goat polyclonal IgG; also available as rabbit IgG, 200 µg/ml, sc-20209-R
epitope corresponding to phosphorylated Thr 490 of B-Myb of mouse origin
recommended for detection of Thr 490 phosphorylated B-Myb of mouse, rat and human origin by WB, IP and IF; also reactive with additional species, including equine, canine, bovine, porcine and avian
B-Myb Background Information A member of the myb proto-oncogene family, B-Myb is a cell cycle-regulated transcription factor that is essential for the transition from G1 to S phase. This nuclear protein becomes phosphorylated at the onset of S phase by the cyclin A/Cdk2 complex. Ten phosphorylation sites have been identified and all sites were on either serine or threonine residues that were followed by a proline residue, suggesting that phosphorylation is due to a proline-directed kinase. Transactivation properties of B-Myb are apparently dependent upon the protein’s hyperphosphorylation. Several phosphorylation sites, including threonine 447, threonine 490, threonine 497 and serine 581, are located near the protein’s C-terminus. Phosphorylation of these C-terminal residues plays a critical role in enhancing the transcriptional activity of B-Myb. Poly(ADP-ribose) polymerase (PARP), which has a role in cellular proliferation, binds to B-Myb and thus enhances B-Myb transactivation. PARP is a B-Myb co-factor and promotes phosphorylation of B-Myb by the Cyclin/Cdk2 complex.
