Anti-Ubiquitin (Autophagy Marker) Monoclonal Antibody (Clone: UBB/1748)

Ubiquitin is a highly conserved and plays an essential role in the ubiquitin-proteasome pathway. In ubiquitination process, it is first activated by forming a thiol-ester complex with the activation component E1, which is then transferred to ubiquitin-carrier protein E2, followed by to ubiquitin ligase E3 for final delivery to epsilon-NH2 of the target protein lysine residue. IkB, p53, cdc25A, Bcl-2 etc. are shown as targets of ubiquitin-proteasome process as part of regulation of cell cycle progression, differentiation, cell stress response, and apoptosis. Moreover, ubiquitin have been reported to bind covalently with pathological inclusions which are resistant to degradation e.g. neurofibrillary tangles/paired helical filaments in Alzheimer's disease, Lewy bodies seen in Parkinson's disease, and Pick bodies found in Pick's disease etc. Protein function: Accepts ubiquitin from the E1 complex and catalyzes its covalent attachment to other proteins. In vitro catalyzes 'Lys-48'- linked polyubiquitination. Mediates the selective degradation of short- lived and abnormal proteins. Functions in the E6/E6-AP-induced ubiquitination of p53/TP53. Mediates ubiquitination of PEX5 and autoubiquitination of STUB1 and TRAF6. Involved in the signal-induced conjugation and subsequent degradation of NFKBIA, FBXW2-mediated GCM1 ubiquitination and degradation, MDM2-dependent degradation of p53/TP53 and the activation of MAVS in the mitochondria by DDX58/RIG-I in response to viral infection. Essential for viral activation of IRF3. [The UniProt Consortium]