Polyethylene Glycol (PEG) Backbone antibody RabMAb®Cat.#: 3104-1
Abcam ID: ab133471
Rabbit Monoclonal Antibody
Swiss Prot: N/A
Polyethylene glycol（PEG）is a family of long chain polymers attached to a glycerine backbone. It is a nonionic, nontoxic, biocompatible, strongly hydrophilic polymer, which has a large exclusion volume in aqueous solution (1). The covalent attachment of PEG is now commonly used to modify a variety of proteins and drugs (2,3). The modification of a biopharmaceutical with polyethylene glycol (PEG) increases its hydrodynamic radius, reduces immunogenicity and proteolytic cleavage. Other benefits include decelerated renal excretion, improved stability towards proteolysis and increased solubility of the biopharmaceutical in aqueous solutions (4). As examples, PEG–adenosine deaminase (Adagen®) is used for the treatment of severe combined immunodeficiency syndrome, PEG–asparaginase (Oncaspar®) is used for the treatment acute lymphoblastic leukemia, PEG–interferon α2a (Pegasys®) is used for the treatment Hepatitis C, Branched PEG–anti–VEGF aptamer (Pegaptanib, Macugen™) is used for the treatment Macular degeneration(age-related) (5). An Anti–PEG antibody can be used to monitor a drugs pharmacokinetics, including distribution, metabolism and excretion. In addition, it can be used for the quality control of pegylated molecules in ELISA, WB and flow cytometery.
Please note, this antibody is Rabbit Monoclonal IgM.
Applications and Recommended Dilution Factors
KLH-PEG20K was used as an immunogen. This antibody recognizes the backbone of the PEG molecule. Please note, this antibody is Rabbit Monoclonal IgM.
Storage Condition and Buffer
Store at 4°C or aliquot and store at -20 °C. Buffer: PBS, 0.01% sodium azide. Stable for 12 months from date of receipt.
1. Guiotto, A. et al. (2004) Anchimeric assistance effect on regioselective hydrolysis of branched PEGs: a mechanistic investigation. Bioorg. Med.Chem. 12, 5031–5037 2. Wong, S.S. (1991) Reactive groups of proteins and their modifying agents. In Chemistry of protein conjugation and cross-linking, p. 13, CRC Press 3. Caliceti, P. et al.(1993) Active site protection of proteolytic enzymes by poly(ethylene glycol) surface modification. J. Bioact. Comp. Polym. 8,41–50 4. Frank Leenders, celares GmbH, Berlin, Germany.(2006) PEGylation technology and biopharmaceuticals. Biopharmaceuticals. 6,39-40 5. Francesco M.Veronese, Gianfranco Pasut. (2005) PEGylation, successful approach