Analytical Data
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Gene name
SERS
- Application
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Alternative Names
Seryl-tRNA synthetase ;SerRSSeryl-tRNA(Ser/Sec) synthetase
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Species
Human
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Source
E. coli
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Tag
N- GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P49591
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Expression Region
2-233aa
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Molecular Weight
53.4 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
Related Products
Protein Description
Surface-enhanced Raman spectroscopy (SERS) is a powerful analytical technique that leverages the unique properties of metal nanostructures to significantly amplify Raman signals, making it possible to detect single molecules. In recent years, the study of SERS with recombinant proteins has gained momentum due to their potential applications in bioanalysis, diagnostics, and therapeutic monitoring. Recombinant proteins, produced through biotechnology, allow for the precise control of protein structure and function, which is essential for optimizing SERS performance. By coupling these proteins with metal nanostructures, researchers can enhance the sensitivity and specificity of detection, facilitating the study of biochemical interactions at the molecular level. The integration of SERS with recombinant proteins opens up new avenues for real-time monitoring of biological processes and the development of biosensors that can detect disease biomarkers with high accuracy. With ongoing advancements in nanotechnology and protein engineering, the future of SERS utilizing recombinant proteins appears promising, potentially revolutionizing fields such as medicine, environmental monitoring, and food safety.
