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Protein Interactions

We offer a number of products for the analysis of protein interactions, including pull-down assays, BRET-based and complementation reporter-based systems.

GST pull-down systems are used in traditional methods based on cell extracts and/or cell-free expression. The HaloTag® Mammalian Pull-Down System is used to isolate and identify intracellular protein complexes from mammalian cells.

NanoBRET™ and NanoBiT® technologies provide methods for direct analysis of protein interactions in live cells. The NanoBRET™ System uses bioluminescence resonance energy transfer (BRET) in a proximity-based assay that detects protein interactions by measuring energy transfer from a bioluminescent protein donor to a fluorescent protein acceptor.

NanoBiT® assays rely on a two-subunit system based on NanoLuc® luciferase that can be used for intracellular detection of protein:protein interactions. The subunits are fused to proteins of interest, forming a functional enzyme that generates a bright, luminescent signal when the proteins interact.
Learn about Protein Interactions
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Protein Interactions Product Groups

Live-Cell Protein Interactions

BRET and complementation reporter methods for detection of protein interactions close to endogenous expression levels.

Protein:DNA Interactions

Products to capture and assess the interaction of transcription factors and other proteins with DNA.

Pull-Down and Two-Hybrid Systems

Resin- and magnetic-based systems for isolating GST or HaloTag fusion proteins.

Lumit® Anti-Tag PPI Reagents

Homogeneous assay to measure protein-protein or protein-small molecule interactions involving tagged proteins.

Top Protein Interactions Products for Your Lab

HaloTag® Mammalian Pull-Down Systems

These systems enable rapid capture of simple or complex protein pairs directly from lysates and allow you to go from pull-downs to imaging studies using same construct.

G6509, G6500, G6504, G6591

NanoBiT® PPI Starter Systems

Complementation reporter for detection of protein interactions in live cells.

N2014, N2015, N2016

NanoBRET® PPI Starter Systems

Live-cell protein:protein interaction assay. Includes vectors, controls and detection reagent for BRET-based PPI.

N1811, N1821

Protein Interactions Resources

Resource

NanoLuc® Luciferase: One Enzyme, Endless Capabilities

Paper

A Luminescent Pull-Down Approach for Confirming NanoBRET® Protein Interaction Assays

Resource

Characterize and Image Human Mediator Complexes

An Introduction to Protein Interactions

Protein:protein interactions (PPIs) are essential to almost every process in a cell, so understanding PPIs is crucial for understanding cell biology in normal and disease states. There are numerous methods used to characterize protein interactions that use cell extracts or live cells to express potential targets.

In a pull-down assay, one protein partner is expressed as a fusion protein (e.g., bait protein) in E. coli and then immobilized using an affinity ligand specific for the fusion tag. The immobilized bait protein can then be incubated with the prey protein.

Co-immunoprecipitation is another option to study protein:protein interactions. To perform co-immunoprecipitation, an antibody against a target protein is coupled to Sepharose® beads through protein A or G, and then the complexes containing the target protein are immunoprecipitated with the antibody-coupled beads.

However, these traditional methods for studying interactions between proteins do not provide data directly in the context of a cellular environment. Using Bioluminescence Resonance Energy Transfer (BRET) or complementation assays, it is possible to quantitatively measure the interaction between proteins in live cells.

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