |
| Synonym | MXD1; MAD1; MGC104659. |
| Protein Sequence | MAAAVRMNIQ MLLEAADYLE RREREAEHGY ASMLPYNNKD RDALKRRNKS KKNNSSSRST
HNEMEKNRRA HLRLCLEKLK GLVPLGPESS RHTTLSLLTK AKLHIKKLED CDRKAVHQID
QLQREQRHLK RQLEKLGIER IRMDSIGSTV SSERSDSDRE EIDVDVESTD YLTGDLDWSS
SSVSDSDERG SMQSLGSDEG YSSTSIKRIK LQDSHKACLG L |
| 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) |
