Recombinant Human G3BP protein (His tag C-Terminus)
Be the first to review this product! Submit a review
|
(2 Publications)
Recombinant Human G3BP protein (His tag C-Terminus) is a Human Full Length protein, in the 1 to 466 aa range, expressed in Escherichia coli, with >85%, suitable for SDS-PAGE, Mass Spec.
View Alternative Names
G3BP, G3BP1, Ras GTPase-activating protein-binding protein 1, G3BP-1, ATP-dependent DNA helicase VIII, GAP SH3 domain-binding protein 1, hDH VIII
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant Human G3BP protein (His tag C-Terminus) (AB103304)
SDS-PAGE analysis of Recombinant Human G3BP protein (ab103304), under reducing conditions. Proteins visualized by coomassie blue stain.
Lane 1 : Molecular Weight Standards
Lane 2 : 3 μg Recombinant Human G3BP protein
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage duration
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Specifications
Form
Liquid
Additional notes
ab103304 was purified using conventional chromatography techniques.
General info
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).
Post-translational modifications
Phosphorylation of the acidic disordered region regulates stress granule assembly (PubMed:32302571, PubMed:32302572). RASA1-dependent phosphorylation of Ser-149 induces a conformational change that prevents self-association (PubMed:11604510, PubMed:12642610). Dephosphorylation after HRAS activation is required for stress granule assembly (PubMed:11604510, PubMed:12642610). Ser-149 phosphorylation induces partial nuclear localization (PubMed:11604510).. Ubiquitinated by TRIM21 via 'Lys-63'-linked polyubiquitination in the NTF2 domain in response to heat shock, leading to stress granule disassembly: ubiquitination promotes interaction with the FAF2 adapter, followed by interaction with VCP, which extracts G3BP1 from stress granules, leading to stress granule disassembly (PubMed:34739333, PubMed:36692217). In case of prolonged stress, ubiquitination by TRIM21 leads to autophagy-dependent degradation of G3BP1 via recruitment of ubiquitinated G3BP1 by SQSTM1 and/or CALCOCO2 to autophagosomes (PubMed:34739333, PubMed:36692217).. (Microbial infection) Cleaved by human enterovirus 71; this cleavage induces the disassembly of cytoplasmic stress granules (PubMed:30006004). Cleaved by Foot-and-mouth disease virus; this cleavage suppresses the formation of cytoplasmic stress granules (PubMed:30404792).. Arg-435 is dimethylated, probably to asymmetric dimethylarginine.. (Microbial infection) Cleaved by Encephalomyocarditis virus protease 3C; this cleavage suppresses the formation of cytoplasmic stress granules.
Subcellular localisation
Nucleus
Target data
Publications (2)
Recent publications for all applications. Explore the full list and refine your search
iScience 27:110788 PubMed39286502
2024
Applications
Unspecified application
Species
Unspecified reactive species
Cell 186:3307-3324.e30 PubMed37385249
2023
Applications
Unspecified application
Species
Unspecified reactive species
Product promise
Please note: All products are 'FOR RESEARCH USE ONLY. NOT FOR USE IN DIAGNOSTIC OR THERAPEUTIC PROCEDURES'.
For licensing inquiries, please contact partnerships@abcam.com