Description
Product Usage Information
Biotinylated antibodies are ideal for immunoassay technologies and high-throughput ELISA platforms that require antibody pairs where both antibodies are from the same host. Platforms utilizing biotinylated antibodies include, but are not limited to, MSD, xMAP, Quanterix Simoa, AlphaLISA, AlphaScreen, HTRF, LANCE, and TR-FRET. Optimal dilutions/working concentrations should be determined by the end user. Please contact us if you require the antibody clone biotinylated at a different concentration, a carrier-free formulation, or a more customized packaging solution.
Storage
Supplied in 140 mM NaCl, 3 mM KCl, 10 mM sodium phosphate (pH 7.4) dibasic, 2 mM potassium phosphate monobasic, 2 mg/mL BSA, and 50% glycerol. Store at -20°C. Do not aliquot the antibody.
Specificity / Sensitivity
K48-linkage Specific Polyubiquitin (D9D5) Rabbit Monoclonal Antibody (Biotinylated) detects polyubiquitin chains formed by Lys48 residue linkage. This antibody does not react with monoubiquitin or polyubiquitin chains formed by specific linkage to a different lysine residue.
Species Reactivity: All Species Expected
Source / Purification
Monoclonal antibody is produced by immunizing animals with a synthetic peptide corresponding to residues surrounding the Lys48 branch of the human diubiquitin chain.
Background
Ubiquitin is a conserved polypeptide unit that plays an important role in the ubiquitin-proteasome pathway. Ubiquitin can be covalently linked to many cellular proteins by the ubiquitination process, which targets proteins for degradation by the 26S proteasome. Three components are involved in the target protein-ubiquitin conjugation process. Ubiquitin is first activated by forming a thiolester complex with the activation component E1; the activated ubiquitin is subsequently transferred to the ubiquitin-carrier protein E2, then from E2 to ubiquitin ligase E3 for final delivery to the epsilon-NH of the target protein lysine residue (1-3). The ubiquitin-proteasome pathway has been implicated in a wide range of normal biological processes and in disease-related abnormalities. Several proteins such as IκB, p53, cdc25A, and Bcl-2 have been shown to be targets for the ubiquitin-proteasome process as part of regulation of cell cycle progression, differentiation, cell stress response, and apoptosis (4-7). Substrate proteins are linked to ubiquitin using seven distinct ubiquitin lysine residues (Lys6, Lys11, Lys27, Lys29, Lys33, Lys48 and Lys63). Formation of a polyubiquitin chain occurs when a lysine residue of ubiquitin is linked to the carboxy-terminal glycine of another ubiquitin. Proteins polyubiquinated at specific lysine residues display a tendency to be targeted for different processes; K48-linked polyubiquitin chains mainly target proteins for proteasomal degradation while K63-linked polyubiquitin regulates protein function, subcellular localization, or protein-protein interactions (8).
