Description
Ubiquitination plays a key role in protein degradation and signal transduction. Characterization of ubiquitination sites is important for understanding the role of this modification in cellular processes and disease. Ubiquitination sites are usually identified by detection of Lys-?-Gly-Gly (K-?-GG)-remnant peptides, which are generated by tryptic digestion of proteomes. The di-glycine remnant left at sites of ubiquitination after trypsin digestion through cleavage of the C-terminal –RGG sequence on ubiquitin (K-ε-GG). This Ubiquitin K-ε-GG remnant motif antibody will recognize the di-glycine remnant independent of flanking amino acid sequence.