Antigen-Antibody Interaction Chip

Category
Capture sensor chip

Description
The product consists of 7 IgG-binding domains and its binding capacity is broader than either Protein A or Protein G alone. Native immobilization via Fc-domain affinity. This product combines protein A and protein G to bind a wide range of antibodies from many mammalian species and almost all subclasses of human immunoglobulins. 50, 200, and 500 nm coating thickness.

Feature
High capacity for quantitation of all human IgG subclasses, IgA, IgE, IgM and to a lesser extent IgD; however, it does not bind mouse IgA, IgM or murine serum albumin

Category
Capture sensor chip

Description
Protein A contains four high-affinity binding sites capable of binding lgG (predominantly human) through the Fc-region.

Feature
Optimal binding occurs at pH 8.2, although binding is also effective at neutral or physiological conditions (pH 7.0 to 7.6)

Category
Capture sensor chip

Description
Recombinant fusion protein A/G (Mw around 50 kDa) is pre-immobilized in a 3-dimensional hydrogel consisting of a linear polycarboxylate with higher flexibility in its polymer chains than carboxymethyldextran. Recombinant fusion protein A/G (Mw around 50 kDa) is pre-immobilized in a 3-dimensional hydrogel consisting of a linear polycarboxylate with higher flexibility in its polymer chains than carboxymethyldextran. Recombinant protein A/G on these sensor chips consists of seven IgG-binding domains (EDABC–C2C3); the protein A portion (segments E, D, A, B, and C) is from Staphylococcus aureus, and the protein G portion (segments C2 and C3) is is a Streptococcal cell wall protein.

Feature
Sensor surfaces with protein A/G are designed to bind antibodies (IgGs) from different subclasses and species through the heavy chain in the Fc region

Category
Capture sensor chip

Description
His-tagged molecules are immobilized via Ni2+/NTA chelationimple and surface regeneration is done by injecting EDTA or imidazole. 200 nm coating thickness.

Feature
Binding is reversible and his-tagged ligand can be removed using a chelating agent (e.g. EDTA)
Results in an oriented capture
High capacity for histidine-tagged molecules such as recombinant proteins

Category
Capture sensor chip

Description
The binding of NeutrAvidin to biotin is one of the strongest non-covalent interactions. Minimal biotinylation of the ligand and subsequent capture on a NeutrAvidin chip results in a more oriented arrangement of ligand molecules on the surface as compared to the more random arrangement from chemical immobilization such as amine coupling.

Feature
Minimal biotinylation of the ligand and subsequent capture results in a more oriented arrangement of ligand molecules on the surface
This surface is used for the high-affinity capture of biotinylated molecules such as proteins, peptides, and nucleic acids

Category
Capture sensor chip

Description
The interaction between streptavidin and biotin results in a high-affinity biomolecular interaction with negligible dissociation of the ligand from the sensor chip surface, making it an ideal choice for high-capacity, reproducible SPR experimentation. Minimal biotinylation of the ligand and subsequent capture on a Streptavidin/Dextran chip results in a more oriented arrangement of ligand molecules on the surface as compared to the more random arrangement from chemical immobilization such as amine coupling and also offers a higher capacity than a planar chip.

Feature
Medium to high capacity for biotinylated ligand captures
Binding resistant to a wide range of conditions including heat, pH, and proteolysis
This surface is used for the high-affinity capture of biotinylated molecules such as proteins, peptides, and nucleic acids

Category
Capture sensor chip

Description
The binding of Streptavidin to biotin is one of the strongest non-covalent interactions. This high-affinity streptavidin (SA) sensor chip immobilizes biotinylated molecules for SPR interaction analysis. Streptavidin covalently immobilized on a planar mSAM surface.

Feature
Lower capacity for biotinylated ligand kinetic lawns
Use for the capture of biotinylated molecules such as proteins, peptides, and nucleic acids

Category
Covalently coupled biosensor chip

Description
Carboxymethyl dextran surfaces are very stable and resistant to the non-specific binding of biomolecules. The dextran layer is in the form of a highly flexible non-cross-linked brush-like structure extending 100 to 200 nanometers from the surface. The flexible nature of the dextran contributes to the accessibility of binding sites on an immobilized ligand. Planar carboxymethyl dextran coating (less than 5 nm) allows the immobilization of ligands in a single monolayer.

Feature
2D planar carboxymethyldextran surface, <5nm coating thickness
Covalent coupling
Recommended for the binding of high molecular weight analytes such as antibodies or nanoparticles
The CMDP coating is also suitable for particulate analytes, such as viruses and whole cells

Category
Covalently coupled biosensor chip

Description
Polycarboxylate hydrogel sensor chip. 150nm coating thickness.

Feature
Use for large/medium sized molecules and low molecular weight molecules
Provides another choice for high capacity coupling when studying protein-small molecule interactions or when dextran is not ideal

Category
Covalently coupled biosensor chip

Description
Flat surface modified with polyethylene glycol (PEG) attached to an alkanethiol monolayer. In addition, carboxyl functional groups enable ligand attachment and amine coupling. By utilizing EDC/NHS chemistry, amine coupling is the most common ligand immobilization approach but thiol, aldehyde, and maleimide coupling are also possible with this surface using the appropriate cross-linking chemistry.

Feature
Enabling interaction analysis that cannot otherwise be performed on dextran-based surfaces
Use for large/medium sized molecules along with viruses and cells