G3BP1 Antibodies

Ras GTPase-activating protein-binding protein 1 (G3BP1)

ATP- and magnesium-dependent helicase (PubMed:9889278). Unwinds preferentially partial DNA and RNA duplexes with a 17 bp annealed part and either a dangling 3' tail or dangling tails at both 5'- and 3'-ends (PubMed:9889278).

Unwinds DNA/DNA, RNA/DNA, and RNA/RNA substrates with similar efficiency (PubMed:9889278). Acts unidirectionally by moving in the 5' to 3' direction along the jump single-stranded DNA (PubMed:9889278).

Gene Information

Human
Gene Name:	G3BP1
Uniprot:	Q13283
Entrez:	10146

Family

Belongs to:
No superfamily

Alternative Names

ATP-dependent DNA helicase VIII; EC 3.6.1; EC 3.6.4.12; EC 3.6.4.13; G3BP-1; G3BPRas-GTPase-activating protein SH3-domain-binding protein; GAP binding protein; GAP SH3 domain-binding protein 1; GTPase activating protein (SH3 domain) binding protein 1; hDH VIII; HDH-VIII; MGC111040; ras GTPase-activating protein-binding protein 1; RasGAP-associated endoribonuclease G3BP

Molecular Weight

Mass (kDA):
52.164 kDA

Genomic Context

Human
Location:	5q33.1
Sequence:	5; NC_000005.10 (151771954..151812785)

Tissue Specificity

Ubiquitous.

Subcellular Localizations

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

Diseases

• Malignant Neoplasms
• Neoplasms
• Hepatitis
• Hepatitis C
• Carcinoma
• Mammary Neoplasms
• Malignant Neoplasm Of Breast
• Cell Transformation, Neoplastic
• Hemorrhagic Fevers, Viral
• Malignant Neoplasm Of Lung
• Lung Neoplasms
• Neoplasms, Experimental

• Malignant Tumor Of Colon
• Lung Diseases
• Lung Diseases, Obstructive
• Fibrosis
• Posttransfusion Purpura
• Acute Promyelocytic Leukemia

Interacting Proteins

• ATXN2
• ATXN2L
• RPTOR
• SND1
• USP10

Pathways

• Translation
• Localization
• Stress Granule Assembly
• Cell Cycle
• Response To Stress
• Cell Proliferation
• Cell Growth
• Viral Replication
• Secretion
• Transport
• Interaction With Host
• Virus-host Interaction
• Virulence

• Response To Heat
• Nuclear Transport
• Sensitization
• Mrna Stabilization
• Atp/adp Exchange
• Cellular Response To Stress
• Induction Of Apoptosis

PTMs

• Phosphorylation

• Cleavage

Research Areas

• Core ESC-Like Genes
• Stem Cell Markers

For details, visit:
bosterbio.com/bosterbio-gene-info-cards/G3BP1

Best Uses Of The G3BP1 Marker

The G3BP1 marker is among the most important proteins for stress granule (SG) assembly. It is essential for docking of SGs to PBs, and is blocked by TDP-43. This antibody is used by scientists to study docking between SGPBs and HeLa cells. However, the role of this protein in the assembly of stress granules is not fully understood.

G3BP1 is required to assemble normal stress granules (SG).

The process of normal SG assembly and disassembly within cells is not well understood. SGs are dynamic and reversible condenses that assemble in response to various kinds of stress. They also disassemble when the stressor is no longer present. While the precise role of SGs in disease and health is not known however it has been established that irregularities in this process may cause many illnesses. This article focuses on the importance of G3BP1 in SG assembly and disassembly.

G3BP1 plays a crucial role in SG assembly and relocalizing SG proteins to MRV factories. This is due to the binding of both sNS and mNS. The DRGG mutant does not completely alter the G3BP1–sNS connection. It is not possible to distinguish G3BP1 from sNS without the use of a fluorescent combination dye.

While the precise mechanism behind G3BP1 and TASG interactions is not understood, the interaction between TASGs and SGs could provide a useful chemical instrument to investigate SG assembly and disassembly. The interactions between TASG, G3BP1 indicate that TASG can detect various components within SGs. This could be a contributing factor in SG accumulation or the turn of fluorescence on.

MRVs interfere with normal SG assembly and function by mislocalizing SG-associated proteins. In the disturbance of SG assembly caused by MRV, it is likely that mNS and the sNS co-express. However, other elements must also be involved in SG disruption. It is important to comprehend the impact of G3BP1's activity on SG formation.

TDP-43 blocks docking with SG-PB

Recent studies have revealed that TDP-43 can disrupt the SG-PB docking process, leading to an accumulation of cytoplasmic SG proteins. The cytoplasmic toxicity of the TDP-43 is further confirmed by the overexpression of the disease-associated mutant as well as full-length TDP-43 protein in animal models. Mutant TDP-43 exhibits rapid growths in granule sizes as well as high stress rate of granule incorporation. TDP-43 is a pathogenic type is a pathogen that disrupts the binding process between SG-PB proteins, leading to cells being exposed to oxidative stress.

TDP-43 is a molecular motifs that recognize RNA, RRM1 and RRM2. Each RRM is able to interact with at least six UG/TG repeats, with more affinity for long repeated UG/TG than shorter UG/GA. TDP-43, which is free double-stranded DNA termini which interferes with docking with SGPB because it prefers shorter UG repeats.

Moreover, it has also been observed that TDP-43 plays an important role in maintaining genomic integrity by efficiently completing the rate-limiting DSB sealing step. Neuronal cells that have TDP-43 downregulation had a lower rate of DSB repair compared to the control group and exhibited increased populations of apoptotic cells and accumulation of unrepaired DSBs. Postmortem brain samples of patients with sporadic ALS showed higher staining levels for DSB markers.

Moreover, TDP-43 is associated with non-ribosomal and polyribosome fractions in Drosophila models of TDP-43 proteinopathy which suggests that the protein plays a pivotal role in dysregulation of translation. In vitro studies in TDP-43-deficient cells showed that TDP43 associates with polyribosomes and then migrates to lighter RNP fragments after EDTA-induced dissolution of polysomes. Furthermore, ribosome profiling has confirmed that TDP-43 is linked to polyribosomes in their active translation state.

Monoclonal antibody against Anti-G3BP1.

Many companies offer monoclonals of Anti-G3BP1 from multiple suppliers. G3BP1 encodes the G3BP1 protein. Although its full-length sequence remains unknown, it could have an similarity in humans, mice, rats, or porcines. It has been implicated with mitogenic signaling pathways. The protein's size is 52.2 kilobatons.

To observe Roquin (18F8) primary antibodies against G3BP1 (dilution 1:1000) and p70 s6-kinase (1 :200) were used. In subsequent experiments, secondary antibodies against G3BP1 (1:1000 dilution) and the p70S6-kinase (1;200) were employed. The results are presented as an average of at most three independent studies conducted with Anti-G3BP1 monoclonal antibodies from Boster Bio.

HeLa cells

We have demonstrated the ability to utilize the G3BP1 marker inside Hela cells. The GFP-B-tagged protein is expressed in the nucleus of HeLa cells and are used to evaluate their functions. Cells were grown in DMEM GlutaMAX, which contains 100 U/mL penicillin streptomycin, and 10% FCS. After 48 hours, cells were taken and lysed in GlutaMAX in DMEM that contained 100 U/mL penicillin, streptomycin and 10 percent FCS. Then, cells were incubated with GFP-Trap beads pre-equilibrated in PBS-T. The beads were then incubated for 1 hour at 4°C.

PB markers include the Dcp1a peptide and the G3BP1 protein. In certain situations they are found in PBs, but do not appear in PBs from HeLa cells that are stressed by SA. TIA-1-labeled cytoplasmic puncta must be at minimum 0.75 um2 in size to be considered SGs.

The G3BP1 is a peptide that was made by fusion of SFV nsP3 SLiMs with GFP. The peptides were confirmed using mass spectrometry, and later characterized for their specific cellular targets. G3BP inhibitors also block the SARS/CoV-2 virus in VeroE6 cell.

Transfection of siRNAs enables expression of the G3BP1 protein in HeLa cells. Polyadenylated DNA is present in normal conditions and induced by stress. The PBs are believed to be mRNA decapping spots and contain enzymes that facilitate the degradation of mRNA. The PB protein is tagged by Dcp1a and TIA-1.

The N protein, which is also important in viral replication, is involved in packaging the viral transcripts. G3BP1 is a vital protein in viral replication and siRNA-tagged HeLa cells also inhibit the creation of stress granules. If these inhibitors target the N protein, it can slow the replication of the virus. It has also been shown that HeLa cells that have siRNA tags are less responsive to arsenite.

Assays of docking for SG-PB

The SG-PB proteome contains more IDRs than other proteome. This leads to an inherent bias towards interactions with IDRs. Additionally, the SGPB proteome is characterized by a higher percentage of significant matches than one would expect. In order to achieve this we conducted a protein sequence analysis to identify the general principles underlying the SG-PB proteome , as well as the composition of the domains in the tier groups. We also evaluated the effectiveness of docking assays by using these two proteomes.

The docking assays for SG-PB are highly sensitive, allowing us to detect differences in protein-protein interactions. However, this method does not yield data for predicting interactions between protein and RNA in the vivo. This is due to the fact that the protein-RNA interactions we observe in vitro may be altered in vivo through chaperones, Helicases, or changes to the RNA.

The docking assays for SG-PB were used to determine molecules that interact with Pg-p. The docking tests employ small molecules with a stereochemically defined geometrie and the correct protonation states. The docking software analyzes the conformations of these molecules within the context of the intended binding site. The result is a ligand protein complex that has the highest interaction affinity and the lowest affinity for Pgp.

In-silico prediction of positive interactions is a useful tool to design new Pgp inhibitors. It is crucial to identify low interactions early in the development of new drugs or new leaders. Therefore the flexibility of docking assays can be exploited to differentiate binders from nonbinders. This method can be used to identify promising new Pgp inhibitors, if performed correctly.