MabMix Antibody Reference Panel

The MabMix monoclonal antibody reference panel is a mixture of glycans commonly found on monoclonal antibodies which includes G2F(NA2F), G0F(NGA2F), and both G1F(FA2G1) isomers. Over 90% purity as assessed by HPLC.

The Ludger MabMix monoclonal antibody reference standard combines fucosylated N-glycans commonly found on monoclonal antibodies and is a test standard used both in FDA- and EMA-approved assays worldwide.

This library is typically used as a reference standard for a mixture of glycans commonly found in therapeutic monoclonal antibodies. It can also be implemented as a process control to assess the performance of a glycan labelling protocol and/or a system suitability standard for the analytical platform.

The use of standards is part of the guidelines listed in the ICH Topic Q6B Specifications: Test Procedures and Acceptance Criteria for biotechnological/Biological Products. They are beneficial for biotherapeutics development, testing of biosimilars and supporting regulatory submissions.

This library combines four N-glycan oligosaccharides which are found on several mammalian glycoproteins including IgG, gamma globulins, and many serum glycoproteins. The glycans are typically purified from the oligosaccharide pool released from porcine thryroglobulin or bovine serum. The antibody reference panels are qualified by MS, HPLC and NMR analysis to meet the high purity and quality standards required by advanced analytical techniques. The standard includes the following; G2F(NA2F), G0F(NGA2F), and both G1F(FA2G1) isomers.

The Ludger MabMix antibody reference panel standards are supported by complete documentation. The certificate of analysis contains the results from the testing used to characterize the material across a complete range of quality characteristics. These standards are well-characterised with documented purity. Each oligomannose reference panel vial contains approximately 10µg of oligomannose N-glycans.

Form: Dry. Dried by centrifugal evaporation from an aqueous solution.

Molecular Weight:
G2F 1787
G1F 1624
G0F 1463

Purity: > 90% pure as assessed by HPLC

Storage: -20˚C both before and after dissolution. This product is stable for at least 5 years as supplied. View Certificate of Stabilty

Shipping: The product can be shipped at ambient when dry. After dissolution, ship on dry ice.

Handling: Allow the unopened vial of the antibody reference panel to reach ambient temperature and tap unopened on a solid surface to ensure that most of the lyophilized material is at the bottom of the vial. Gently remove the cap, add the desired volume of reconstitution medium, re-cap and mix thoroughly to bring all the oligosaccharide into solution. For maximal recovery of oligosaccharide, ensure that the cap lining is also rinsed and centrifuge the reconstituted vial briefly before use. Ensure that any glass, plasticware or solvents used are free of glycosidases and environmental carbohydrates. Minimise exposure to elevated temperatures or extremes of pH. High temperatures and low pH will cause desialylation. High pH will cause epimerisation of the reducing terminus GlcNAc.

Safety: The MabMix antibody reference panel is non-hazardous and has been purified from natural sources certified to be free of all hazardous material including pathogenic biological agents.

References

Beyer B, Schuster M, Jungbauer A, Lingg N. Microheterogeneity of Recombinant Antibodies: Analytics and Functional Impact. Biotechnol J. 2018 Jan;13(1). doi: 10.1002/biot.201700476. Epub 2017 Sep 25. Review.

Sha S, Agarabi C, Brorson K, Lee DY, Yoon S. N-Glycosylation Design and Control of Therapeutic Monoclonal Antibodies. Trends Biotechnol. 2016 Oct;34(10):835-846. doi: 10.1016/j.tibtech.2016.02.013. Epub 2016 Mar 22. Review

Liu L. Antibody glycosylation and its impact on the pharmacokinetics and pharmacodynamics of monoclonal antibodies and Fc-fusion proteins. J Pharm Sci. 2015 Jun;104(6):1866-1884. doi: 10.1002/jps.24444. Epub 2015 Apr 14.

Jefferis R. Recombinant antibody therapeutics: the impact of glycosylation on mechanisms of action. Trends Pharmacol Sci. 2009 Jul;30(7):356-62. doi: 10.1016/j.tips.2009.04.007. Epub 2009 Jun 22. Review.

Jefferis R. Glycosylation of recombinant antibody therapeutics. Biotechnol Prog 21: pp11-16, 2005

Fernandes D. Demonstrating Comparability of Antibody Glycosylation during Biomanufacturing. European Biopharmaceutical Review. Summer 2005. pp 106 -110