SI1104BP: Biotinylated K11-Linked Tetra-Ubiquitin (Phosphorylated)

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K11-linked ubiquitination is traditionally associated with cell cycle regulation and proteasomal degradation. Phospho-ubiquitin chains represent a specialized class of polyubiquitin characterized by phosphorylation at Serine 65 and play a central role in mitophagy signaling pathways. K11 linkage appears to play an important role in cell cycle signaling, as it is associated with the anaphase promoting complex (APC).

K11 Tetra-Ubiquitin (phosphorylated) is a tetrameric chain of wild-type ubiquitin, wherein ubiquitin monomers are enzymatically linked together via an isopeptide bond between Lysine 11 and the C-terminal Glycine. The chains are then enzymatically phosphorylated at the Ser65 position. These phosphorylated tetra ubiquitin are then biotinylated on an available cysteine that was mutated in one of the ubiquitins to allow for one biotin molecule to be attached.



Species Human
Source E. coli
Tag None
Molecular Weight 34842-35466 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


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  • Biotinylated chains are meant to label the protein so they can be selectively separated via a multitude of methods such as Western Blotting, pull downs (see website), ELISAs, etc.
  • Can use streptavidin or avidin to visualize this protein specifically.
  • 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