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Ubiquitin is a small polypeptide that is conjugated via its C-terminus to an ε-amino group of lysine on a target protein; this conjugation is referred to as monoubiquitylation. Subsequently, additional ubiquitin moieties can be conjugated to the initial ubiquitin, utilizing any of seven lysine residues (K6, K11, K27, K29, K33, K48, K63) on the surface of ubiquitin; this ubiquitin chain formation is referred to as polyubiquitylation. Enzymatic conjugation of ubiquitin is performed by a series of enzymes — ubiquitin activating enzyme E1, ubiquitin conjugating enzyme E2, and ubiquitin ligase E3.  Ubiquitylation of proteins is reversible in cells; both mono- and polyubiquitylated chains are cleaved by hydrolysis catalyzed by deubiquitylases (DUBs).

Based on UBA domains known to possess a high affinity for ubiquitin, Tandem Ubiquitin Binding Entities (TUBEs) have been developed for the isolation and identification of ubiquitinated proteins. TUBEs display up to a 1000-fold increase in affinity for polyubiquitin moieties over the single ubiquitin binding associated domain (UBA). In addition, TUBEs have been demonstrated to protect polyubiquitinated proteins from both deubiquitination and proteasome-mediated degradation, allowing for the detection of relatively low abundant proteins that cannot be detected with current technologies. This product is protected by one or more US or Foreign patents. Please read the Limited Use Label License to learn more. By purchasing this product, the purchaser agrees to comply with these terms.