Analytical Data
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Gene name
S100B
- Application
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Alternative Names
S100B;Protein S100-B
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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
P23297
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Expression Region
2-94aa
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AA Sequence
GSELETAMETLINVFHAHSGKEGDKYKLSKKELKELLQTELSGFLDAQKDVDAVDKVMKELDENGDGEVDFQEYVVLVAALTVACNNFFWENS
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Molecular Weight
26.4kDa
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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
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Protein Description
S100B is a member of the S100 family of proteins, characterized by its two EF-hand calcium-binding motifs, which contribute to its diverse biological functions. Originally identified in brain tissue, S100B is now recognized for its roles in neuronal development, inflammation, and cell proliferation. Research has shown that S100B is involved in various pathological conditions, including neurodegenerative diseases, brain injuries, and cancers. As a result, it has gained attention as a potential biomarker for diagnosing and monitoring these conditions. The recombinant form of S100B has become an essential tool for studying its biological activity and interactions, enabling researchers to explore its functions in vitro and in vivo. Understanding the structure-function relationship of S100B through recombinant protein studies can provide insights into its role in health and disease. Additionally, it opens avenues for therapeutic interventions targeting S100B-related pathways, making it a significant focus in biomedical research. The growing body of evidence surrounding S100B's involvement in critical physiological and pathological processes underscores the importance of continued research in this area.
