LifeSensors Inc products

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).