Capture Antibody
Capture Antibody - Related Videos
14:48
Conversion of a Capture ELISA to a Luminex xMAP Assay using a Multiplex Antibody Screening Method
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Cited by 53 •
2012
An ELISA can be easily converted to a Luminex xMAP assay and, through the benefits of multiplexing, several antibodies can be screened simultaneously to identify an optimum antibody pair, resulting in increased sensitivity and dynamic range, while reducing assay cost.
04:43
Antibody Conjugated Nanoparticle-based Quantification Using Dark Field Microscopy: A Procedure to Capture and Quantify Specific Exosomes from Body Fluids
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2023
This video describes the use of low-magnification, dark-field microscopy to quantify specific exosomes in small volume biofluidic samples. The exosomes thus identified can serve as potential cancer biomarkers.
04:27
The Virus-Like Particles Capture Assay: A Method to Isolate Antigen-Displaying VLPs from a Sample Using Neutralizing Antibody-Conjugated Magnetic Beads
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2025
In this video, we demonstrate an immunoprecipitation assay, called the VLP capture assay, to isolate antigen-displaying virus-like particles, or VLPs, from a sample. The antigen binds with specific antibodies bound to magnetic beads, forming an immobilized antigen-antibody complex that is later separated and stored for further analysis.
29:02
Cell Capture Using a Microfluidic Device
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Cited by 1 •
2007
12:55
Scalable High Throughput Selection From Phage-displayed Synthetic Antibody Libraries
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Cited by 33 •
2015
A method is described with visual accompaniment for conducting scalable, high throughput selections from phage-displayed combinatorial synthetic antibody libraries against hundreds of antigens simultaneously. Using this parallel approach, we have isolated antibody fragments that exhibit high affinity and specificity for diverse antigens that are functional in standard immunoassays.
FAQs
Selectivity arises from the antibody’s ability to recognize and bind a particular antigen in a complex biological sample. Immobilizing the antibody on a solid surface allows the target to be retained while other sample components remain available for separation from the captured material. This selective retention supports detection of pathogens, toxins, cytokines, and other biomarkers.
The second antibody provides an independent recognition event after the antigen has been retained by the capture antibody. Its interaction with the captured target generates a measurable signal, linking signal intensity to the amount of antigen present. This two-antibody arrangement supports specific antigen quantification rather than relying on capture alone.
The two antibodies perform complementary roles. The capture antibody is immobilized and retains the antigen from the sample, whereas the detection antibody recognizes the retained antigen and contributes to the measurable readout. Using both roles in one assay creates the sandwich format used to quantify immune-related or infectious targets.
A typical workflow begins by immobilizing the capture antibody on a solid surface, followed by exposure to a biological sample so the target antigen can bind. A second antibody is then applied to recognize the retained antigen, and the resulting signal is measured. The signal provides information about the antigen concentration in the sample.
The approach can be applied to serum, cell culture fluid, and clinical specimens, depending on the target and assay design. These samples may contain pathogens, toxins, cytokines, or other immune-related biomarkers. Such flexibility makes capture antibody assays useful for both laboratory studies and investigations involving clinically relevant biological material.
In immunology and infection research, these assays support antigen quantification, diagnostic testing, and disease surveillance. They can also help evaluate host-pathogen interactions by measuring relevant targets in biological samples. The resulting concentration information allows researchers to compare antigen presence or abundance across experimental, clinical, or surveillance contexts.