p-Thr Background Information
Protein kinases catalyze the phosphorylation of serine, threonine or tyrosine residues in target substrates, providing a mechanism of control for myriad cellular signaling pathways. Threonine phosphorylation plays a role in the activation of ERK and JNK MAP kinases, which are dually phosphorylated on tyrosine and threonine residues by MEK family kinases (1,2). Several families of kinases phosphorylate both serine and threonine residues in target substrates, including the Raf, Rsk, ROCK, PAK, Ak, and PKC families of protein kinases (3–8). Antibodies to phosphothreonine may be used for the characterization of proteins with phosphorylated threonine residues, and for the elucidation of cellular pathways involving threonine phosphorylation.
