Anti-G3BP Rabbit Monoclonal Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application
| WB, IHC, IF, ICC, IP, FC |
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Primary Accession | Q13283 |
Host | Rabbit |
Isotype | IgG |
Reactivity | Rat, Human, Mouse |
Clonality | Monoclonal |
Format | Liquid |
Description | Anti-G3BP Rabbit Monoclonal Antibody . Tested in WB, IHC, ICC/IF, IP, Flow Cytometry applications. This antibody reacts with Human, Mouse, Rat. |
Gene ID | 10146 |
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Other Names | Ras GTPase-activating protein-binding protein 1, G3BP-1, 3.6.4.12, 3.6.4.13, ATP-dependent DNA helicase VIII, hDH VIII, GAP SH3 domain-binding protein 1, G3BP1 {ECO:0000303|PubMed:23279204, ECO:0000312|HGNC:HGNC:30292} |
Calculated MW | 68 kDa |
Application Details | WB 1:500-1:2000 IHC 1:50-1:200 ICC/IF 1:50-1:200 IP 1:20 FC 1:50 |
Contents | Rabbit IgG in phosphate buffered saline, pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol, 0.4-0.5mg/ml BSA. |
Clone Names | Clone: 22G81 |
Immunogen | A synthesized peptide derived from human G3BP |
Purification | Affinity-chromatography |
Storage | Store at -20°C for one year. For short term storage and frequent use, store at 4°C for up to one month. Avoid repeated freeze-thaw cycles. |
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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