Biotinylated K63-Linked Tetra-Ubiquitin (Phosphorylated)

K63 chains traditionally play a role in intracellular signaling, trafficking, and autophagy. The topology of this linkage and its apparent role in cellular processes are quite different from that of K48. Poly-Ub chains of this type appear to play a role in endocytic trafficking, DNA repair, neurodegeneration and more. Phospho-ubiquitin chains represent a specialized class of polyubiquitin characterized by phosphorylation at Serine 65 and play a central role in mitophagy signaling pathways. K63 Tetra-Ubiquitin (phosphorylated) is a tetrameric chain of wild-type ubiquitin, wherein ubiquitin monomers are linked together via an isopeptide bond between Lysine 63 and the C-terminal Glycine. This linkage takes place onto other ubiquitin monomers and are then enzymatically linked from specific UPS enzymes. The chains are then enzymatically phosphorylated at the Ser65 position. After phosphorylation, we then biotinylate it once on one available cysteine site on the ubiquitin chain. This biotin then acts as a means of detection via streptavidin or vidin. The applications are numerous from Western Blots to ELISAs. Testing can vary based off of intended application (EX: DUB activity/specificity).