Recombinant Human Ras Gtpase-Activating Protein-Binding Protein 1 (G3BP1) Protein (His)

Name: Recombinant Human Ras Gtpase-Activating Protein-Binding Protein 1 (G3BP1) Protein (His)
Brand: Beta LifeScience
SKU: BLC-01104P
Availability: InStock

Greater than 85% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Human Ras Gtpase-Activating Protein-Binding Protein 1 (G3BP1) Protein (His) is produced by our E.coli expression system. This is a full length protein.
Purity	Greater than 85% as determined by SDS-PAGE.
Uniprotkb	Q13283
Target Symbol	G3BP1
Synonyms	(G3BP-1)(ATP-dependent DNA helicase VIII)(hDH VIII)(GAP SH3 domain-binding protein 1)
Species	Homo sapiens (Human)
Expression System	E.coli
Tag	N-6His
Target Protein Sequence	MVMEKPSPLLVGREFVRQYYTLLNQAPDMLHRFYGKNSSYVHGGLDSNGKPADAVYGQKEIHRKVMSQNFTNCHTKIRHVDAHATLNDGVVVQVMGLLSNNNQALRRFMQTFVLAPEGSVANKFYVHNDIFRYQDEVFGGFVTEPQEESEEEVEEPEERQQTPEVVPDDSGTFYDQAVVSNDMEEHLEEPVAEPEPDPEPEPEQEPVSEIQEEKPEPVLEETAPEDAQKSSSPAPADIAQTVQEDLRTFSWASVTSKNLPPSGAVPVTGIPPHVVKVPASQPRPESKPESQIPPQRPQRDQRVREQRINIPPQRGPRPIREAGEQGDIEPRRMVRHPDSHQLFIGNLPHEVDKSELKDFFQSYGNVVELRINSGGKLPNFGFVVFDDSEPVQKVLSNRPIMFRGEVRLNVEEKKTRAAREGDRRDNRLRGPGGPRGGLGGGMRGPPRGGMVQKPGFGVGRGLAPRQ
Expression Range	1-466aa
Protein Length	Full Length
Mol. Weight	56.2 kDa
Research Area	Epigenetics And Nuclear Signaling
Form	Liquid or Lyophilized powder
Buffer	Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution	Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage	1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes	Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target 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.
Subcellular Location	Cytoplasm, cytosol. Perikaryon. Cytoplasm, Stress granule. Nucleus.
Database References	HGNC: 30292 OMIM: 608431 KEGG: hsa:10146 STRING: 9606.ENSP00000348578 UniGene: 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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Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

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