Analytical Data
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Gene name
S375SLEH
- Application
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Species
Human
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P35659
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Expression Region
309-375aa(S375SLEH)
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Molecular Weight
15.7 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
The S375SLEH recombinant protein has garnered significant interest in the field of molecular biology and therapeutic research due to its unique structural and functional properties. This protein is derived from a specific sequence modification aimed at enhancing the stability and solubility of the original protein, thus improving its potential for biomedical applications. Researchers are particularly interested in S375SLEH for its role in cellular signaling pathways and its implications in various diseases, including cancer and metabolic disorders. The ability to produce this recombinant protein in a controlled laboratory setting allows for extensive studies on its interactions with other biomolecules, as well as its potential as a therapeutic agent. Furthermore, understanding its biochemical characteristics could shed light on the mechanisms of disease progression and lead to the development of innovative treatment strategies. The ongoing investigations into S375SLEH aim to elucidate its precise role in biological systems, paving the way for future applications in drug design and regenerative medicine.
