β-Tubulin (Ser-172), Phosphospecific Antibody

Microtubules (MTs) are cytoskeletal elements that play an essential role in cell division and cytoplasmic organization. MTs are dynamic polymers of α/β-tubulin heterodimers. At least two populations of MTs, called dynamic and stable according to their rates of turnover, are readily distinguishable in cells. The proteins associated with MTs (MAPs) are among the best-known factors that regulate MT dynamics and stability. In addition, a variety of different post-translational modifications may also regulate MT dynamics and stability. Phosphorylation is one of these modifications and it can occur on serine, threonine, and tyrosine residues in β-Tubulin isoforms. Multiple kinases can phosphorylate Ser-444 at the C-terminus of βIII-Tubulin in vitro. Unphosphorylated Ser-444 in βIII-Tubulin is an early marker for cells of neuronal lineage, while phosphorylation of Ser-444 is upregulated after neuronal maturation and may preferentially occur in assembled MTs. By contrast, Cdk1 phosphorylation of Ser-172 in β-Tubulin occurs in mitotic cells and may impair tubulin incorporation into microtubules.

This antibody was cross-adsorbed to unphosphorylated βIII-Tubulin (Ser-172) peptide before affinity purification using phospho-βIII-Tubulin (Ser-172) peptide (without carrier) . The antibody detects a 50 kDa* protein corresponding to the molecular mass of β-Tubulin on SDS-PAGE immunoblots of purified brain tubulin phosphorylated with ERK2 kinase. This sequence is identical to similar regions in βI, βII, and βIII-Tubulin isotypes, and is well conserved in tubulins from most eukaryotic species.