G3BP1 Antibodies

Background

G3BP1 (Ras GTPase activator protein binding protein 1) is a widely expressed multi-domain RNA-binding protein, which mainly participates in the regulation of cellular stress response as a core assembly factor of stress particles. This protein mediates liquid-liquid phase separation through its NTF2-like domain, drives the aggregation of messenger ribonucleoproteins under stress conditions to form membrane-free organelles, thereby regulating the stability, translation and degradation processes of mRNA. In the study of viral infection, G3BP1 has been confirmed to be a key host factor of multiple RNA viral replication complexes, and its phosphorylation status directly regulates the antiviral innate immune response. As an important molecular hub of cellular stress pathways, the abnormal expression of G3BP1 is closely related to tumorigenesis, neurodegenerative diseases and autoimmune diseases. The study of its structure and function provides an important molecular basis for revealing post-transcriptional regulatory mechanisms and developing targeted therapies.

Structure Function Application Advantage Our Products

Structure of G3BP1

G3BP1 is a multi-domain RNA-binding protein with a molecular weight of approximately 52 kDa. This protein is highly conserved among different species, and the differences in its molecular weight mainly result from the variations in amino acid sequences within the regulatory domain.

Species	Human	Mouse	Zebrafish	African clawed toad	Fruit fly
Molecular Weight (kDa)	52.1	51.8	50.9	51.5	49.7
Primary Structural Differences	Contains NTF2-like domains, RGG boxes, and RRM domains	The NTF2 domain is highly conserved	RGG box sequence variation	RRM structure domain function	Simplify the composition of the domain structure

G3BP1 is composed of 466 amino acids and forms a dimer through its N-terminal NTF2-like domain, driving liquid-liquid phase separation. This protein contains two RNA recognition motifs (RRM) and an arginine-glycine-glycine (RGG) -rich region, which jointly coordinate its binding to the target mRNA. Among them, RRM1 is responsible for specifically recognizing nucleic acid sequences, while the RGG region at the C-terminal promotes multivalent binding through weak electrostatic interactions. Under stress conditions, these domains act in synergy to cause conformational changes in G3BP1, exposing hydrophobic regions and thereby initiating the assembly process of stress particles.

Fig. 1 Domain architecture of G3BP1.¹

Key structural properties of G3BP1:

Multi-domain modular architecture
Intrinsic disordered regions mediate phase separation
Conservative nucleic acid binding interface and regulatory switch

Functions of G3BP1

The main function of G3BP1 is to act as a core assembly factor of stress granules to regulate gene expression. However, it is also involved in a variety of cellular physiological processes, including signal transduction, immune response and cell cycle regulation.

Function	Description
Stress particle assembly	Under cellular stress, G3BP1 undergoes liquid-liquid phase separation through its NTF2 domain, driving messenger ribonucleoprotein aggregation and thereby the formation of nucleate stress particles.
Regulation of mRNA metabolism	By binding to specific mrnas through its RRM and RGG domains, it regulates the stability, translation and degradation of target mrnas, determining their fate under stress conditions.
Antiviral innate immunity	As a host limiting factor, it can be cleaved and inactivated by viral proteins (such as the 3C protease of rhinovirus). Its active state can inhibit the replication of various RNA viruses.
Cell signal integration	As a linker molecule of Ras GTPase activating protein, it participates in integrating growth factors and stress signals, influencing cell proliferation and survival decisions.
Maintenance of genomic stability	By interacting with DNA damage response proteins (such as USP10), it participates in the repair of DNA double-strand breaks and maintains the integrity of the genome.

The binding and phase separation activities of G3BP1 to RNA are precisely regulated by its phosphorylation state, which contrasts sharply with the oxygen-binding curve fixed by myoglobin, demonstrating its characteristic as a dynamic signal hub that can flexibly adjust its functional role according to the cell state.

Applications of G3BP1 and G3BP1 Antibody in Literature

1. Jayabalan, Aravinth Kumar, Diane E. Griffin, and Anthony KL Leung. "Pro-viral and anti-viral roles of the RNA-binding protein G3BP1." Viruses 15.2 (2023): 449. https://doi.org/10.3390/v15020449

The article indicates that viral replication depends on host cells, among which G3BP1, as a key RNA-binding protein, has become a common target for multiple viruses. Viruses regulate G3BP1 through degradation, isolation or redistribution, thereby influencing its dual functions of promoting and inhibiting viral replication.

2. Burke, James M., et al. "G3BP1-dependent condensation of translationally inactive viral RNAs antagonizes infection." Science Advances 10.5 (2024): eadk8152. https://doi.org/10.1126/sciadv.adk8152

The article indicates that G3BP1 can coagulate viral RNA to inhibit its replication, which constitutes an inherent antiviral mechanism. To counter this mechanism, many viruses prevent their own RNA from being condensed by inhibiting the function of G3BP1, hijacking host factors or maintaining translation.

3. Sahoo, Pabitra K., et al. "Disruption of G3BP1 granules promotes mammalian CNS and PNS axon regeneration." Proceedings of the National Academy of Sciences 122.9 (2025): e2411811122. https://doi.org/10.1073/pnas.2411811122

The article indicates that G3BP1 granules are a key obstacle to the regeneration of central nervous system axons. Studies have shown that by inhibiting G3BP1 or using its cell-penetrating peptide depolymerization granules, axonal regeneration after spinal cord and optic nerve injuries can be effectively promoted, providing a new strategy for nerve repair.

4. Piloto, Ana Margarida, et al. "Plastic antibodies tailored on quantum dots for an optical detection of myoglobin down to the femtomolar range." Scientific reports 8.1 (2018): 4944. https://doi.org/10.1002/advs.202403262

Research has found that DCAF7 stabilizes the G3BP1 protein and promotes the formation of stress granules, inducing nasopharyngeal carcinoma to develop resistance to cisplatin chemotherapy and metastasis. This mechanism provides new potential targets and biomarkers for the treatment of nasopharyngeal carcinoma.

5. Zheng, Xianchong, et al. "G3BP1 and SLU7 Jointly Promote Immune Evasion by Downregulating MHC‐I via PI3K/Akt Activation in Bladder Cancer." Advanced Science 11.7 (2024): 2305922. https://doi.org/10.1002/advs.202305922

Research has found that G3BP1 stabilizes PI3K mRNA and forms complexes with SLU7 and others, activates the PI3K/Akt signaling pathway, and down-regulates MHC-I expression, thereby promoting immune escape in bladder cancer. Epigallocatechin gallate (EGCG) targeting G3BP1 can enhance the efficacy of anti-PD-1 therapy.

Creative Biolabs: G3BP1 Antibodies for Research

Creative Biolabs specializes in the production of high-quality G3BP1 antibodies for research and industrial applications. Our portfolio includes monoclonal antibodies tailored for ELISA, Flow Cytometry, Western blot, immunohistochemistry, and other diagnostic methodologies.

Custom G3BP1 Antibody Development: Tailor-made solutions to meet specific research requirements.
Bulk Production: Large-scale antibody manufacturing for industry partners.
Technical Support: Expert consultation for protocol optimization and troubleshooting.
Aliquoting Services: Conveniently sized aliquots for long-term storage and consistent experimental outcomes.

For more details on our G3BP1 antibodies, custom preparations, or technical support, contact us at email.

Reference

Jayabalan, Aravinth Kumar, Diane E. Griffin, and Anthony KL Leung. "Pro-viral and anti-viral roles of the RNA-binding protein G3BP1." Viruses 15.2 (2023): 449. https://doi.org/10.3390/v15020449