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RNA EMSA Assay Kits

Clean Visual Validation of RNA-Protein Interactions

RNA-binding proteins (RBPs) are essential regulators of gene expression, controlling mRNA splicing, stability, and non-coding RNA processing (miRNAs/lncRNAs). Dysregulation of these pathways drives numerous diseases, making RBP validation vital for functional genomics and target discovery.

The Electrophoretic Mobility Shift Assay (EMSA) is the gold standard for verifying direct RBP-RNA interactions. Running complexes on a native gel provides clear visual validation of binding specificity, affinity, and multi-protein assembly.

Principle 

The assay is based on the fact that RNA-protein complexes migrate more slowly through a non-denaturing polyacrylamide gel than free RNA probes.

  1. Binding Reaction: A biotin-labeled RNA probe is incubated with a purified protein or nuclear/cytoplasmic extract.

  2. Electrophoresis: The mixture is resolved on a native gel. Free probes migrate quickly to the bottom, while bound RNA-protein complexes are retarded ("shifted") higher in the gel.

  3. Detection: The gel is transferred to a membrane and visualized using an optimized, ultra-sensitive chemiluminescent substrate.

  4. Specificity Control: Specificity is confirmed by adding an excess of unlabeled ("cold") competitor probe, which prevents the formation of the shifted biotin-labeled complex.

Benefits

Universal  Compatibility

Validated for human, mouse, rat, and all other mammalian samples—ideal for translational research.

Safe, Non-Radioactive

Matches traditional radioactive sensitivity while eliminating regulatory burdens, hazards, and disposal costs.

Pre-Validated

Probe Pairs

Includes a biotin-labeled "hot" probe and an unlabeled "cold" competitor, enabling immediate specificity controls without oligo design.

Comprehensive Insights

Easily characterize binding dynamics, measure competition, and visualize multi-protein supershifts.

Ultra-Sensitive Chemiluminescence

Combining an optimized workflow with a highly sensitive substrate ensures clear detection of low-abundance RBPs and weak interactions.

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