Products | SPR Sensor chips | Data sheets

HC–modified sensor chips

XanTec’s HC sensor chips are based on a 2D (HCP) or 3D hydrogel matrix composed of highly flexible, bioinert polycarboxylate chains grafted onto a hydrophilic adhesion promoter on a gold support. Ligands can be covalently attached through their amine, thiol, or aldehyde groups using established coupling chemistries such as EDC/NHS activation, thiol-maleimide coupling, or reductive amination. This versatility enables the immobilization of a wide range of biomolecules including proteins, antibodies, peptides, nucleic acids, carbohydrates, and small organic compounds.

The HC sensor chip portfolio spans electrostatic immobilization capacities from a few thousand μRIU (HCP) to ≈ 55,000 μRIU (HC1500M), covering analytes from large viruses to small organic fragments. The HC polycarboxylate matrix is more flexible and less bulky than carboxymethyl-dextran coatings, occupying a smaller fraction of the evanescent field. Its strongly hydrated polymer brush makes the surface highly bioinert and minimizes nonspecific binding. This combination provides high immobilization capacity with excellent diffusion properties, making HC chips a preferred alternative to CMD-based sensor surfaces in biochemical research, assay development, quality control, trace analysis, and drug discovery.

Key features:

Schematic illustration of a 2D HCP (left) and a 3D HC (right) sensor chip. Red dots indicate the negatively charged carboxyl groups distributed along the green polymer chains. The decaying red gradient represents the evanescent field.1
Product code 2 HCP HC30M HC200M HC1500M
Base coating 2D, ultra-short bioinert polycarboxylate (high density) 3D, 30 nm bioinert polycarboxylate (medium density) 3D, 200 nm bioinert polycarboxylate (medium density) 3D, 1500 nm bioinert polycarboxylate (medium density)
Immobilization capacity [µRIU] 3 ≈ 5,000 ≈ 19,000 ≈ 33,000 ≈ 55,000
Recommended ligands
  • proteins
  • peptides
  • nucleic acids
  • carbohydrates
Recommended analytes
  • proteins
  • peptides
  • nucleic acids
  • viruses and cells
  • carbohydrates
  • proteins
  • peptides
  • nucleic acids
  • small molecules
  • carbohydrates
  • peptides
  • nucleic acids
  • small molecules
  • carbohydrates
  • small molecules
  • fragments
  • short nucleic acids
  • small carbohydrates
Intended purpose
  • kinetics of medium and large analytes
  • especially suitable for weak binders with fast on- and off-rates
  • applications requiring lowest diffusion limitation possible
  • all-purpose
  • kinetics of small, medium, and large analytes
  • especially suitable for weak binders with fast on- and off-rates
  • applications requiring very low diffusion limitation
  • immobilization of secondary antibodies and capture proteins
  • all-purpose
  • kinetics of medium and small analytes
  • equilibrium analysis
  • concentration analysis
  • immobilization of secondary antibodies and capture proteins
  • kinetics of small analytes
  • fragment-based drug discovery
  • affinity and concentration analyses
  • immobilization of capture proteins

1 All illustrations are schematic representations and are not drawn to scale; dimensions, densities, and spatial relationships do not reflect actual physical or chemical proportions.

2 This overview represents a selection of the full HC sensor chip portfolio.

3 Preconcentration capacity determined by injecting 100 µg/mL bovine serum albumin (BSA) in 5 mM sodium acetate pH 5.0, with 1 µRIU corresponding approximately to 1 RU. Maximum covalent coupling yields can vary and depend strongly on the properties of the protein to be immobilized. Under optimal conditions, typical coupling efficiencies range from approximately 20–45% of the respective electrostatic preconcentration capacity, with acidic proteins generally exhibiting lower coupling efficiencies.