SI0603P: K6-Linked Tri-Ubiquitin (Phosphorylated)

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K6-linked ubiquitination is traditionally associated with mitophagy and also a main contributor to the DNA damage 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. K6 Tri-Ubiquitin (phosphorylated) is a trimeric chain of wild-type ubiquitin, wherein ubiquitin monomers are enzymatically linked together via an isopeptide bond between Lysine 6 and the C-terminal Glycine. The chains are then enzymatically phosphorylated at the Ser65 position.


Species Human
Source E. coli
Tag None
Molecular Weight 25766-25926 Da (depending on degree of phosphorylation)
Quantity Variable
Concentration Variable
Formulation 20 mM Tris pH 7.5, 150 mM NaCl
Storage -80°C, avoid freeze/thaw cycles

Additional information



100 µg


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  • Investigation of phosphoubiquitin chain specificity and selectivity
  • Studies on the role of phosphoubiquitin chains in protein degradation pathways (e.g., proteasomal and autophagic degradation)
  • Analysis of phosphoubiquitin-mediated signaling pathways and cellular responses
  • Structural studies to elucidate the architecture and dynamics of phosphoubiquitin chains
  • Screening assays to identify modulators of phosphoubiquitin chain assembly and disassembly processes