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Thermo Scientific™ CaptureSelect™ Biotin Anti-IgE Conjugate
Tienda Thermo Scientific ProductosCódigo de producto. 18436498
Marca: Thermo Scientific™ 7103542100
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Descripción
CaptureSelect Biotin Anti-IgE Conjugate consists of a 13-kDa recombinant single domain antibody fragment (VHH affinity ligand) that specifically binds with high affinity and selectivity to human IgE (immunoglobulin E) from recombinant and plasma sources. The Anti-IgE affinity ligand targets the Fc region (CH4 domain) of human IgE antibodies independent of the light chain subclass.
The affinity ligand is chemically conjugated to biotin via an appropriate spacer that retains the binding reactivity of the ligand when used in combination with streptavidin-based conjugates or streptavidin pre-coated surfaces. This conjugate allows you to detect, quantitate, and characterize native and recombinant human IgE antibodies.
Applications for CaptureSelect Biotin Anti-IgE Conjugate include ELISA, immunoprecipitation with streptavidin-coupled Dynabeads, Gyrolab™-based immunoassays, and label-free detection platforms such as those based on surface plasmon resonance (Biacore™ and IBIS-MX96 systems) and bio-layer interferometry (ForteBio™ Octet™ systems).
Animal origin statement
CaptureSelect products contain affinity ligands based on recombinant single-domain antibody fragments (VHH) created by a proprietary technology. The VHH affinity ligand is a 12–15 kDa fragment comprising the three complementarity-determining regions (CDRs) that form the antigen-binding domain, efficiently produced in the yeast Saccharomyces cerevisiae by a production process free of any animal components (Animal Origin-Free).
Especificaciones
Especificaciones
| Contenido y almacenamiento | Store in freezer (-5°C to -30°C). |
| Condiciones de envío | Dry Ice |
| Formulario | Líquido |
| Línea de productos | CaptureSelect |
| Cantidad | 100 μg |
| Tipo | Conjugate |
| Etiqueta o tinte | Biotin & Analogs |
Para uso exclusivo en investigación. No apto para uso en procedimientos diagnósticos.
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