Analytical Data
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Gene name
SMO
- Application
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Alternative Names
Gx; SMOH
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Species
Human
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Source
E. coli
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Tag
N-His
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Purity
Greater than 95% as determined by SDS-PAGE.
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Uniprot
Q99835
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Expression Region
Ala30~Ile234
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Molecular Weight
31kDa
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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 study of Secreted Modular Protein (SMO) and its recombinant forms has gained significant attention due to its potential applications in various biomedical fields. SMO proteins are characterized by their modular structure, allowing for versatile functional roles in biological systems, including cell signaling, immune response modulation, and tissue repair. Research has shown that SMO proteins play essential roles in developmental processes and disease mechanisms, particularly in cancer and metabolic disorders. The ability to produce recombinant SMO proteins in laboratory settings enables researchers to explore their biological functions and interactions in detail, facilitating the development of novel therapeutic strategies. Advances in molecular cloning and protein engineering techniques have further accelerated the production and characterization of these proteins, making it possible to tailor their properties for specific applications. Additionally, understanding the structure-function relationships of SMO proteins can lead to the design of more effective drugs and biomaterials. The overall research in this area is not only vital for elucidating fundamental biological processes but also holds promise for innovative solutions in regenerative medicine and targeted therapies.
