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Product Details
FAB
- Comprehensive validation - Validated with various antibody subtypes and antibody drugs.
- Simple and fast operation - No complicated washing steps, significantly reducing time.
- High batch consistency - Strict control over raw materials and finished product quality, ensuring a stable supply.
- Accurate and reliable results - High sensitivity with minimal matrix effects.
- High throughput capability - Support multiple product specifications, ideal for high-throughput screening.
- Fast completion - Results in just 1 hour.
Product Specifications
Assay TypeCompetition-TR-FRETReactivityHumanRegulatory StatusRUOAssay Time1 hrSample volume10 μLProduct Overview
The Human Fc gamma RIIIA / CD16a (V176) binding Kit (TR-FRET) is based on a homogeneous (no wash) competition TR-FRET technology (Time-Resolved Fluorescence Resonance Energy Transfer) to measure the interaction between human CD16a (V176) and antibody drug candidates or CD16a (V176) inhibitors. It is designed to facilitate the ADCC functional performance evaluation of antibody drug candidates, high-throughput screening of CD16a (V176) inhibitors within 0.5-1 hours. It can also be used as a universal detection tool to identify the ability of antibody drugs to bind to human CD16a (V176).
Storage
1. Unopened kit should be stored at 2℃-8℃ upon receiving.
2. Find the expiration date on the outside packaging and do not use reagents past their expiration date.
3. The opened kit should be stored per components table. The shelf life is 30 days from the date of opening.
Materials Provided
IDComponentsSizeFRT07-C01Human Fc gamma RIIIA / CD16a (V176) Protein Europium-chelate100 tests/500 testsFRT07-C02FA labeled human IgG antibody100 tests/500 testsFRT07-C03Human IgG Standard400 μg/100 tests 2 mg/500 testsDB-04TR-FRET Sample Dilution Buffer, pH7.450 mL/100 tests & 500 testsDB-05TR-FRET Detection Buffer, pH7.450 mL/100 tests & 500 testsAssay Principles
This Human Fc gamma RIIIA / CD16a (V176) binding Kit (TR-FRET) is based on TR-FRET technology (Time-Resolved Fluorescence Resonance Energy Transfer). This assay uses the mixture of biotinylated Fc gamma RIIIA / CD16a (V176) and Europium-chelate labeled streptavidin as the Donor and FA labeled human IgG antibody as the Acceptor.
— When the sample does not contain human Fc gamma RIIIA / CD16a (V176) binding components, the Donor and Acceptor are in close proximity because of the binding of human Fc gamma RIIIA / CD16a (V176) and human IgG antibody. Upon Donor excitation with light of a specific wavelength (337nm), in addition to Donor emission (620nm), non-radiative transfer of energy occurs between Donor and Acceptor, resulting in Acceptor emission (665nm).
— When the sample contains human Fc gamma RIIIA / CD16a (V176) binding components, the components inhibit the binding between the Donor and Acceptor and thereby prevent FRET from occurring.
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Performance Data
Bioactivity-TR-FRET
Please refer to DS document for the assay protocol.
In this TR-FRET assay, Human Fc gamma RIIIA / CD16a (V176) Protein Europium-chelate is used as the Donor and FA labeled human IgG antibody is used as the Acceptor. An inhibition Assay was performed to evaluate the interaction between Human Fc gamma RIIIA / CD16a (V176) Protein Europium-chelate and FA labeled human IgG antibody using Human IgG standard resulting in a typical IC50 of 447.9 nM (QC tested).
The kit can be used to detect different subclasses of human IgG (human IgG1, human IgG2, human IgG3 and human IgG4). As shown in the figure, human CD16a (V176) is a high-affinity receptor that binds to human IgG1 and human IgG3, while it shows lower affinity for human IgG2 and human IgG4.
The kit has been used to detect different subclasses of mouse IgG (mouse IgG1, mouse IgG2a and mouse IgG2b), which exhibit different IC50 results. As shown in the figure, human CD16a (V176) binds to mouse IgG1, mouse IgG2a and mouse IgG2b with a low affinity.
This kit was used to evaluate four FDA-approved antibody drugs with different affinities for human CD16a (V176). Bevacizumab and Efgartigimod alfa bind to human CD16a (V176) with high affinity. Toripalimab shows no binding to this receptor. The Fc region of Eculizumab has been modified into the human IgG2 hinge region and the human IgG4 CH2-CH3 region, so it doesn’t bind to human CD16a (V176).
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Drug Development Progress- English Name：
Low affinity immunoglobulin gamma Fc region receptor III-A
- Category：
- Approved Drugs：
0 Details
- Drugs in Clinical Trials：
14 Details
- Highest Development Stage：
Phase 2 Clinical
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