RAS-related Proteins

We offer an extensive panel of KRAS and RAS pathway-related recombinant proteins, including a wide range of clinically relevant KRAS mutants such as G12C, G12D, G12V, G13D, Q61H, Q61L, and A146T. These proteins are available in various tag formats (N-His, C-Avi, or N-GST), truncated or full-length forms, and are primarily expressed in E. coli. Key regulatory proteins such as SOS1/2 and CRAF are also available to support RAS pathway research from target validation to drug development.

KRAS Biochemical Assays

Assay Notes and Abbreviations 

All assays listed above are based on TR-FRET (Time-Resolved Förster Resonance Energy Transfer) technology. 

1. PPI (Protein–Protein Interaction): Assays that measure direct binding between RAS proteins and partners such as SOS1, SOS2, or cRAF RBD. 

2. NEA (Nucleotide Exchange Assay): Functional assays evaluating the conversion of RAS from GDP-bound to GTP-bound state, typically triggered by SOS1 in the presence of GTP. 

3. RAS NEA via cRAF*: A functional NEA assay where downstream effector binding (RAF-RBD) is used as the readout for RAS activation, reflecting GTP-loading indirectly.

4. KRAS(ON)/CypA/cRAF Competitive Binding Assay**: A molecular glue-enabled assay that detects whether KRAS forms a ternary complex with Cyclophilin A, displacing native effector cRAF as a result of induced conformational locking.

KRAS SPR Binding Assay Platform

Our SPR assay platform enables detailed kinetic and mechanistic analysis of KRAS-targeting molecules across mutant forms and nucleotide states. 

We support profiling of: 

✅ Direct KRAS binders, 

✅ Tri-complex inhibitor, which stabilize KRAS–Cyclophilin A interactions and prevent effector binding. 

By using validated KRAS proteins (G12D, G12C, G12V, WT, etc.)  in a GDP-bound state, GTP-bound state, GMPPNP-bound state or GppNHp-bound state, our assays quantify binding affinity (KD), rate constants (kon/koff), and conformational selectivity. This platform is optimized for screening and mechanistic validation of molecular glues and next-generation RAS inhibitors.

KRAS Covalent Inhibitor Evaluation

We offer an integrated platform for comprehensive evaluation of covalent KRAS inhibitors, combining intact protein mass spectrometry and kinetic analysis.

Our platform supports:

✅ Covalent adduct identification by high-resolution intact MS, enabling precise detection of protein–inhibitor conjugates and modification ratios.

✅ Time-dependent binding kinetics using multiple inhibitor concentrations and time points to derive quantitative parameters such as kinact/Ki, based on MS signal fitting.

✅ Occupancy-based analysis for accurate modeling of covalent reaction progression, facilitating SAR exploration and compound ranking.

Applicable to KRAS mutants such as G12C, this platform enables reliable characterization of covalent binding efficiency, specificity, and reaction rate—critical for rational development of covalent RAS inhibitors.

RAS Pathway Cell Model Platform

Our RAS pathway platform integrates both advanced in vitro models and in vivo CDX studies, enabling comprehensive profiling of RAS-targeted therapies across key mutation types and tumor contexts.

We offer fixed and customizable KRAS cancer cell panels in both 2D and 3D formats, covering hotspot mutations such as G12C, G12D, G12V, and NRAS, across up to 15 tumor types. These panels enable high-throughput assessment of drug sensitivity, selectivity, and lineage-specific response.

Complementing this, our Ba/F3 isogenic KRAS models express KRAS mutants in a cytokine-dependent system, providing a clean, tractable background for precise evaluation of compound potency and resistance mechanisms.

In vivo, our platform includes a growing library of validated CDX models, derived from human cell lines across multiple cancer types and Ba/F3 cell models. We provide study-ready tumor growth curves, compound sensitivity benchmarks (e.g., AMG510, Dabrafenib), and can support custom CDX establishment or efficacy evaluation.