Description: Ubiquitin is a highly conserved 76kDa protein which is ligated to many proteins in both monomeric and polymeric forms. Ubiquitin polymers (polyubiquitin) can be found in several varieties depending on which of its 7 lysine residues is the site of ligation. The two most common polymer chains are linked via an isopeptide bond between glycine-76 and either lysine-48 (K-48) or lysine-63 (K-63). K-48-linked polyubiquitination typically results in targeting the protein to the 26S proteosome resulting in proteolysis, although recently exceptions to this have been observed. In contrast, K-63-linked polyubiquitination results in signals related to intracellular trafficking, cell signaling, ribosomal biogenesis, and DNA damage repair. There are also reports that K63-linked polyubiquitin is involved in proteosome-independent proteolysis via autophagy.
HWA4C4 reacts specifically with the isopeptide linkage region of lysine-63-linked polyubiquitin. It does not react with other forms of ubiquitin including ubiquitin monomer and lysine-48-linked chains.
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