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Anti-Ubiquitin [ZTA10-90-6]

Info

Applications IP WB
Antigen/Gene or Protein Targets Ubiquitin
Reactivity All
Relevance Ubiquitin is a small regulatory protein that affects proteins through a process called ubiquitination. Ubiquitin can signal for protein degradation via the proteasome, alter their cellular location, affect their activity, and promote or prevent protein interactions. Ubiquitination is carried out in three main steps: activation, conjugation, and ligation, performed by ubiquitin-activating enzymes (E1s), ubiquitin-conjugating enzymes (E2s), and ubiquitin ligases (E3s), respectively. The result of this sequential cascade binds ubiquitin to the protein substrate. When covalently bound, ubiquitin is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin) or a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked. Inappropriate ubiquitin-mediated protein degradation has been implicated in a number of diseases, especially neurodegenerative disorders that involve protein aggregation and inclusion body formation, such as Alzheimer’s disease, Parkinson’s disease, Huntington’s disease and amyotrophic lateral sclerosis (ALS), where protein misfolding may play a role.
Host Mouse
Subclass IgG1 kappa
Myeloma Used Sp2/0
Research Area Epigenetics & Nuclear Signalling, Neurobiology, Protein Degradation

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