K33-Linked Di-Ubiquitin (Phosphorylated)

K33-linked ubiquitination is traditionally associated with regulation of the innate immune response. These chain types are also involved in protein stabilization and other non-degradative processes. Phospho-ubiquitin chains represent a specialized class of polyubiquitin characterized by phosphorylation at Serine 65 and play a central role in mitophagy signaling pathways. K33 Di-Ubiquitin (phosphorylated) is a dimeric chain of wild-type ubiquitin, wherein ubiquitin monomers are enzymatically linked together via an isopeptide bond between Lysine 33 and the C-terminal Glycine. The chains are then enzymatically phosphorylated at the Ser65 position.