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Arrays of numerous spots containing specific oligonucleotides, DNA, proteins, peptides or other small molecules chemically attached to a substrate and organized in a grid on a supporting material; probe-based technique used in biochemistry and genetics.
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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.
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Ubiquitin-K48R K63R is recombinant ubiquitin having arginine substituted for lysine at positions 48 and 63. Ubiquitin is a small polypeptide that can be conjugated via its C-terminus to amine groups of lysine residue on target proteins. This conjunction is referred to as monoubiquitylation. Additional ubiquitin moieties can subsequently be conjugated to this initial ubiquitin. Utilizing any one (of seven) lysine residues on the surface of ubiquitin. The formation of these ubiquitin chains is referred to as polyubiquitylation.
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