SI0104B: Biotinylated M1 (linear) Tetra-Ubiquitin

M1-linked ubiquitination is traditionally associated with regulation of NFĸB and IFN signaling. M1 Tetra-Ubiquitin is a tetrameric chain of wild-type ubiquitin. It is expressed as a linear chain wherein monomers are linked through N-terminal methionines and C-terminal glycines. 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 types have been determined to 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). This is recombinant tetra-ubiquitin expressed as a linear chain. Amide linkages join the N- and C-terminus of each ubiquitin molecule. This molecule is HIS-tagged at the N-terminus of the most distal ubiquitin. The M1 Linear Tetra-Ubiquitin chain is biotinylated on one available site. This biotin acts as a means of detection via streptavidin or avidin. The applications are numerous from Western Blots to ELISAs. Testing can vary based off of intended application (EX: DUB activity/specificity). Info

Species	Human
Source	E. coli
Tag	Biotin
Molecular Weight	35,146.5 Da
Quantity	25µg
Concentration	Variable
Formulation	20 mM Tris pH 7.5, 150 mM NaCl
Storage	-80°C, avoid freeze/thaw cycles