In early discovery stages, aptamers are often evaluated primarily by apparent affinity. However, as programs advance toward application-driven validation, limitations frequently surface:
Comprehensive characterization mitigates these risks by generating an integrated performance profile. This approach enables informed go/no-go decisions, rational optimization, and smooth handoff to formulation, assay development, or therapeutic engineering workflows.
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Our platforms consist of four tightly coordinated service modules. Each module can function independently or as part of a full characterization pipeline, depending on project scope and development stage.
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Our platform supports a wide range of research scenarios, including:
Aptamer-based diagnostic and biosensor development
Biomarker validation and detection assay optimization
Comparative evaluation of aptamer libraries or variants
Pre-optimization studies prior to chemical modification or conjugation
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| Stage | What We Do | What You Provide |
| Consultation & Study Design | Clarify target context, application scenario, module selection | Aptamer info (sequence/modifications), target info, intended use |
| Sample Review & Readiness Check | Confirm sample compatibility and assay feasibility | Aptamer sample + target material (or specs) |
| Experimental Execution | Run selected module assays under defined conditions | |
| Cross-Module Analysis | Integrate structure/binding/stability/competition interpretation | |
| Reporting & Discussion | Deliver report and walk through outcomes | Feedback/next-stage goals |
Design Your Workflow
The Selection and Characterization of A Novel ssDNA Aptamer Targeting Carcinoembryonic Antigen
Carcinoembryonic antigen (CEA), a well-known cancer biomarker that is used to diagnose various cancers, notably colorectal cancer, was used as a target to select and characterize single-stranded DNA aptamers. In this study, SELEX and NGS techniques were employed in the aptamer selection processes. Aptamer characterization techniques, such as enzyme-linked oligonucleotide assay (ELONA), dot blot, and bioinformatics assays, were conducted to observe the affinity binding of the selected aptamer to the target protein.
Fig.1 Schematic overview of CEA aptamer selection and characterization.1,2
References
Yes. All modules are fully modular. Clients may choose individual services based on immediate research needs or integrate multiple modules into a comprehensive workflow. Many projects begin with one module and expand as development progresses.
Basic affinity testing provides a single snapshot of binding strength. Our platform expands beyond that by analyzing kinetics, stability, structural integrity, and competitive behavior, offering a multidimensional understanding of aptamer performance that is critical for downstream reliability.
Absolutely. We routinely characterize chemically modified, labeled, and application-specific aptamers. Experimental conditions and analytical approaches are adjusted to accurately assess how modifications impact folding, binding, stability, and specificity.
Yes. Comparative characterization is one of the most common use cases. Multiple aptamers can be evaluated under identical conditions, enabling objective ranking and evidence-based candidate prioritization.
Where appropriate, assays can be conducted under conditions that mimic physiological or application-specific environments, such as defined ionic strength, temperature ranges, or buffer systems, to enhance translational relevance.
Each project includes a structured, presentation-ready report with experimental summaries, module-specific results, integrated interpretation, and application-oriented conclusions. Reports are designed to support internal review, decision-making, and downstream planning.
Yes. By correlating structural features with binding behavior, stability, and competition outcomes, our data often highlights specific optimization opportunities—such as sequence refinement, modification strategy adjustments, or condition tuning—reducing reliance on trial-and-error approaches.
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