From Lab Automation to Lab Autonomy. Powered by Polariton's High-End SPR.
Products
R-CLASS
8-Needle Automation via Robot Integration for Scalable SPR Workflows
Designed for AI-driven drug discovery, laboratory automation, and advanced biopharma R&D environments. R-CLASS delivers automated, high-throughput SPR analysis with strong workflow integration for large-scale and data-driven applications.
Consumables
Polariton Life offers sensor chips and consumables designed for reliable, reproducible SPR analysis. They support efficient assay setup and a wide range of interaction analysis applications.
Online ordering for SPR consumables will be available soon.
| PRODUCT NAME | DESCRIPTION |
|---|---|
| Sensor Chip C5 | Preferred chip for ligand immobilization via NH2, SH, CHO, OH, or COOH functional groups |
| Sensor Chip C3 | Features a shorter dextran matrix with similar charge density, suitable for large analytes. |
| Sensor Chip C4 | Similar to a dextran matrix but with lower carboxymethyl density, suitable for samples with highly positively charged analyte. |
| Sensor Chip C1 | Matrix-free carboxymethylated surface for multivalent or large-particle samples. |
| Sensor Chip C7 | High ligand loading capacity, suitable for small molecules, fragment compounds, and other samples requiring high immobilization levels. |
| NTA Sensor Chip | Designed for immobilization of His-tagged molecules and used together with the His Capture Kit. |
| Sensor Chip SA | Streptavidin coated surface enabling high affinity immobilization of biotinylated ligand. |
| Sensor Chip PA | Protein A coated surface binding IgG antibodies from many mammals through the Fc region |
| Sensor Chip PG | Protein G binds various IgG antibodies including human, mouse, rabbit, guinea pig, goat, sheep, and bovine |
| Sensor Chip PL | Protein L captures antibody fragments such as Fab, scFv, kappa light chain subtypes 1, 3, 4, and domain antibodies |
| Maintenance Chip | Dedicated chip for instrument fluidic system cleaning and maintenance |
| Human Antibody Capture Kit | For reversible capturing of humanized antibody Fc domains, enabling over 500 regeneration cycles. |
| Mouse Antibody Capture Kit | For reversible capturing of mouse antibodies, enabling over 500 regeneration cycles. |
| Rabbit Antibody Capture Kit | For reversible capturing of rabbit antibody Fc domains, enabling over 500 regeneration cycles. |
| His-Tag Capture Kit | For reversible capture of His-tagged proteins, enabling over 500 regeneration cycles. |
| RSA Capture Kit | Regenerable streptavidin surface designed for binding biotinylated ligands, with support for over 200 regeneration cycles. |
| Strep-Tag Capture Kit | Capture kit for immobilization of Twin-Strep-tagged molecules, with support for over 200 regeneration cycles. |
Highlights
R.M.S noise < 0.03 RU
Enabling routine analysis within single digit Rmax
Why Low Rmax Matters?
Mass Transport Minimized
Low surface density prevents analyte depletion near the sensor surface, ensuring measured kinetics reflect true molecular behavior.
True 1:1 Kinetics
Reduced ligand density eliminates rebinding artifacts and avidity effects that inflate apparent affinities on crowded surfaces.
No Molecular Weight Limit for Small Molecule Analysis
Polariton SPR delivers exceptional baseline stability and low noise, enabling reliable measurement of Rmax values below 1 RU.
Low Ab Density
Rmax ≈ 2.078 RU
Ultra Low Ab Density
Rmax ≈ 0.699 RU
Ultra Low Ligand Density for Bivalent Interaction
In this study, a biotinylated antigen was captured on a streptavidin (SA) chip as the ligand, and a full-sized antibody was injected as the analyte. To minimize avidity effects from the bivalent antibody, antigen capture was controlled at low ligand density and ultra low ligand density. As a result, antibody binding responses were in the single digit RU range and even below 1 RU. The values were obtained from kinetic fitting using Polaris Evaluation Software. The increase in KD as ligand density was reduced, even at very low ligand levels, highlights the importance of minimizing multivalent interactions in bivalent antibody binding studies.
Low Ultra Low
ka (M⁻¹s⁻¹) 2.97E+6 2.55E+6
kd (s⁻¹) 1.48E-3 3.33E-3
KD (M) 4.99E-10 1.30E-9
Case 1: Methanesulfonamide (95 Da) Binding To CA II
~6,300RU of carbonic anhydrase II was coupled to a C5 chip surface and then a series of concentrations of Methanesulfonamide was injected at 10Hz data acquisition rate, generating small but detectable responses owing to the high sensitivity of the Polariton S-CLASS System. The affinity fit (Langmuir isotherm, inset) yields a KD of 680.2 µM.
Case 2: Furosemide (331 Da) Binding To CA II
Furosemide binding to carbonic anhydrase II for a series of concentrations is shown here. The values obtained for ka, kd, and KD are 6.50E+4 M⁻¹s⁻¹, 3.79E-2 s⁻¹, and 5.83E-7 M respectively from a kinetic fit from Polaris Evaluation Software.
Baseline drift < 0.03 RU/min
High Affinity Antibody – Antigen Interaction Resolved By Ultra-long Dissociation (10000s)
Two high affinity antibodies, mAb1 and mAb2, were studied by capturing the antibody on to an anti-Human Fc chip, injecting the antigen (MW 28.3 kDa) in a series of concentrations, and followed by an injection of regeneration buffer (glycine buffer pH 1.5).
mAb1
mAb2
mAb1 mAb2
ka (M⁻¹s⁻¹) 5.71E+6 8.99E+6
kd (s⁻¹ ) 4.93E-6 2.59E-5
KD (M) 8.62E-13 2.89E-12
Who We Are
We are a team of passionate, driven scientists and engineers dedicated to equipping researchers with the tools to accelerate discovery and advance human health. We have focused that conviction on one problem: making high-end SPR instrumentation accessible to the wider biopharma community.
Our S.P.R. product line — spanning benchtop systems to fully automated platforms — balances high throughput, premium data quality, application versatility, and ease of use, with full compatibility with lab automation in the AI era.
We believe science holds the key to solving the world's most pressing health challenges, and that better tools make better science possible. By putting world-class data within reach of more labs, we aim to empower the scientific community to move faster toward a healthier future for all.
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