1. Analyzable molecular interactions include but are not limited to the following four types: binary binding kinetics and affinity analysis; simultaneous ternary complex binding kinetics and affinity analysis; conformation and size changes of protein-nucleic acid molecules; nuclease binding and catalytic constant analysis. Sample types include: proteins, nucleic acids, small molecules, polypeptides, antibodies, and enzymes.
2. Equipped with four single-photon fluorescence counters.
3. Capable of simultaneous dual-color detection for green (525-575 nm) and red (655-685 nm) channels.
4. The automatic sampler is compatible with 96-well and 384-well plates, and can simultaneously accommodate twelve 1.5 mL tubes and three 10.0 mL tubes.
5. Sample injection pump speed range: 1–500 μL/min.
6. Sample chamber temperature control range: 4°C–40°C.
7. Supports automatic chip loading, capable of loading ≥5 chips at a time.
8. Includes four measurement modes: Dynamic Mode, Static Mode, FRET Mode, and Enzyme Activity Assay Mode.
9. Detection limit: ≤10 fM.
10. Affinity (KD) detection range: 50 fM–1 mM.
11. Association rate constant (kon) detection range: 1×10³—1×10⁸ M⁻¹s⁻¹.
12. Dissociation rate constant (koff) detection range: 1×10⁻⁶—30 s⁻¹.
13. Minimum sample consumption: ≤20 μL; effective volume of detection spot: ≤1 nL.
14. Chips are reusable, with typical regeneration cycles ≥20 times and a minimum regeneration time of ≤7 minutes.
15. Chips are equipped with NFC functionality; the chip status, usage times, applicable reagents, etc., can be directly tracked via a mobile APP.
16. The software is equipped with a multi-phase fitting algorithm, which can distinguish between Affinity and Avidity.
1. Antibody Drug R&D: Differentiation analysis of Affinity and Avidity for bispecific/multispecific antibodies; evaluation of antibody epitope mapping and multivalent binding synergy; accurate characterization of binding kinetics (kon/koff/Kd) for antibody drugs.
2. PROTAC and Small Molecule Drug R&D: Binding kinetics analysis of PROTAC-mediated target protein-ubiquitin ligase ternary complexes; binary/ternary interaction screening and activity evaluation of small molecule inhibitors/molecular glues; verification of specificity and binding mechanisms for DNA/RNA-binding small molecules.
3. Protein Function and Interaction Research: Analysis of regulatory mechanisms for protein-protein interactions (PPI); dynamic monitoring of protein conformational changes (folding/unfolding, aggregation, ligand-induced conformational alterations); simultaneous analysis of binding kinetics and enzyme activity (kcat, KM) for enzymes (e.g., polymerases, reverse transcriptases, helicases, nucleases).
4. Nucleic Acid and Gene-Related Research: Affinity screening and specificity verification of aptamers; interaction analysis of DNA/RNA origami structures; sensitivity detection of single-nucleotide mismatches; research on transcription factor-nucleic acid binding kinetics; analysis of binding and catalytic efficiency of gene editing-related molecules (e.g., Cas proteins).
5. Biologic Characterization: Evaluation of binding properties between parent antibodies and "warheads" of antibody-drug conjugates (ADC); analysis of binding kinetics and stability of biomolecules such as polypeptides and nanobodies; quantification of synergistic binding effects of multivalent biologics.
6. Nucleic Acid-Modifying Enzyme Research: Simultaneous detection of binding kinetics and catalytic activity for DNA/RNA polymerases, ligases, helicases, etc.; screening of nucleic acid-modifying enzyme inhibitors and analysis of their mechanism of action.
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