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CaptureSelect™ Biotin Anti-LC-kappa (Human) Conjugate

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CaptureSelect™ Biotin Anti-LC-kappa (Human) Conjugate

詳細(xì)介紹

CaptureSelect™ Biotin Anti-LC-kappa (Hu) Conjugate consists of a 13 kDa recombinant single domain antibody fragment (VHH affinity ligand) that specifically binds to the constant domain of human kappa light chains. 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.

The CaptureSelect™ Biotin Anti-LC-kappa (Hu) Conjugate allows you to:

• Detect, quantitate, and characterize all human antibody isotypes and subclasses (for example, IgG1 to 4, IgM, IgA, IgD, and IgE), and Fab fragments thereof, that contain a kappa light chain; as well as recombinant human Fab fragments and/or Fab and Fab2 fragments obtained after papain or pepsin digestion
• Avoid cross-binding with human antibodies that possess a lambda light chain or IgG from bovine sources such as FCS
• Screen antibody-antigen interactions—biotin anti-LC-kappa (Hu) forms a stable [low k(diss)] complex with, for example, human IgG antibodies through bivalent binding

Applications for CaptureSelect™ Biotin Anti-LC-kappa (Hu) Conjugate include ELISA, Western blot, 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).

Free of animal components
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 to 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).

For Research Use Only. Not for use in diagnostic procedures.


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