Analytical Data
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Gene name
SERS
- Application
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Alternative Names
SERS；SARS；SERS；Serine--tRNA ligase. cytoplasmic
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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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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AA Sequence
VLDLDLFRVDKGGDPALIRETQEKRFKDPGLVDQLVKADSEWRRCRFRADNLNKLKNLCSKTIGEKMKKKEPVGDDESVPENVLSFDDLTADALANLKVSQIKKVRLLIDEAILKCDAERIKLEAERFENLREIGNLLHPSVPISNDEDVDNKVERIWGDCTVRKKYSHVDLVVMVDGFEGEKGAVVAGSRGYFLKGVLVFLEQALIQYALRTLGSRGYIPIYTPFFMRKEV
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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) has emerged as a powerful analytical technique for probing molecular interactions at the nanoscale, particularly in the realm of biomolecular research. The SERS platform's sensitivity is significantly enhanced by the use of metallic nanoparticles which amplify the Raman signal of molecules adsorbed on their surfaces. This has led to the investigation of SERS in studying recombinant proteins, which are artificially produced proteins that have been engineered for various applications, including diagnostics, therapeutics, and industrial processes. The ability to obtain molecular-level information about their structure and dynamics through SERS is particularly beneficial for understanding protein folding, conformational changes, and interactions with ligands or other biomolecules. Moreover, the non-destructive nature of SERS allows for real-time monitoring of protein behavior under various conditions. As research in the field of biotechnology advances, the integration of SERS with recombinant protein studies has the potential to offer insights into protein functionality, stability, and the identification of post-translational modifications. This area of study is rapidly evolving, promising to enhance our understanding of protein science and to facilitate the development of innovative applications in medicine and beyond.
