Biotinylated K48-Linked Tetra-Ubiquitin (Phosphorylated)

K48 chains traditionally play a role in proteasomal degradation pathways. These polymeric chains of ubiquitin molecules play critical roles in regulating protein stability, localization, and activity. K48 chains traditionally play a role in proteasomal degradation pathways and have a central role in mitophagy signaling pathways. K48 linkage remains a critical pathway for the cells to maintain homeostasis through proteolytic degradation, and as such remains very intriguing for the study of DUBs that play a role in the degradation, as well as the proteasome itself. Phospho-ubiquitin chains represent a specialized class of polyubiquitin characterized by phosphorylation at Serine 65 and play a central role in mitophagy signaling pathways. K48 Tetra-Ubiquitin (phosphorylated) is a tetrameric chain of wild-type ubiquitin, wherein ubiquitin monomers are linked together via an isopeptide bond between Lysine 48 and the C-terminal Glycine. The chains are then enzymatically phosphorylated at the Ser65 position. Once the K48 Tetra Ubiquitin has been formed and phosphorylated we then biotinylate it once on one available 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).