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SI3303P: K33-Linked Tri-Ubiquitin (Phosphorylated)

$695.00

  • 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
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 Tri-Ubiquitin (phosphorylated) is a trimeric 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. Info
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
 
  • 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

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