SI4804BP: Biotinylated K48-Linked Tetra-Ubiquitin (Phosphorylated)

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Specifications

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).

Info
Species Human
Source E. coli
Tag Biotin
Molecular Weight 34842-35082 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

Size

100 µg

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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