Anti-Ubiquitin

0.5mg/ml if reconstituted with 0.2ml sterile DI water. Ubiquitin (originally, ubiquitous immunopoietic polypeptide) is a small regulatory protein that has been found in almost all tissues (ubiquitously) of eukaryotic organisms. Its gene is mapped to 16p 13.3. The ubiquitin protein itself consists of 76 amino acids and has a molecular mass of about 8.5 kDa. Ubiquitin binds to proteins and labels them for destruction. It directs protein recycling and also direct proteins to other locations in the cell, where they control other protein and cell mechanisms. 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 lysosomal degradation, 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]