Anti-Diglycyllysine Rabbit pAb

IAP

Ambient temperature

Multiple

Post-Translational Modificaiton

Ubiquitin (Ub) is a highly conserved 76-amino acid protein that plays a critical role in regulating cellular processes. By covalently attaching to target proteins through a three-step process involving Ub-activating (E1), Ub-conjugating (E2), and Ub-ligating (E3) enzymes, ubiquitination marks the target proteins for proteasomal degradation, modulates membrane protein trafficking, alters protein-protein interactions, and controls the activity of many signal transduction pathways. Ubiquitination occurs through the formation of an isopeptide bond between its C-terminal Gly76 and a lysine residue in the target protein. This process can occur either as a monomer (monoubiquitin) or as a polymer (polyubiquitin chains), where the C-terminus of a chain extending ubiquitin becomes linked to the N-terminus (M1) or one of seven Lys residues (Lys6, Lys11, Lys27, Lys29, Lys33, Lys48, and Lys63) within a substrate-bound ubiquitin molecule, resulting in polyubiquitin chains with different functions.Members of the ubiquitin-like protein family, such as small ubiquitin-related modifier 1, 2 and 3 (SUMO1, 2 and 3), have functions similar to ubiquitin, whereby they bind to target proteins as part of a post-translational modification system. SUMO can be covalently attached to proteins as a monomer or a lysine-linked polymer via an isopeptide bond. SUMO-1 regulates nuclear trafficking, formation of subnuclear structures, transcriptional activity, and protein stability by being conjugated to proteins such as RanGAP, PML, p53 and IκB-α. SUMO-2/-3 forms poly-(SUMO) chains and is conjugated to topoisomerase II and APP, regulating chromosomal segregation and cellular responses to environmental stress.

Anti-Diglycyl-Lysine Rabbit pAb selectively captures peptides/proteins bearing K-ɛ-G-G residues, which are remnants of ubiquitin left in protein substrates after trypsin digestion, or SUMO remnants generated by α-lytic protease WaLP digestion. This pan antibody recognizes diglycyl-lysine independent of its surrounding sequences and has been well utilized to affinity purify peptides for global proteomic screening of ubiquitination and SUMOylation.

Diglycyl

Diglycylated lysine peptides

Ubiquitin (Ub) is a highly conserved 76-amino acid protein that plays a critical role in regulating cellular processes. By covalently attaching to target proteins through a three-step process involving Ub-activating (E1), Ub-conjugating (E2), and Ub-ligating (E3) enzymes, ubiquitination marks the target proteins for proteasomal degradation, modulates membrane protein trafficking, alters protein-protein interactions, and controls the activity of many signal transduction pathways. Ubiquitination occurs through the formation of an isopeptide bond between its C-terminal Gly76 and a lysine residue in the target protein. This process can occur either as a monomer (monoubiquitin) or as a polymer (polyubiquitin chains), where the C-terminus of a chain extending ubiquitin becomes linked to the N-terminus (M1) or one of seven Lys residues (Lys6, Lys11, Lys27, Lys29, Lys33, Lys48, and Lys63) within a substrate-bound ubiquitin molecule, resulting in polyubiquitin chains with different functions.
Members of the ubiquitin-like protein family, such as small ubiquitin-related modifier 1, 2 and 3 (SUMO1, 2 and 3), have functions similar to ubiquitin, whereby they bind to target proteins as part of a post-translational modification system. SUMO can be covalently attached to proteins as a monomer or a lysine-linked polymer via an isopeptide bond. SUMO-1 regulates nuclear trafficking, formation of subnuclear structures, transcriptional activity, and protein stability by being conjugated to proteins such as RanGAP, PML, p53 and IκB-α. SUMO-2/-3 forms poly-(SUMO) chains and is conjugated to topoisomerase II and APP, regulating chromosomal segregation and cellular responses to environmental stress.