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Advanced cell-free protein synthesis enabling precise stable isotope labeling for high-resolution NMR spectroscopy and structural biology research. Cost-effective labeling with minimal precursor requirements.
Trusted by leading research and pharmaceutical institutions
U-15N, U-15N,13C for comprehensive structural assignment
Single amino acid types for focused spectral analysis
Intein-based labeling for complex multidomain proteins
Advanced cell-free technology enabling precise stable isotope labeling for NMR spectroscopy and structural biology research
CFPS systems require significantly less isotopic media than cell culture, drastically reducing costs of expensive precursors like 13C Glucose and D2O while maintaining exceptional labeling fidelity.
The defined, open nature of our lysate ensures precise control over the amino acid pool, resulting in minimal scrambling and near 100% labeling efficiency for clean NMR spectra.
Successfully labels toxic, aggregation-prone, and membrane proteins that are often difficult or impossible to express in standard E. coli culture for NMR study.
The synthesis reaction is completed in hours, accelerating the overall timeline for structural data acquisition compared to traditional cell-based methods.
Get expert consultation on your labeling strategy and project requirements
Comprehensive isotope labeling solutions for NMR spectroscopy and structural biology applications
Standard U-15N or U-15N,13C labeling using minimal quantities of 15NH4Cl and/or 13C-Glucose for comprehensive structural assignment and backbone resonance determination.
Using D2O as solvent, this method replaces exchangeable protons with deuterium, essential for large protein studies to improve relaxation properties and spectral quality.
Only one or a few specific amino acid types are labeled, ideal for focusing on active sites or specific protein regions without spectral congestion.
Advanced CFPS capability to label only a defined N or C-terminal segment via protein ligation using intein splicing technology for complex multidomain proteins.
Specific labeling of methyl groups in a deuterated background for high-sensitivity NMR of very large protein complexes up to 1 MDa.
Using deuterated D-glucose as carbon source in H2O-based medium, achieving high deuteration levels for enhanced spectral resolution in MAS NMR studies.
Comprehensive specifications for our isotope labeling service
| Parameter | Specification | Details |
|---|---|---|
| Labeling Efficiency | 95% or higher | Near 100% incorporation verified by mass spectrometry |
| Protein Purity | 95% or higher | NMR-grade, verified by SDS-PAGE and HPLC |
| Protein Size Range | Up to 1 MDa | Methyl labeling in deuterated background for large complexes |
| Expression Systems | E. coli CFPS | Standard lysate system, optimized for isotope labeling |
| Available Labels | 15N, 13C, 2H | Uniform, selective, and segmental labeling options |
| Delivery Format | Lyophilized powder | With COA, MS report, and purity data |
| Quality Verification | MS + SDS-PAGE | Complete documentation package included |
Streamlined process from project design to NMR-ready protein delivery
Consultation on optimal labeling strategy based on target protein and NMR experiment
Optimization of DNA template for maximal expression in lysate system
Precise addition of isotopic precursors for maximum incorporation
Affinity chromatography and SEC for NMR-grade purity
MS verification of labeling fidelity and SDS-PAGE purity
Broad applicability for structural biology and biochemistry research
3D NMR experiments for complete backbone resonance assignment
Proton-proton distance measurements for structure calculation
Ligand binding and protein-protein interaction analysis
Relaxation measurements for protein motion characterization
Selenomethionine labeling for SAD phasing
High-purity samples for electron microscopy studies
Solid-state NMR with deuterated samples
Small-angle scattering for solution structure
Structural characterization of drug targets
STD-NMR and ligand-observed experiments
Structure-activity relationship studies
Enzyme mechanism and catalysis investigation
Trusted by researchers worldwide for quality and reliability.
The CFPS system enabled us to express a toxic kinase domain for NMR that simply would not work in traditional E. coli culture. We obtained high-quality spectra within two weeks.
We performed segmental labeling on a 80 kDa multidomain protein, which was impossible with traditional cell-based expression. The labeling efficiency exceeded our expectations.
Incorporating unnatural amino acids for site-specific labeling was straightforward with the open nature of the CFPS system. This capability has transformed our structural studies.
Key references supporting our CFPS isotope labeling technology
Van Raad D, Otting G, Huber T | Magnetic Resonance | 2023
Novel eCell system maintains complete metabolic enzyme activity in cell-free protein synthesis. Demonstrates selective 13C labeling of methyl groups in ubiquitin and PpiB proteins from inexpensive precursors with 70%+ labeling efficiency.
View DOIDubey A, Stoyanov N, Viennet T, et al. | Angewandte Chemie | 2021
Efficient method to observe methyl groups of leucine residues in proteins expressed in bacterial, eukaryotic, or cell-free systems without modifying expression protocols. Achieves 20x cost reduction compared to previous methods.
View DOIImbert L, Lenoir-Capello R, Crublet E, et al. | Methods in Molecular Biology | 2021
Cell-free synthesis enables large-scale protein sample production for structural investigations. Optimized protocols for perdeuterated protein production with full protonation of amide NMR probes for high-molecular-weight proteins up to 468 kDa.
View DOIDaniilidis M, Sperl LE, Müller BS, et al. | JACS | 2024
Stabilized split-intein system enables rapid high-yield protein trans-splicing of integral membrane proteins under denaturing conditions. Demonstrates simplified NMR spectra and structure determination of membrane proteins.
View DOIRowlinson B, Crublet E, Kerfah R, Plevin MJ | Biochemical Society Transactions | 2022
Comprehensive review of specific isotopic labeling and reverse labeling strategies using metabolic precursors. Methods simplify NMR spectra, improve sensitivity, and facilitate resonance assignment for various NMR applications.
View DOICommon questions about our CFPS isotope labeling services
Get a customized quote for your CFPS Isotope Labeling for NMR/Structure Service project. Our experts will respond within 24 hours.
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