Hibit Bioreporter
Hibit Bioreporter - Related Videos
03:11
Bioreporter Assay: A Sensitive Technique using a Bioluminescent Reporter System to Detect SARS-CoV-2 Antibodies
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2025
In this video, we show the HiBit-RBD bioreporter system-based assay for detecting SARS-CoV-2 neutralizing antibodies. This system targets the viral RBD domain by using a bioluminescent reporter system containing HiBiT fused to the RBD domain.
07:44
Detection of SARS-CoV-2 Receptor-Binding Domain Antibody using a HiBiT-Based Bioreporter
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Cited by 2 •
2021
The outlined protocol describes the procedure for producing the HiBiT-receptor-binding domain protein complex and its application for fast and sensitive detection of SARS-CoV-2 antibodies.
02:36
The Luciferase Assay: A High-Throughput Assay to Measure Luminescent Signals Using Engineered Nanoluciferase System-Based Bioreporters
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2025
The video demonstrates the luciferase assay used to quantify luciferase-tagged proteins. The assay uses an engineered luciferase enzyme composed of a large fragment that binds with the small fragment, which is conjugated with a protein of interest. The bound subunits form an active enzyme that, in the presence of the substrate, releases a luminescent signal. This signal is then quantified using a luminometer.
05:33
High-Throughput Cellular Profiling of Targeted Protein Degradation Compounds Using HiBiT CRISPR Cell Lines
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Cited by 27 •
2020
This protocol describes the quantitative luminescent detection of protein degradation kinetics in living cells that have been engineered using CRISPR/Cas9 to express antibody free endogenous protein detection tag fused to a target protein. Detailed instructions for calculating and obtaining quantitative degradation parameters, rate, Dmax, DC50, and Dmax50 are included.
13:16
A Whole Cell Bioreporter Approach to Assess Transport and Bioavailability of Organic Contaminants in Water Unsaturated Systems
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Cited by 5 •
2014
A whole cell bioreporter assay with Burkholderia sartisoli RP037-mChe was developed to detect fractions of an organic contaminant (i.e., fluorene) available for bacterial degradation after active transport by mycelia bridging air-filled pores in a water unsaturated model system.
FAQs
The genetically attached HiBiT peptide combines with its complementary LgBiT component when both are present with the required substrate. This reconstitutes an active luciferase, producing light that reflects the amount or activity of the tagged protein. Because the signal is luminescent and quantitative, researchers can follow changes in living cells rather than relying only on endpoint measurements.
HiBiT is compact, which can reduce disruption of the protein being examined compared with a larger reporter attachment. That feature is important when the target must retain its normal abundance, trafficking, degradation, or interaction behavior. Maintaining more native-like protein behavior can make measurements of immune signaling and pathogen-host processes more representative of the underlying biology.
The system can be adapted to track several distinct protein behaviors, including changes in abundance, movement within the cell, degradation, and interactions between pathogen-associated and host proteins. These readouts allow investigators to examine how infection affects immune pathways over time. The same platform therefore supports both protein-level monitoring and analysis of host-pathogen biological events.
A typical measurement requires a protein of interest genetically fused to the HiBiT peptide, the complementary LgBiT component, and the substrate needed for luciferase activity. These elements are combined in living-cell assays so that reporter assembly produces a measurable light output. The resulting signal can then be used to quantify changes in the tagged protein or its behavior.
Researchers can tag proteins involved in host immune pathways or pathogen-host interactions and monitor their behavior while cells remain viable. Measurements may reveal changes in protein abundance, trafficking, degradation, or interaction state during infection-related events. This approach connects molecular protein dynamics with immune responses and can provide quantitative data for comparing experimental conditions.
The method is useful when experiments require sensitive measurements in living cells, repeated monitoring over time, or analysis of many conditions. Its luminescent output supports real-time assays, while the compact tag and quantitative signal help preserve target-protein behavior and enable higher-throughput analysis. These properties make it suitable for screening how infection-related conditions alter cellular proteins.