NC0102: Non-Cleavable Linear Di-Ubiquitin


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**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 a 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). These specific chains are not cleaved by the linear specific deubiquitylase Otulin and have applications as a control.Recombinant linear chains of defined length expressed in E. coli and purified to homogeneity. 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.


Species Human
Source E. coli
Tag His
Molecular Weight 17,786.2 Da
Quantity 100 µg
Concentration Variable
Formulation 20 mM Tris pH 7.5, 150 mM NaCl, 1 mM EDTA
Storage -80°C, avoid freeze/thaw cycles

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  • Investigation of binding interactions through pull-down studies.
  • Determining potential deubiquitylase activity towards linear chains.
  • Please note: These linear ubiquitin chains have had the methionine residue between each ubiquitin moiety genetically removed, i.e. Gly76 is fused directly to Gln2.  As a result, they are not recognized by LUB-9, the linear chain-specific monoclonal antibody, nor are they cleaved by Otulin (aka Gumby), the linear chain-specific DUB.