Ubiquitin Remnant (K-ε-GG) Immunoaffinity Sorbent

Ubiquitin remnant (K-ε-GG) is a diglycyl-lysine motif found in proteins subject to ubiquitination, a process for tagging proteins for proteasomal degradation that is disrupted in certain diseases.^1,2 During ubiquitination, ubiquitin is covalently bound to the ε-NH₂ in lysine residues of the target protein via the C-terminal carboxyl group of ubiquitin, which is preceded by arginine-glycine-glycine (-RGG) residues.³ Ubiquitinated proteins can be detected, and enriched for, via antibodies toward the K-ε-GG motif resulting from this covalent bond.^1,4 Cayman's Ubiquitin Remnant (K-ε-GG) Immunoaffinity Sorbent is designed for immunoprecipitation (IP) of ubiquitin remnant (K-ε-GG) motif-containing proteins from biological samples. This is an effective way to concentrate ubiquitin remnant (K-ε-GG) motif-containing proteins for subsequent detection and analysis by LC-MS/MS. The ubiquitin remnant (K-ε-GG) affinity sorbent consists of a diglycyl-lysine specific monoclonal antibody coupled to CNBr-activated Sepharose 4B.

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1. Walton, A., Stes, E., Cybulski, N., et al. It’s time for some "site"-seeing: Novel tools to monitor the ubiquitin landscape in Arabidopsis thaliana. Plant Cell 28(1), 6-16 (2016).

2. Popovic, D., Vucic, D., and Dikic, I. Ubiquitination in disease pathogenesis and treatment. Nat. Med. 20(11), 1242-1253 (2014).

3. Hochstrasser, M. Evolution and function of ubiquitin-like protein-conjugation systems. Nat. Cell Biol. 2(8), E153-E157 (2000).

4. Udeshi, N.D., Svinkina, T., Mertins, P., et al. Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments. Mol. Cell. Proteomics 12(3), 825-831 (2013).