G3BP Antibody
Rabbit Polyclonal Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application ![]()
| WB |
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Primary Accession | Q13283 |
Reactivity | Human, Mouse, Rat |
Host | Rabbit |
Clonality | Polyclonal |
Isotype | Rabbit IgG |
Calculated MW | 52164 Da |
Gene ID | 10146 |
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Positive Control | Western blot: Jurkat, 3T3, rat kidney cell lysate |
Application & Usage | Western blot: 1:200 |
Other Names | ATP-dependent DNA helicase VIII |
Target/Specificity | G3BP |
Antibody Form | Liquid |
Appearance | Colorless liquid |
Formulation | 100 µg (0.5 mg/ml) of antibody in PBS, 0.01 % BSA, 0.01 % thimerosal, and 50 % glycerol, pH 7.2 |
Handling | The antibody solution should be gently mixed before use. |
Reconstitution & Storage | -20 °C |
Background Descriptions | |
Precautions | G3BP Antibody is for research use only and not for use in diagnostic or therapeutic procedures. |
Name | G3BP1 {ECO:0000303|PubMed:23279204, ECO:0000312|HGNC:HGNC:30292} |
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Function | Protein involved in various processes, such as stress granule formation and innate immunity (PubMed:12642610, PubMed:20180778, PubMed:23279204, PubMed:30510222, PubMed:30804210). Plays an essential role in stress granule formation (PubMed:12642610, PubMed:20180778, PubMed:23279204, PubMed:32302570, PubMed:32302571, PubMed:32302572, PubMed:34739333, PubMed:35977029, PubMed:36183834, PubMed:36279435, PubMed:36692217, PubMed:37379838). Stress granules are membraneless compartments that store mRNAs and proteins, such as stalled translation pre-initiation complexes, in response to stress (PubMed:12642610, PubMed:20180778, PubMed:23279204, PubMed:27022092, PubMed:32302570, PubMed:32302571, PubMed:32302572, PubMed:36279435, PubMed:37379838). Promotes formation of stress granules phase-separated membraneless compartment by undergoing liquid-liquid phase separation (LLPS) upon unfolded RNA-binding: functions as a molecular switch that triggers RNA-dependent LLPS in response to a rise in intracellular free RNA concentrations (PubMed:32302570, PubMed:32302571, PubMed:32302572, PubMed:34739333, PubMed:36279435, PubMed:36692217). Also acts as an ATP- and magnesium-dependent helicase: unwinds DNA/DNA, RNA/DNA, and RNA/RNA substrates with comparable efficiency (PubMed:9889278). Acts unidirectionally by moving in the 5' to 3' direction along the bound single-stranded DNA (PubMed:9889278). 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 (PubMed:9889278). Plays an essential role in innate immunity by promoting CGAS and RIGI activity (PubMed:30510222, PubMed:30804210). Participates in the DNA-triggered cGAS/STING pathway by promoting the DNA binding and activation of CGAS (PubMed:30510222). Triggers the condensation of cGAS, a process probably linked to the formation of membrane-less organelles (PubMed:34779554). Enhances also RIGI-induced type I interferon production probably by helping RIGI at sensing pathogenic RNA (PubMed:30804210). May also act as a phosphorylation- dependent sequence-specific endoribonuclease in vitro: Cleaves exclusively between cytosine and adenine and cleaves MYC mRNA preferentially at the 3'-UTR (PubMed:11604510). |
Cellular Location | Cytoplasm, cytosol. Perikaryon {ECO:0000250|UniProtKB:P97855}. Cytoplasm, Stress granule. Nucleus Note=Cytoplasmic in proliferating cells (PubMed:11604510). Cytosolic and partially nuclear in resting cells (PubMed:11604510). Recruited to stress granules in response to arsenite treatment (PubMed:12642610, PubMed:20180778). The unphosphorylated form is recruited to stress granules (PubMed:12642610). HRAS signaling contributes to this process by regulating G3BP dephosphorylation (PubMed:12642610) |
Tissue Location | Ubiquitous.. |

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Provided below are standard protocols that you may find useful for product applications.
Background
G3BP1 (GTPase activating protein (SH3 domain) binding protein 1), also known as G3BP or HDH-VIII, is a ubiquitously expressed protein that localizes to the cytoplasm in proliferating cells and to the nucleus in non-proliferating cells. One of several DNA-unwinding enzymes, G3BP1 functions as a sequence-specific, phosphorylation-dependent helicase that unwinds partial RNA and DNA duplexes containing hanging 3’- or 5’- ends. G3BP1 uses magnesium as a cofactor and, in addition to its helicase activity, acts as an endoribonuclease that cleaves mRNA between adenine and cytosine residues at the 3’-UTR. An element of the Ras signaling pathway, G3BP1 binds to the SH3 domain of Ras GTPase-activating protein (Ras GAP) in proliferating cells, thereby regulating Ras signaling events in developing tissues. Due to its involvement in both DNA replication and signaling pathways within the cell, G3BP1 expression is implicated in the pathogenesis of several cancers, including esophageal squamous carcinoma.

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