B Cell-based Nuclear Magnetic Resonance (NMR) Assay

Antigen-antibody Interaction NMR Spectrum

Nuclear magnetic resonance (NMR) spectroscopy is a sensitive and high-resolution technique that can be used to characterize antigen-antibody interactions. NMR is a widely used structure technique for small, less complicated molecule analysis and can yield high-resolution, multidimensional spectra of large molecules. NMR technique is necessary to help us further understand the antigen-antibody interaction dynamics and obtain predominant antigen epitope information.

With extensive knowledge of structural biology and antigen epitope discovery, Creative Biolabs offers the antibody-based NMR Assay for cancer epitope analysis for clients all over the world.

NMR Assay Service at Creative Biolabs

Creative Biolabs offers NMR spectroscopy technique-based epitope mapping by comparing the NMR spectrum changes before and after an antibody binding to an antigen and determining the atoms at the interaction interface.

What Can We Do in NMR Spectroscopy-mediated Cancer Epitope Analysis?

The Technology Of ¹⁵N-HSQC Experiment for Epitope Mapping

Principal of the ¹⁵N-HSQC Experiment

Fig.1 Schematic representation of an NMR epitope mapping experiment.¹

Our Protocol

• First, the free antigen protein is labeled with ¹⁵N, generating an NMR spectrum.
• Then, an unlabeled antibody is added to interact with the antigen and will not generate any NMR signal in the spectrum but affect the antigen signal by antigen-antibody complex formation.
• Finally, by overlaying the two NMR spectra, we can identify the signals influenced by antibody contact and generate potential epitope residues of the antigen.

Choose the NMR Epitope Mapping Method Based on the Sample

• Conduct both ¹⁵N-HSQC and its TROSY equivalent experiment.
• Find the better method suitable for your specific sample from the two methods.
• Conduct the whole experiment with the chosen option.
• Transverse Relaxation Optimized Spectroscopy (TROSY): Detect signals generated from large protein residues.

Fig.2 ¹H¹⁵N HSQC data acquisition and analysis.²

More Related Services

Highlights

• High Sensitivity
• High Resolution
• Multidimensional Analysis

References

1. Bardelli, M.; et al. Epitope mapping by solution NMR spectroscopy. Journal of molecular recognition : JMR. 2015, 28(6): 393–400.
2. Valente, A. P.; Manzano-Rendeiro, M. Mapping conformational epitopes by NMR spectroscopy. Current opinion in virology. 2021, 49: 1–6.
3. Pourmodheji, H.; et al. A Multidisciplinary Approach to High Throughput Nuclear Magnetic Resonance Spectroscopy. Sensors. 2016, 16: 850.

For Research Use Only | Not For Clinical Use