SI4804B: Biotinylated K48-Linked Tetra-Ubiquitin

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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. K48 Tetra-Ubiquitin is a tetrameric chain of wild-type ubiquitin, wherein ubiquitin monomers are enzymatically linked together via an isopeptide bond between Lysine 48 and the C-terminal Glycine. Once the K48 Tetra Ubiquitin has been formed and phosphorylated it is then biotinylated 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.


Species Human
Source E. coli
Tag Biotin
Molecular Weight 35207 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 ubiquitin chain specificity and selectivity
• Studies on the role of ubiquitin chains in protein degradation pathways (e.g., proteasomal and autophagic degradation)
• Analysis of ubiquitin-mediated signaling pathways and cellular responses
• Structural studies to elucidate the architecture and dynamics of ubiquitin chains
• Screening assays to identify modulators of ubiquitin chain assembly and disassembly processes