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Clinical Chemistry 49: 1775-1777, 2003; 10.1373/49.10.1775
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(Clinical Chemistry. 2003;49:1775-1777.)
© 2003 American Association for Clinical Chemistry, Inc.

Abstracts of Oak Ridge Posters

RAMP®: High Accuracy from Immunochromatographic Assays by the Use of Internal Control Ratios

Lynn P. Cloneya, Linda J. Spiller1, Whalley K. Fong1, Joanne E. Harris1 and Paul C. Harris1

1 (Product Development, Response Biomedical Corporation, 8855 Northbrook Court, Burnaby, BC, V5J 5J1 Canada)

aauthor for correspondence: fax 604-412-9830, e-mail lcloney@responsebio.com

The first 20% of the full text of this article appears below.

RAMP® (Rapid Analyte Measurement Platform) is a platform technology that can be adapted to quantify immunologically active substances. The system consists of two components: a disposable test cartridge that houses an analyte-specific immunochromatographic nitrocellulose membrane strip and a portable scanning fluorescence reader that quantifies antibody-antigen complexes. The unique feature of the RAMP technology is that an internal control is run and measured concurrently in every assay, allowing the system to compensate for inherent test-to-test and reader-to-reader variations (1).

In the RAMP System, the test sample is delivered into the sample well of a RAMP test cartridge and the cartridge is inserted into the reader. As the sample migrates along the strip, fluorescently dyed latex particles conjugated to analyte-specific antibodies bind to antigen, if present in the sample. Antigen-bound particles are immobilized at the detection zone by specific antibodies, and some of the excess particles are immobilized at the internal control zone by anti-immunoglobulin antibodies. On completion of the test, the reader measures fluorescence (F-units) emitted by the complexes bound at the detection and internal control zones and calculates a ratio between these measurements.

Immunochromatographic assays are dynamic in nature. In these tests the sample is in contact with the immobilized capture antibodies for only a short time; therefore, the degree of antibody-antigen binding is subject to variability. For any fixed amount of free antigen, the captured signal will increase with longer contact time. This contact time is affected by such factors as capillary speed, sample viscosity, humidity, and temperature (. . . [Full Text of this Article]






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