Analytical Data
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Gene name
GMPS
- Application
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Alternative Names
GMP Synthase; Glutamine amidotransferase; GMP synthase [glutamine-hydrolyzing]
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P49915
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Expression Region
Met1~Glu263
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Molecular Weight
32kDa
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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
Related Products
Protein Description
The study of GMPS (Guanosine Monophosphate Synthetase) recombinant proteins has garnered significant attention in the field of molecular biology due to the enzyme's critical role in nucleotide biosynthesis and its implications in various biological processes. GMPS catalyzes the conversion of xanthosine monophosphate (XMP) to guanosine monophosphate (GMP), a key step in the purine nucleotide pathway, which is essential for DNA and RNA synthesis. Abnormalities in GMPS activity are associated with various diseases, including certain cancers and immunodeficiencies, making it a vital target for therapeutic intervention. The recombinant expression of GMPS allows for detailed structural and functional studies that can elucidate its mechanisms of action, regulatory properties, and interactions with other cellular components. By employing techniques such as molecular cloning, protein expression in suitable host systems (like E. coli or yeast), and purification methods, researchers can obtain active forms of GMPS for in vitro analyses. Additionally, characterizing GMPS at a molecular level may lead to the development of specific inhibitors, which could serve as potential drugs for treatment strategies against diseases related to its dysfunction. Overall, the research on GMPS recombinant proteins not only enhances our understanding of purine metabolism but also opens avenues for novel therapeutic approaches targeting nucleotide synthesis pathways.
