Advanced search×

Capillary electrophoresis-based immunoassays: principles and quantitative applications.

Electrophoresis 29(16):3279-95 (2008) PMID 18646279

The use of CE as a tool to conduct immunoassays has been an area of increasing interest over the last decade. This approach combines the efficiency, small sample requirements, and relatively high speed of CE with the selectivity of antibodies as binding agents. This review examines the various assay formats and detection modes that have been reported for these assays, along with some representative applications. Most CE immunoassays in the past have employed homogeneous methods in which the sample and reagents are allowed to react in solution. These homogeneous methods have been conducted as both competitive binding immunoassays and as noncompetitive binding immunoassays. Fluorescent labels are most commonly used for detection in these assays, but enzyme labels have also been utilized for such work. Some additional work has been performed in CE immunoassays with heterogeneous methods in which either antibodies or an analog of the analyte is immobilized to a solid support. These heterogeneous methods can be used for the selective isolation of analytes prior to their separation by CE or to remove a given species from a sample/reagent mixture prior to analysis by CE. These CE immunoassays can be used with a variety of detection modes, such as fluorescence, UV/Vis absorbance, chemiluminescence, electrochemical measurements, MS, and surface plasmon resonance.

DOI: 10.1002/elps.200700871
Version: za2963e q8za9 q8zb9 q8zc1 q8zda q8ze9 q8zf9 q8zg5

Similar articles you may find interesting…

  1. Evolving concepts of specificity in immune reactions.

    Audio, Transactions of the IRE Profes... 107(52):22373-80 (2010) PMID 21173256

    We critically consider the mechanistic bases for this specificity/degeneracy enigma and also compare and contrast Ag recognition by Abs and TCRs....
  2. Interdisciplinary research: Big science at the table.

    Nature 468(7327):S2-4 (2010) PMID 21179080

  3. Structures of the CXCR4 chemokine GPCR with small-molecule and cyclic peptide antagonists.

    Science 330(6007):1066-71 (2010) PMID 20929726

    We report five independent crystal structures of CXCR4 bound to an antagonist small molecule IT1t and a cyclic peptide CVX15 at 2.5 to 3.2 angstrom resolution. All structures reveal a consistent homodimer with an interface including helices V and VI that may be involved in regulating signaling. The...