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RAS NanoBRET™ Target Engagement Assays

Measure RAS-Compound Affinity and Fractional Occupancy in Live Cells

  • Quantitate compound affinity in live cells for multimeric RAS, including binding via allosteric switch II pocket
  • Profile compound selectivity across RAS variants, including hotspots G12, G13 and Q61
  • Ready-to-use, scalable assays yielding high-quality data
  • Vectors, assays, and thaw-and-use cells available

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RAS NanoBRET™ Target Engagement Assays
RAS Kit/1K
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Measure Engagement at Multimeric RAS in Live Cells

The RAS NanoBRET™ Target Engagement (TE) Assay is a novel method for studying the small GTPase RAS family, the most frequently mutated protein in cancer. Based on bioluminescence resonance energy transfer (BRET) technology, the RAS NanoBRET™ TE Assay can be used to measure compound affinity and fractional occupancy for multiple RAS variants in live cells. However, unlike previous NanoBRET™ TE Assays that utilize NanoLuc® luciferase, the RAS assay utilizes the Promega NanoBiT® Protein:Protein Interaction (PPI) System to measure cellular target engagement at RAS protein complexes.

How It Works

The RAS NanoBRET™ TE Assay utilizes the Promega NanoLuc® Binary Technology (NanoBiT®) PPI System to measure cellular target engagement at protein complexes. The NanoBiT® PPI System is structural complementation reporter that consists of two optimized subunits of the bioluminescent NanoLuc® Luciferase, LgBiT and SmBiT, which are fused to target proteins of interest. When these proteins interact, an active bioluminescent enzyme is reconstituted. When a NanoBRET™ Tracer binds one of these proteins in the complex, a BRET signal results. Using this approach, the RAS NanoBRET™ TE Assay quantifies compound affinity and fractional occupancy to RAS multimers.

A.
NanoBRET™ TE Assay using a NanoLuc®-tagged target protein.

B.
NanoBRET™ TE Assay using the NanoBiT® complementation reporter.

C.
NanoBRET™ TE RAS Assay uses the NanoBiT® system.

Applying NanoBRET™ target engagement to protein targets. Panel A. The initial NanoBRET™ TE Assays use a NanoLuc®-tagged target protein. BRET results from energy transfer from the target-NanoLuc® fusion protein and a cell-permeable fluorescent tracer inside intact cells. Panel B. The newest iteration of NanoBRET™ TE Assay can measure compound binding at select protein:protein interactions (PPI) by using the NanoBiT® complementation reporter. Panel C. The NanoBRET™ TE RAS Assay uses the NanoBiT® system to measure compound binding at RAS multimers in cells.


Measure Multiple RAS Variants

The RAS NanoBRET™ TE Assay can be used to measure compound cellular affinity and occupancy for multiple RAS proteins, including:

  • KRAS WT and G12 hotspot mutants (A, C, D, S, V)
  • KRAS G13D & Q61 hotspot mutants (H, L, R)
  • HRAS WT and G12 mutants (C & V)

This assay can measure binding of inhibitors known to engage the allosteric switch II pocket of RAS, such as MRTX-849.

A.
Measuring compound binding to KRAS mutants using NanoBRET™ TE RAS Assay.

B.
Measuring compound binding to KRAS WT using NanoBRET™ TE RAS Assay.

C.
Measuring compound binding to HRAS WT using NanoBRET™ TE RAS Assay.

Measuring compound binding to KRAS mutants, KRAS WT and HRAS WT in live cells using the NanoBRET™ Target Engagement RAS Assay.

Patents and Disclaimers

Materials may be covered by pending or issued patents or may have certain limitations.
Information is available upon request and will be included on applicable quotes.

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