Biomolecular Interaction Analysis
Get the accuracy, sensitivity and wide dynamic range you need for high-quality traditional biomolecular interaction analysis. Reichert’s Surface Plasmon Resonance (SPR) systems are designed to give you more — more flexibility, more choices, and more ways to advance your research.
- Combine SPR with other techniques
- Analyze crude samples and whole cells
- Study protein-low molecular weight applications
All Major Classes of Biomolecules
Biomolecular interaction analysis involves interactions within and between:
- Nucleic acids (DNA/RNA)
With Reichert SPR, you can characterize these interactions by determining the binding kinetics and affinity of the interaction of interest. These results let you relate structure to function, and understand complex biological pathways.
More Sensitive, More Accurate
Reichert SPR systems are highly sensitive, which allows you to work with very low immobilization levels — and therefore improve the accuracy of your results.
Differentiate antibody affinity and kinetics — and carry out epitope mapping.
Human Serum Albumin (HSA) Binding to Biotinylated Anti-HSA lgG Captured on Planar Neutravidin Surface
- Application Note 1
- Presents the binding kinetics of a model antibody-antigen system, HSA binding to anti-HSA IgG
Antibody based capture analysis using a Reichert SR7500DC Surface Plasmon Resonance (SPR) system
- Application Note 8
- Uses non-covalent capture methods to attach ligands to an SPR surface
Surface Plasmon Resonance and Vaccine Research – Developments in Malaria Research
- Application Note 18
- Outlines how SPR can be used for early stage studies related to the development of vaccines.
Jinzhao Hou, Sharon A. Townson, Joseph T. Kovalchin, Allyson Masci, Olga Kiner, Yanqun Shu, Bracken M. King, Emily Schirmer, Kathryn Golden, Christoph Thomas, K. Christopher Garcia, Gregory Zarbis-Papastoitsis, Eric S. Furfine, and Thomas M. Barnes. “Design of a superior cytokine antagonist for topical ophthalmic use.” PNAS March 5, 2013 110 (10) 3913-3918; https://doi.org/10.1073/pnas.1217996110
Filippova EV, Zemaitaitis B, Aung T, Wolfe AJ, Anderson WF. “Structural Basis for DNA Recognition by the Two-Component Response Regulator RcsB.” MBio. 2018 Feb 27;9(1). pii: e01993-17. doi: 10.1128/mBio.01993-17.
Gruszczyk J, Kanjee U, Chan LJ, Menant S, Malleret B, Lim NTY, Schmidt CQ, Mok YF, Lin KM, Pearson RD, Rangel G, Smith BJ, Call MJ, Weekes MP, Griffin MDW, Murphy JM, Abraham J, Sriprawat K, Menezes MJ, Ferreira MU, Russell B, Renia L, Duraisingh MT, Tham WH. “Transferrin receptor 1 is a reticulocyte-specific receptor for Plasmodium vivax.” Science. 2018 Jan 5;359(6371):48-55. doi: 10.1126/science.aan1078.