Analytical Data
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Gene name
SPEA
- Application
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Alternative Names
(Erythrogenic toxin)(SPE A)(Scarlet fever toxin)
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Species
Streptococcus pyogenes
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P0DJY7
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Expression Region
31-250aa
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Molecular Weight
38.6 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
SPEA (Sustained Protein Expression and Activity) recombinant proteins have garnered significant interest in biochemistry and molecular biology due to their potential applications in therapeutic development and biotechnology. The study of these proteins arose from the need to enhance protein expression levels and stability, which are critical for a variety of applications including enzyme production, vaccine development, and drug discovery. Traditional methods of protein expression often face challenges such as low yield, misfolding, and rapid degradation; thus, researchers have focused on optimizing expression systems and modifying protein structures to improve these aspects. Advances in genetic engineering and protein engineering techniques, such as fusion tags, chaperone co-expression, and directed evolution, have facilitated the development of SPEA proteins with superior properties. Additionally, the growing demand for recombinant proteins in research and clinical settings, coupled with the increasing complexity of therapeutic proteins, has spurred innovation in this field. The successful production of SPEA proteins not only addresses the challenges of traditional expression systems but also opens new avenues for functional studies, high-throughput screening, and the design of more effective therapeutics, reinforcing the importance of ongoing research in this area.
