Anti-Ubiquitin, clone rUBB/9476

0.2 mg/ml in 1X PBS with 0.1 mg/ml BSA (US sourced), 0.05% sodium azide. 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: [Ubiquitin]: Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair, Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell- cycle regulation, Lys-29-linked is involved in proteotoxic stress response and cell cycle, Lys-33-linked is involved in kinase modification, Lys-48-linked is involved in protein degradation via the proteasome, Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling. [The UniProt Consortium]