Analytical Data
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Gene name
Gnaq
- Application
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Alternative Names
Guanine nucleotide-binding protein alpha-q
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Species
Mouse
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P21279
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Expression Region
1-359aa
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Molecular Weight
49.2 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
Gnaq is a key gene encoding a protein that plays a crucial role in various signaling pathways, particularly in the regulation of cell proliferation, differentiation, and apoptosis. Research into Gnaq and its associated protein, Gαq, has gained significant attention due to its involvement in several physiological processes and its implications in diseases, including cancer and cardiovascular disorders. The protein functions as a molecular switch, activating downstream signaling cascades upon binding to specific receptors, such as G-protein-coupled receptors (GPCRs). Abnormalities in Gnaq signaling have been linked to tumorigenesis, making it a potential target for therapeutic interventions. Researchers have employed recombinant protein technology to produce Gnaq and its variants, allowing for detailed structural and functional analyses. These studies aim to unravel the mechanisms by which Gnaq influences various cellular functions and to identify new pathways that can be targeted in disease treatment. Overall, understanding Gnaq's role in cellular signaling not only enriches our knowledge of basic biological processes but also opens avenues for innovative therapeutic strategies against diseases fueled by dysregulated Gnaq pathways.
