G3BP2 Antibody
Description
G3BP2 Protein Overview
G3BP2 (GTPase-activating protein SH3 domain-binding protein 2) is a member of the Ras-GAP SH3 domain-binding protein family, sharing 60% sequence identity with G3BP1 . Key features include:
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Domains: NTF2-like domain, RNA-binding motifs, and proline-rich regions for SH3 domain interactions .
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Functions:
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Disease associations: Overexpressed in breast, lung, and esophageal cancers, and linked to cardiac hypertrophy and atherosclerosis .
Cancer Studies
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Esophageal Squamous Cell Carcinoma (ESCC):
Cardiovascular Research
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Cardiac Hypertrophy:
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Atherosclerosis:
Stress Granule Dynamics
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G3BP2 antibodies confirm cytoplasmic localization during sodium arsenite-induced stress .
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Co-immunoprecipitation studies show G3BP2 recruits RNA-binding proteins to stress granules .
Validation and Protocol Considerations
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Western Blotting: Use 1:2,000–1:16,000 dilution (Proteintech) or 1:1,000 (Cell Signaling) with expected bands at 60–70 kDa .
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Immunofluorescence: Detect stress granules in HeLa cells treated with 0.5 mM sodium arsenite .
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Troubleshooting: Optimize antigen retrieval with TE buffer (pH 9.0) for IHC .
Clinical and Therapeutic Implications
Product Specs
Target Background
- Elevated G3BP2 levels have been associated with a worse prognosis in breast cancer. Cell lines exhibiting lower G3BP2 levels required significantly higher cell numbers to form tumors in NOD/SCID mice. G3BP2 regulates the expression of SART3, Nanog, and Oct-4, potentially contributing to the maintenance of breast cancer cell subpopulations with long-term proliferative capabilities. G3BP2 appears to be important in the initiation of breast tumors. PMID: 28096337
- The translocation of p53 is regulated by androgen-dependent sumoylation, a process mediated by the G3BP2-interacting SUMO-E3 ligase, RanBP2. Knockdown of G3BP2 leads to reduced tumor growth and increased nuclear p53 accumulation in mouse xenograft models of prostate cancer, both with and without long-term androgen deprivation. PMID: 28692047
- The FGDF peptide binds and alters the conformation of the protruding N-terminal residues of G3BP2 by providing hydrophobic interactions with a symmetry-related molecule, facilitating the crystallization of the G3BP2 isoform. PMID: 26410532
- G3BP1, G3BP2, and CAPRIN1 are essential for the translation of interferon-stimulated mRNAs and are targeted by a dengue virus non-coding RNA. PMID: 24992036
- Research has identified a TWIST1-G3BP2 mechanotransduction pathway that responds to biomechanical signals from the tumor microenvironment, driving epithelial-mesenchymal transition (EMT), invasion, and metastasis. PMID: 25893917
- Stress granule components G3BP1 and G3BP2 play a proviral role in the early stages of Chikungunya virus replication. PMID: 25653451
- Both G3BP1 and G3BP2 contribute to the formation of stress granules (SGs) in various human cells, facilitating recovery from cellular stresses. PMID: 23279204
- Studies indicate that the nsP3/G3BP interaction also blocks stress granules (SGs) induced by stresses other than viral infection. PMID: 23087212
- This research provides the first evidence of direct interactions between PKCalpha and G3BP2, demonstrating that PKCalpha can phosphorylate G3BP2. PMID: 22536444
- A study revealed that just four genes, G3BP2, SCARB2, CSNK1A1, and SPRR2B, can accurately classify patients as having either negative or positive lymph node metastasis, with an accuracy rate of 80.0%. PMID: 21985131
- Both G3BP1 and G3BP2 isoforms may act as negative regulators of the tumor suppressor protein p53. PMID: 17297477
