Anti-Diglycyl-Lysine Antibody Conjugated Agarose Beads

IAP

Cold packs / dry ice

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 and controls the activity of many signal transduction pathways. Ubiquitination occurs through the formation of an isopeptide bond between its C-terminus 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.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.

Antibody conjugated agarose beads are supplied as a 50% slurry containing 66% glycerol and 4 mg/ml immobilized antibody.

Lys

Polyclonal/Monoclonal