Magnetic beads have become a valuable tool in separating proteins or nucleic acids through their use as a chromatographic matrix. One such widely used technique is ion exchange chromatography which enables the separation and purification of a target molecule from crude biological materials. This separation is achieved by exploiting the differences in surface charges between the molecules, and by utilizing light binding and eluting conditions to maintain biological activity.
A magnetic bead known as BcMag™ Strong Cation Exchange (SCX) is composed of a uniform magnetic core that has been grafted with strong cation exchangers on its surface, using sulphonic acid functional groups. This magnetic resin-based format is capable of rapidly processing up to 96 samples in 20 minutes, with high yield. This technology can extract proteins or nucleic acids from complex biological samples (such as serum, plasma, etc.) either manually or automatically. Once purified, the protein can be used in a variety of downstream applications, including sample fractionation for 1D and 2D SDS-PAGE, X-ray crystallization, and NMR spectroscopy. In cases where weak ion exchangers fail, strong ion exchangers have been shown to be effective separation tools, since their selectivities differ greatly.
Strong Cation Exchange magnetic resins are used to replace time-consuming, complex, and costly chromatographic procedures such as agarose, cellulose, Sepharose, and Sephadex-based columns or resins. In column-based procedures, the lysate is centrifuged or cleared, the supernatant is added to the column, the membrane or resin is washed with buffer through centrifugation or vacuum manifold, and the required biomolecules are eluted in an adequate volume of buffer. When using column-based technologies, processing multiple samples in academic research labs may necessitate a significant quantity of hand pipetting. This pipetting can discourage differences in target biomolecule yield between experiments and people. Staff and students may require extensive training and practice to produce constant protein yields.
Strong Cation Exchange Magnetic resins have significant advantages over non-magnetic resin technologies. It is due to the numerous benefits of magnetic beads, such as their ease of use, rapid experimental protocols, suitability, and convenience for high-throughput automated and miniaturized processing. They thus see increasing use in various areas of life-sciences research and development, including drug discovery, biomedicine, bioassay development, diagnostics, genomics, and proteomics.
feature and benefits
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Fast and straightforward – Magnetic beads-based format eliminates columns or filters or a laborious repeat of pipetting or centrifugation.
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Convenient and expandable – Magnetic format enables high-throughput processing of multiple samples in parallel with many different automated liquid handling systems.
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Robust – Magnetic beads do not crack or run dry.
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Low bed volume – Working with small magnetic bead volumes allows for minimal buffer volumes, resulting in concentrated elution fractions.
Applications
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Protein pre-fractionation in cell lysates
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Optimizing purification conditions for new protein preparation protocols
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Protein purification and concentration
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Antibody purification from serum, ascites, or tissue culture supernatant
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Preparation of samples before 1D or 2D PAGE
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Phosphopeptide purification before MS analysis
Learn More
Instruction Manual
MSDS
Related Ion Exchange Magnetic Beads →General Reference
1.
Edelmann MJ. Strong cation exchange chromatography in analysis of posttranslational modifications: innovations and perspectives. J Biomed Biotechnol. 2011;2011:936508.
2.
Stone MT, Cotoni KA, Stoner JL. Cation exchange frontal chromatography for the removal of monoclonal antibody aggregates. J Chromatogr A. 2019 Aug 16;1599:152-160.
3.
Herciková J, Spálovská D, Frühauf P, Izák P, Lindner W, Kohout M. Design and synthesis of naphthalene-based chiral strong cation exchangers and their application for chiral separation of basic drugs. J Sep Sci. 2021 Sep;44(18):3348-3356.
4.
Janakiraman VN, Solé M, Maria S, Pezzini J, Cabanne C, Santarelli X. Comparative study of strong cation exchangers: Structure-related chromatographic performances. J Chromatogr B Analyt Technol Biomed Life Sci. 2018 Mar 30;1080:1-10.
5.
Wang F, Dong J, Jiang X, Ye M, Zou H. Capillary trap column with strong cation-exchange monolith for automated shotgun proteome analysis. Anal Chem. 2007 Sep 1;79(17):6599-606.
6.
Das S, Bosley AD, Ye X, Chan KC, Chu I, Green JE, Issaq HJ, Veenstra TD, Andresson T. Comparison of strong cation exchange and SDS-PAGE fractionation for analysis of multiprotein complexes. J Proteome Res. 2010 Dec 3;9(12):6696-704.
7.
Steinebach F, Wälchli R, Pfister D, Morbidelli M. Adsorption Behavior of Charge Isoforms of Monoclonal Antibodies on Strong Cation Exchangers. Biotechnol J. 2017 Dec;12(12).
