Product Details

Uniprot No.

Target Names

Alternative Names

ATP dependent DNA helicase VIII antibody; ATP-dependent DNA helicase VIII antibody; G3BP antibody; G3BP stress granule assembly factor 1 antibody; G3BP-1 antibody; G3bp1 antibody; G3BP1_HUMAN antibody; GAP binding protein antibody; GAP SH3 domain binding protein 1 antibody; GAP SH3 domain-binding protein 1 antibody; GTPase activating protein (SH3 domain) binding protein 1 antibody; hDH VIII antibody; Human DNA helicase VIII antibody; MGC111040 antibody; Ras GTPase activating protein binding protein 1 antibody; Ras GTPase activating protein SH3 domain binding protein antibody; Ras GTPase-activating protein-binding protein 1 antibody; RasGAP associated endoribonuclease G3BP antibody

Species Reactivity

Human, Mouse

Immunogen

A synthesized peptide derived from human G3BP1

Immunogen Species

Homo sapiens (Human)

Conjugate

Non-conjugated

Clonality

Monoclonal

Isotype

Rabbit IgG

Clone No.

13E9

Purification Method

Affinity-chromatography

Concentration

It differs from different batches. Please contact us to confirm it.

Buffer

Rabbit IgG in 10mM phosphate buffered saline , pH 7.4, 150mM sodium chloride, 0.05% BSA, 0.02% sodium azide and 50% glycerol.

Form

Liquid

Tested Applications

ELISA, IF, FC

Recommended Dilution

Application	Recommended Dilution
IF	1:50-1:200
FC	1:50-1:200

Protocols

ELISA Protocol
Immunofluorescence (IF) Protocol
Flow Cytometry (FC) Protocol

Troubleshooting and FAQs

Antibody FAQs

Storage

Upon receipt, store at -20°C or -80°C. Avoid repeated freeze.

Lead Time

Basically, we can dispatch the products out in 1-3 working days after receiving your orders. Delivery time maybe differs from different purchasing way or location, please kindly consult your local distributors for specific delivery time.

Description

G3BP1 serves as a central nucleating factor in stress granule assembly, making it an essential marker for studying cellular stress responses, RNA metabolism, and translational regulation. This protein rapidly aggregates cytoplasmic mRNA and associated proteins when cells encounter environmental stressors, positioning it at the intersection of multiple signaling pathways including those downstream of Ras-GTPase activating protein. Researchers investigating stress granule dynamics, viral infection responses, or neurodegenerative disease mechanisms will find G3BP1 detection particularly valuable.

This recombinant monoclonal antibody, generated from clone 13E9 in rabbit host, offers the reproducibility that demanding experimental workflows require. Because the antibody sequence is defined and production occurs through recombinant expression, researchers can expect consistent performance across different lots, eliminating a common source of experimental variability that can complicate longitudinal studies or multi-site collaborations.

Validation across multiple platforms demonstrates this antibody's experimental flexibility. Western blot analysis detects G3BP1 in HeLa, Jurkat, K562, and NIH/3T3 whole cell lysates at 1:1000 dilution, with the observed band appearing at approximately 70 kDa rather than the predicted 52 kDa, a shift likely attributable to post-translational modifications such as phosphorylation or glycosylation that are characteristic of this protein. Immunohistochemistry performed on paraffin-embedded human colorectal cancer tissue at 1:100 dilution shows clear target localization. Immunofluorescence staining in HepG2 cells and flow cytometry analysis in HeLa cells further confirm reliable detection, with recommended dilutions ranging from 1:50 to 1:200 for these applications. Cross-species reactivity with human and mouse samples broadens its utility across common experimental models.

This antibody supports research into stress response pathways, cancer biology, and RNA granule formation where consistent G3BP1 detection is essential.

Usage

For Research Use Only. Not for use in diagnostic or therapeutic procedures.

Target Background

Function

ATP- and magnesium-dependent helicase that plays an essential role in innate immunity. Participates in the DNA-triggered cGAS/STING pathway by promoting the DNA binding and activation of CGAS. Enhances also DDX58-induced type I interferon production probably by helping DDX58 at sensing pathogenic RNA. In addition, plays an essential role in stress granule formation. Unwinds preferentially partial DNA and RNA duplexes having a 17 bp annealed portion and either a hanging 3' tail or hanging tails at both 5'- and 3'-ends. Unwinds DNA/DNA, RNA/DNA, and RNA/RNA substrates with comparable efficiency. Acts unidirectionally by moving in the 5' to 3' direction along the bound single-stranded DNA. Phosphorylation-dependent sequence-specific endoribonuclease in vitro. Cleaves exclusively between cytosine and adenine and cleaves MYC mRNA preferentially at the 3'-UTR.

Gene References into Functions

The disruption of stress granules (SGs) during the late stage of Enterovirus 71 (EV71) infection is caused by viral protease 3C-mediated cleavage of G3BP stress granule assembly factor 1 (G3BP1). Over-expression of G3BP1-SGs negatively impacts viral replication at the cytopathic effect (CPE), protein, RNA, and viral titer levels. PMID: 30006004
JMJD6 is a novel Stress Granule component that interacts with G3BP1 complexes, and its expression reduces G3BP1 monomethylation and asymmetric dimethylation at three Arg residues. PMID: 28972166
Activated glucocorticoid receptor induced phosphorylation of v-AKT Murine Thymoma Viral Oncogene Homologue (AKT) kinase, which in turn phosphorylated and promoted nuclear translocation of G3BP1. The nuclear G3BP1 bound to the G3BP1 consensus sequence located on primary miR-15b~16-2 and miR-23a~27a~24-2 to inhibit their maturation. PMID: 28523344
Results show the crystal structure of the NTF2-like domain of G3BP-1 in complex with nsP3 protein revealing a poly-complex of G3BP-1 dimers interconnected through the FGDF motifs in nsP3. Although in vitro and in vivo binding studies revealed a hierarchical interaction of the two FGDF motifs with G3BP-1, viral growth curves clearly demonstrated that two intact FGDF motifs are required for efficient viral replication. PMID: 27383630
Based on insights from the structures and existing biochemical data, the existence of an evolutionarily conserved ribonucleoprotein (RNP) complex consisting of Caprin-1, FMRP and G3BP1 is proposed. PMID: 27303792
G3BP1 interacts directly with the foot-and-mouth disease virus internal ribosome entry site and negatively regulates translation. PMID: 28755480
The data suggested that JNK-enhanced Tudor-SN phosphorylation promotes the interaction between Tudor-SN and G3BP and facilitates the efficient recruitment of Tudor-SN into stress granules under conditions of sodium arsenite-induced oxidative stress. PMID: 28011284
These data support a role for casein kinase 2 in regulation of protein synthesis by downregulating stress granule formation through G3BP1. PMID: 27920254
G3BP1 is differentially methylated on specific arginine residues by protein arginine methyltransferase (PRMT) 1 and PRMT5 in its RGG domain. PMID: 27601476
Our data define G3BP1 as a novel independent prognostic factor that is correlated with gastric cancer progression. PMID: 25809930
G3BP mediates the condensation of stress granules by shifting between two different states that are controlled by the phosphorylation of S149 and by binding to Caprin1 or USP10. PMID: 27022092
Host G3BP1 captures HIV-1 RNA transcripts and thereby restricts mRNA translation, viral protein production and virus particle formation. PMID: 26432022
Our findings identified a novel function of G3BP1 in the progression of breast cancer via activation of the epithelial-to-mesenchymal transition PMID: 25962958
G3BP1 granules were assembled independently of TIA-1 and had a negative impact on Dengue virus replication. PMID: 26350772
The G3BP1-Caprin1-PKR complex represents a new mode of PKR activation and is important for antiviral activity of G3BP1 and PKR during infection with mengovirus. PMID: 25784705
In this report, we demonstrate that a novel peptide GAP161 blocked the functions of G3BP and markedly suppressed HCT116 cell growth through the induction of apoptosis PMID: 22703643
eQTLs acting across multiple tissues are significant carriers of inherited risk for CAD. FLYWCH1, PSORSIC3, and G3BP1 are novel master regulatory genes in CAD that may be suitable targets. PMID: 25578447
ICP8 binding to G3BP also inhibits SG formation, which is a novel function of HSV ICP8. PMID: 25658430
G3BP1 has a role in modulating stress granule assembly during HIV-1 infection PMID: 25229650
G3BP1, G3BP2 and CAPRIN1 are required for translation of interferon stimulated mRNAs and are targeted by a dengue virus non-coding RNA. PMID: 24992036
These findings disclose a novel mechanism of resveratrol-induced p53 activation and resveratrol-induced apoptosis by direct targeting of G3BP1. PMID: 24998844
G3BP1 is essential for normal stress granule-processing body interactions and stress granule function. PMID: 25847539
these findings demonstrate a critical role for YB-1 in stress granule formation through translational activation of G3BP1, and highlight novel functions for stress granules in tumor progression. PMID: 25800057
Stress granule components G3BP1 and G3BP2 play a proviral role early in Chikungunya virus replication. PMID: 25653451
Authors show that the PXXP domain within G3BP1 is essential for the recruitment of PKR to stress granules, for eIF2alpha phosphorylation driven by PKR, and for nucleating stress granules of normal composition. PMID: 25520508
Data revealed that knockdown of G3BP inhibited the migration and invasion of human lung carcinoma cells through the inhibition of Src, FAK, ERK and NF-kappaB and decreased levels of MMP-2, MMP-9 and uPA. PMID: 24157923
Binding motifs specificity has been determined for human G3BP1 NTF2-like domain. PMID: 24324649
G3BP1 regulation of cell proliferation in breast cancer cells, may occur via a regulatory effect on PMP22 expression. PMID: 24321297
both G3BP1 and G3BP2 play a role in the formation of SGs in various human cells and thereby recovery from these cellular stresses. PMID: 23279204
Data show that the nsP3/G3BP interaction also blocks stress granules (SGs) induced by other stresses than virus infection. PMID: 23087212
These findings establish a novel function for Poly(ADP-ribose) in the formation of G3BP-induced stress granules upon genotoxic stress. PMID: 22767504
Data indicate that assembly of large RasGAP SH3-binding protein (G3BP)-induced stress granules precedes phosphorylation of eukaryotic initiation factor 2alpha (eIF2alpha). PMID: 22833567
MK-STYX inhibits stress granule formation independently of G3BP-1 phosphorylation at Ser149. PMID: 23163895
arguments against G3BP1 being a genuine RasGAP-binding partner PMID: 22205990
overexpression of the amino (N)-terminal region of G3BP, including the binding region for BART mRNA, dominant-negatively inhibits formation of the complex between endogenous G3BP and BART mRNA, and increases the expression of BART. PMID: 21665939
interaction between IncA and G3BP1 of Hep-2 cells infected with Chlamydophila psittaci reduces c-Myc concentration PMID: 21304914
TAR DNA-binding protein 43 (TDP-43) regulates stress granule dynamics via differential regulation of G3BP and TIA-1. PMID: 21257637
CD24 may play a role in the inhibition of cell invasion and metastasis, and that intracellular CD24 inhibits invasiveness and metastasis through its influence on the posttranscriptional regulation of BART mRNA levels via G3BP RNase activity. PMID: 21266361
The nuclear transport factor 2-like (NTF2-like) domain of human G3BP1 was subcloned, overexpressed in Escherichia coli and purified. PMID: 21206022
Molecular and functional studies indicate that the interaction of G3BP1 with beta-F1 mRNA inhibits its translation at the initiation level, supporting a role for G3BP1 in the glycolytic switch that occurs in cancer. PMID: 20663914
The kinetics of assembly of stress granules(SGs) in living cells demonstrated that Tudor-SN co-localizes with G3BP and is recruited to the same SGs in response to different stress stimuli. PMID: 20643132
these results strongly indicate that (-)-epigallocatechin gallate suppresses lung tumorigenesis through its binding with G3BP1 PMID: 20424128
Results illustrated a role for MK-STYX in regulating the ability of G3BP1 to integrate changes in growth-factor stimulation and environmental stress with the regulation of protein synthesis. PMID: 20180778
The expressions of G3BP and OPN proteins have a close relationship with lymphoid metastasis and survival in esophageal squamous carcinoma patients. PMID: 17253181
involvement of cellular protein G3BP in transcription of intermediate stage genes may regulate the transition between early and late phases of vaccinia virus replication PMID: 15471883
G3BPs are scaffolding proteins linking signal transduction to RNA metabolism (review) PMID: 15602692
Hepatitis C virus viral gene and proteins may regulate the presence of host cellular proteins in detergent resistant membrane PMID: 16996479
Caprin-1/G3BP-1 complex is likely to regulate the transport and translation of mRNAs of proteins involved with synaptic plasticity in neurons PMID: 17210633
Both G3BP1 and G3BP2 isoforms may act as negative regulators of tumor suppressor protein p53. PMID: 17297477
The expression of G3BP and RhoC protein is closely related to the lymph node metastasis and survival in esophageal squamous carcinoma (ESC) patients. G3BP and RhoC proteins can be considered as predictors of prognosis in ESC patients. PMID: 17696235

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Subcellular Location

Cytoplasm, cytosol. Perikaryon. Cytoplasm, Stress granule. Nucleus.

Tissue Specificity

Ubiquitous.

Database Links

HGNC: 30292

OMIM: 608431

KEGG: hsa:10146

STRING: 9606.ENSP00000348578

UniGene: Hs.3353

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Code	CSB-RA583845A0HU
Size	US$210
	Order now
Image	Western Blot Positive WB detected in: Hela whole cell lysate(30µg), JURKAT whole cell lysate(30µg), K562 whole cell lysate(30µg), NIH/3T3 whole cell lysate(30µg) All lanes: G3BP1 antibody at 1:1000 Secondary Goat polyclonal to rabbit IgG at 1/40000 dilution Predicted band size: 52 kDa Observed band size: 70 kDa Exposure time：1min IHC image of CSB-RA583845A0HU diluted at 1:100 and staining in paraffin-embedded human colorectal cancer performed on a Leica BondTM system. After dewaxing and hydration, antigen retrieval was mediated by high pressure in a citrate buffer (pH 6.0). Section was blocked with 10% normal goat serum 30min at RT. Then primary antibody (1% BSA) was incubated at 4°C overnight. The primary is detected by a Goat anti-rabbit polymer IgG labeled by HRP and visualized using 0.05% DAB. Immunofluorescence staining of HepG2 cell with CSB-RA583845A0HU at 1:50, counter-stained with DAPI. The cells were fixed in 4% formaldehyde, permeabilized using 0.2% Triton X-100 and blocked in 10% normal Goat Serum. The cells were then incubated with the antibody overnight at 4°C. The secondary antibody was Alexa Fluor 488-congugated AffiniPure Goat Anti-Rabbit IgG(H+L). Overlay Peak curve showing Hela cells stained with CSB-RA583845A0HU (red line) at 1:100. The cells were fixed in 4% formaldehyde and permeated by 0.2% TritonX-100 for 10min. Then 10% normal goat serum to block non-specific protein-protein interactions followed by the antibody (1ug/110⁶cells) for 45min at 4℃. The secondary antibody used was FITC-conjugated goat anti-rabbit IgG (H+L) at 1/200 dilution for 35min at 4℃.Control antibody (green line) was Rabbit IgG (1ug/110⁶cells) used under the same conditions. Acquisition of >10,000 events was performed.
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G3BP1 Recombinant Monoclonal Antibody

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