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Trusted by Leading Research & Pharma Institutions

CFPS Isotope Labeling for NMR & Structure

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.

95%+ Labeling Efficiency
NMR Grade Purity
Up to 1 MDa Complexes
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Trusted by leading research and pharmaceutical institutions

Harvard
Pfizer
MIT
Roche
Stanford
Merck

Why Choose Us

Cost-effective labeling with minimal precursors
Near 100% incorporation verified by MS
Minimal scrambling in defined lysate
Toxic and membrane proteins supported

Uniform Labeling

U-15N, U-15N,13C for comprehensive structural assignment

Selective Labeling

Single amino acid types for focused spectral analysis

Segmental Labeling

Intein-based labeling for complex multidomain proteins

Protein Size
Up to 1 MDa

Why Choose Our CFPS Isotope Labeling Service

Advanced cell-free technology enabling precise stable isotope labeling for NMR spectroscopy and structural biology research

Cost Efficiency

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.

Maximum 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.

Difficult Proteins

Successfully labels toxic, aggregation-prone, and membrane proteins that are often difficult or impossible to express in standard E. coli culture for NMR study.

Rapid Turnaround

The synthesis reaction is completed in hours, accelerating the overall timeline for structural data acquisition compared to traditional cell-based methods.

Ready to Accelerate Your NMR Research

Get expert consultation on your labeling strategy and project requirements

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Advanced Labeling Technologies

Comprehensive isotope labeling solutions for NMR spectroscopy and structural biology applications

Uniform Labeling

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.

Deuteration

Using D2O as solvent, this method replaces exchangeable protons with deuterium, essential for large protein studies to improve relaxation properties and spectral quality.

Selective Labeling

Only one or a few specific amino acid types are labeled, ideal for focusing on active sites or specific protein regions without spectral congestion.

Segmental Labeling

Advanced CFPS capability to label only a defined N or C-terminal segment via protein ligation using intein splicing technology for complex multidomain proteins.

Methyl Group Labeling

Specific labeling of methyl groups in a deuterated background for high-sensitivity NMR of very large protein complexes up to 1 MDa.

Inverse Fractional Deuteration

Using deuterated D-glucose as carbon source in H2O-based medium, achieving high deuteration levels for enhanced spectral resolution in MAS NMR studies.

Service Specifications

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

Integrated Service Workflow

Streamlined process from project design to NMR-ready protein delivery

1

Project Design

Consultation on optimal labeling strategy based on target protein and NMR experiment

2

Template Prep

Optimization of DNA template for maximal expression in lysate system

3

Labeling Reaction

Precise addition of isotopic precursors for maximum incorporation

4

Protein Purification

Affinity chromatography and SEC for NMR-grade purity

5

Quality Control

MS verification of labeling fidelity and SDS-PAGE purity

Applications

Broad applicability for structural biology and biochemistry research

Backbone Assignment

3D NMR experiments for complete backbone resonance assignment

NOE Distance Restraints

Proton-proton distance measurements for structure calculation

Interaction Studies

Ligand binding and protein-protein interaction analysis

Dynamics Analysis

Relaxation measurements for protein motion characterization

Testimonials

What Our Clients Say

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.

SR
Senior Researcher
Pharmaceutical Company

We performed segmental labeling on a 80 kDa multidomain protein, which was impossible with traditional cell-based expression. The labeling efficiency exceeded our expectations.

PI
Principal Investigator
Academic Research Institution

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.

PD
Postdoctoral Fellow
Biotechnology Company

Scientific Literature

Key references supporting our CFPS isotope labeling technology

15 Citations

Cell-free synthesis of proteins with selectively 13C-labelled methyl groups from inexpensive precursors

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 DOI
42 Citations

Local Deuteration Enables NMR Observation of Methyl Groups in Proteins from Eukaryotic and Cell-Free Expression Systems

Dubey 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 DOI
28 Citations

In Vitro Production of Perdeuterated Proteins in H2O for Biomolecular NMR Studies

Imbert 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 DOI
12 Citations

Efficient Segmental Isotope Labeling of Integral Membrane Proteins for High-Resolution NMR Studies

Daniilidis 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 DOI
35 Citations

Specific isotopic labelling and reverse labelling for protein NMR spectroscopy: using metabolic precursors in sample preparation

Rowlinson 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 DOI

Frequently Asked Questions

Common questions about our CFPS isotope labeling services

What types of isotope labeling do you offer?
We offer comprehensive isotope labeling including uniform labeling (U-15N, U-15N/13C), selective amino acid labeling, deuteration (perdeuteration and selective deuteration), segmental labeling via intein splicing, and methyl group labeling (Ile, Val, Leu, Met) in deuterated background. Each strategy is optimized for specific NMR applications and protein size ranges.
What labeling efficiency can I expect?
Our CFPS system consistently achieves 95%+ incorporation efficiency for uniform labeling, verified by mass spectrometry. The defined nature of the cell-free lysate minimizes metabolic scrambling, ensuring clean spectral data. We provide mass spec verification reports with every labeled sample.
Can you label large protein complexes?
Yes, our system supports protein complexes up to 1 MDa. For large systems, we recommend methyl group labeling in a deuterated background, which provides high-sensitivity NMR signals while minimizing spectral complexity. This approach is ideal for studying protein-protein interactions in large assemblies.
What are the cost advantages of CFPS labeling?
CFPS requires significantly less isotopic precursor than traditional cell culture because the reaction volume is much smaller and the system is closed. This reduces costs for expensive isotopes like 13C-Glucose and D2O by up to 90% while maintaining excellent labeling fidelity.
Do you support segmental labeling?
Yes, we offer segmental labeling using intein-mediated protein ligation. This allows labeling of specific domains within a multidomain protein, dramatically reducing spectral complexity for large proteins. This is particularly valuable for proteins where only one domain is of interest for NMR studies.
How do I submit my project?
Submit your gene sequence (FASTA format) or plasmid map through our online portal. Include information about your target protein, desired labeling scheme, and NMR experiments planned. Our scientific team will review your requirements and provide a detailed quote within 24 hours.

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