G3BP antibodies target the Ras GTPase-activating protein-binding protein (G3BP) family, comprising G3BP1 and G3BP2. which are multifunctional RNA-binding proteins involved in stress granule (SG) formation, RNA metabolism, and cellular stress responses. These proteins contain conserved domains, including an N-terminal nuclear transport factor 2 (NTF2)-like domain, an RNA recognition motif (RRM), and acidic and proline-rich regions, enabling interactions with RNAs, proteins, and signaling molecules. G3BP1. the better-characterized isoform, acts as a scaffold for SGs—dynamic cytoplasmic aggregates formed during stress to sequester untranslated mRNAs and regulate translation. It also modulates Ras signaling, antiviral immunity, and cell proliferation.
G3BP antibodies are widely used to study SG dynamics, particularly in neurodegenerative diseases (e.g., ALS, Alzheimer’s) and cancer, where dysregulated SG assembly correlates with pathology. They enable detection of G3BP expression/localization via techniques like Western blotting, immunofluorescence, and immunoprecipitation. Some viruses exploit G3BP to disrupt SGs, facilitating replication, making these antibodies valuable in virology research. Additionally, G3BP antibodies help investigate post-translational modifications (e.g., phosphorylation) that regulate its functions. Their specificity varies; some distinguish G3BP1 from G3BP2. while others cross-react. Overall, G3BP antibodies are critical tools for exploring cellular stress adaptation, RNA biology, and disease mechanisms.