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Biophysical Protein Characterization Services |
Accelerate protein and antibody development with integrated analytics
Outsource your protein or antibody expression and gain immediate access to high-quality biophysical characterization data. Our integrated workflow combines recombinant protein expression with nanoDSF, DLS, and SEC MALS analysis—helping you identify stability, aggregation, and molecular integrity risks early.
Tailored for antibody discovery, protein engineering, and therapeutic development, this service enables clear, actionable insights—without the complexity of managing multiple vendors.
Why biophysical characterization matters in protein development
Early-stage protein candidates often fail due to hidden developability risks such as:
- Low thermal stability
- Aggregation or oligomerization
- Structural heterogeneity
Detecting these issues after scale-up or preclinical research studies can lead to costly delays. Our biophysical characterization services enable early, reliable detection of these risks, supporting better candidate selection and faster decision-making.
Integrated protein expression and characterization workflow
We offer a seamless, end-to-end solution:
- Gene synthesis with optional sequence optimization
- Transient protein expression in mammalian systems
- Purification and documented analytical data
- Biophysical characterization (nanoDSF, DLS, SEC MALS)
With all steps integrated into a single workflow, sample integrity is maintained while timelines are shortened. Data can be provided either with or without shipment of the purified protein.
Protein Characterization Services
What is nanoDSF?
Nano differential scanning fluorimetry (nanoDSF) measures intrinsic protein fluorescence to assess thermal stability and unfolding behavior as temperature increases.
What it tells you:
- Onset temperature of unfolding (Ton)
- Melting temperature (Tm) and unfolding transitions
- Onset of aggregation (Tmacro)
Why it matters:
Identify unstable protein regions and compare candidate molecules based on thermal robustness.
What is DLS?
Dynamic Light Scattering (DLS) measures the size and distribution of particles in solution.
What it tells you:
- Hydrodynamic radius (rH)
- Polydispersity index (PDI)
Why it matters:
DLS detects early aggregation and colloidal instability, even before visible aggregates form.
What is SEC MALS?
Size Exclusion Chromatography with Multi-Angle Light Scattering (SEC MALS) determines absolute molecular weight independent of retention time.
What it tells you:
- Absolute molecular weight (MW)
- Protein homogeneity
- Presence of oligomers or aggregates
- Mass fraction of main peak
Why it matters:
Confirm oligomerization, detect high molecular weight species, and validate protein integrity.
Why combine nanoDSF, DLS, and SEC MALS?
Each technique examines a different dimension of protein behavior:
- nanoDSF + DLS: thermal + colloidal stability
- DLS + SEC MALS: aggregation detection + confirmation
- All three methods: comprehensive developability assessment
Combining orthogonal techniques enables deeper insight and higher confidence in your results. For example, DLS and nanoDSF together offer complementary views of stability and aggregation, and their combined use offers the greatest value.
Key benefits of our protein characterization services
- End-to-end workflow—Gene synthesis through analysis in one place
- Fast timelines—No need to transfer samples between vendors
- Low sample requirements—Only 12.5 µg to 55 µg per assay
- High-throughput compatible—Scalable for multiple candidates
- Decision-ready data—Clear, quantitative outputs for candidate selection
Applications of protein biophysical characterization
Our services support a wide range of protein and antibody development workflows:
- Antibody developability screening
- Lead candidate selection
- Protein engineering and optimization
- Early formulation studies
- Comparability and biosimilar analysis
What you can learn from your data
Using integrated biophysical characterization, you can:
- Differentiate stable vs. unstable candidates
- Detect early aggregation risks
- Confirm molecular weight and oligomeric state
- Prioritize molecules with the highest developability potential
For example, differences in thermal stability, hydrodynamic radius, and molecular weight can reveal whether a candidate is monomeric and stable or prone to oligomerization and aggregation.
Case study: Orthogonal analysis reveals aggregation risk not seen by thermal stability alone
We compared two well-characterized antibodies using nanoDSF, DLS, and SEC MALS. While both show sufficient thermal stability, Antibody 2 displays clear aggregation behavior and oligomerization, making it a higher-risk candidate.
Antibody 1: Lower-risk profile
- Expected hydrodynamic radius (monomeric)
- Monomeric by SEC MALS
- Sufficient thermal stability
Antibody 2: Higher-risk profile
- Increased hydrodynamic radius (larger species)
- Oligomerization detected by SEC MALS
- Aggregation tendency despite good thermal stability
How the data support the conclusion
Each technique provides a different view of developability. Together, they reveal important differences.
| Antibody 1 (Lower risk) | Antibody 2 (Higher risk) | What the data show | |
|---|---|---|---|
| nanoDSF – Thermal stability Measures unfolding transitions and aggregation onset with increasing temperature. |  |  | Both antibodies show sufficient thermal stability Domain-level melting events (CH2, Fab, CH3) are observed for both antibodies. |
| DLS – Size & Aggregation Measures hydrodynamic radius (rH) and size distribution to detect early aggregation. |  |  | Antibody 2 has increased hydrodynamic radius Larger rH indicates the presence of larger species and aggregation tendency. |
| SEC MALS – Molecular integrity Determines absolute molecular weight and detects oligomers and high-molecular-weight species. |  |  | Antibody 2 shows oligomerization Higher molecular weight species are present, confirming aggregation observed by DLS. |
Conclusion
- Antibody 1 maintains a monomeric profile with expected size and molecular weight, indicating lower developability risk.
- Antibody 2 exhibits aggregation tendencies and oligomerization, making it a higher-risk candidate to pursue.
Key takeaway
Combining orthogonal biophysical methods provides the most complete assessment of protein developability and enables confident, data-driven decisions earlier in your program.
Frequently asked questions
How much protein is required?
Typical requirements are approximately 12.5 µg for nanoDSF and DLS, and 55 µg for SEC MALS.
Can I select individual assays?
Yes. Each method can be selected individually, though combining assays provides the most comprehensive insight.
When should I use these services?
As early as possible after protein expression to identify developability risks before investing in scale-up.
Start your protein characterization project
Get the data you need to make confident decisions in protein and antibody development.
Featured resources for protein expression services
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