Analytical Data
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Gene name
G3BP
- Application
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Alternative Names
(G3BP-1)(ATP-dependent DNA helicase VIII)(hDH VIII)(GAP SH3 domain-binding protein 1)
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q13283
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Expression Region
1-466aa
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AA Sequence
MVMEKPSPLLVGREFVRQYYTLLNQAPDMLHRFYGKNSSYVHGGLDSNGKPADAVYGQKEIHRKVMSQNFTNCHTKIRHVDAHATLNDGVVVQVMGLLSNNNQALRRFMQTFVLAPEGSVANKFYVHNDIFRYQDEVFGGFVTEPQEESEEEVEEPEERQQTPEVVPDDSGTFYDQAVVSNDMEEHLEEPVAEPEPDPEPEPEQEPVSEIQEEKPEPVLEETAPEDAQKSSSPAPADIAQTVQEDLRTFSWASVTSKNLPPSGAVPVTGIPPHVVKVPASQPRPESKPESQIPPQRPQRDQRVREQRINIPPQRGPRPIREAGEQGDIEPRRMVRHPDSHQLFIGNLPHEVDKSELKDFFQSYGNVVELRINSGGKLPNFGFVVFDDSEPVQKVLSNRPIMFRGEVRLNVEEKKTRAAREGDRRDNRLRGPGGPRGGLGGGMRGPPRGGMVQKPGFGVGRGLAPRQ
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Molecular Weight
56.2 kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
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Protein Description
G3BP (GTPase-activating protein 2-binding protein) is a multifunctional protein that plays a critical role in cellular stress responses, RNA metabolism, and the regulation of gene expression. The study of G3BP has gained prominence due to its involvement in various biological processes, including the formation of stress granules, which are cytoplasmic aggregates that sequester mRNA and proteins during stress conditions, ultimately influencing cell survival and adaptation. Furthermore, G3BP is implicated in viral infections, as several viruses exploit G3BP's functions to enhance their replication and evade host immune responses. Research has revealed that dysregulation of G3BP is associated with several diseases, including cancer and neurodegenerative disorders, making it a potential therapeutic target. Investigating G3BP through recombinant protein techniques enables a deeper understanding of its structural and functional properties, paving the way for the development of novel strategies to modulate its activity in various pathological contexts. Thus, research on G3BP, especially in its recombinant form, is vital for unraveling its complex roles in health and disease, as well as for exploring its potential in therapeutic interventions.
