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SI1104B: Biotinylated K11-Linked Tetra-Ubiquitin

LifeSensors SI1104B is biotinylated K11-linked tetra-ubiquitin, ideal for studying ubiquitin signaling, protein degradation, and cellular regulation in biochemical research.

$0.00

• 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

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-linked ubiquitination is traditionally associated with cell cycle regulation and proteasomal degradation. 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 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. These 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. Info
Species Human
Source E. coli
Tag Biotin
Molecular Weight 34759 Da
Quantity Variable
Concentration Variable
Formulation 20 mM Tris pH 7.5, 150 mM NaCl
Storage -80°C, avoid freeze/thaw cycles

• 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

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