Analytical Data
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Gene name
ST
- Application
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Species
Escherichia coli
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Source
E. coli
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Tag
Tag Free
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P01560
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Expression Region
1-18aa
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Molecular Weight
2.0 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
ST recombinant proteins, derived from the fusion of specific signal transduction and regulatory proteins, have garnered significant attention in recent years due to their potential applications in biomedical research and therapeutic development. The ST family of proteins plays a critical role in various cellular processes, including cell signaling, growth, differentiation, and apoptosis. Advances in molecular biology techniques have facilitated the rational design and production of these recombinant proteins, allowing researchers to study their functions and interactions in a controlled environment. Specifically, ST recombinant proteins are instrumental in elucidating complex molecular pathways, identifying new biomarkers for diseases, and developing innovative drug delivery systems. Additionally, their ability to be tailored for specific functions makes them valuable in vaccine development and targeted therapies. As the understanding of protein dynamics and structure evolves, the potential for ST recombinant proteins in clinical applications continues to expand, making them a focal point of research in biochemistry, pharmacology, and therapeutic innovation. Consequently, ongoing studies aim to refine their production methods, enhance their efficacy, and explore their applications across various disease models, paving the way for novel therapeutic strategies.
