**This chain is not recognized by LUB-9, the linear chain-specific monoclonal antibody, nor is it cleaved by Otulin (aka Gumby), the linear chain-specific DUB.**
A wide range of cellular processes are modulated through the generation and attachment of polyubiquitin (polyUb) chains to target proteins. Increasing evidence suggests that polyUb chains joined through linear peptide bonds between the C-terminus of one ubiquitin and the N-terminus of another play important functional roles. The enzyme machinery responsible for the generation of linear polyUb chains has been termed LUBAC, consisting of HOIL-1L and HOIP. Chains of these type have an open conformation, similar to polyUb K63, but with very distinct functional properties. Linear polyUb chains are cleaved by the deubiquitylases CYLD, USP5 (IsoT), USP2 and have been shown to bind to many UBDs including NEMO and Trabin-n (3xnzf). Recombinant pentaubiquitin is expressed as a linear chain. Amide linkages join the N- and C-terminus of each ubiquitin molecule to each other. This molecule is His-tagged at the N-terminus of the most distal ubiquitin. The methionine residue normally found between each ubiquitin moiety in the chain has been deleted, making this chain resistant to cleavage by otulin as well as not recognized by LUB9, a linear chain specific antibody (Cat. # AB130).
|20 mM Tris pH 7.5, 150 mM NaCl, 1 mM EDTA
|-80°C, avoid freeze/thaw cycles