Analytical Data
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Gene name
S100
- Application
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Alternative Names
S100；Protein S100-Z
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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
P04271
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Expression Region
1-92aa
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AA Sequence
MSELEKAMVALIDVFHQYSGREGDKHKLKKSELKELINNELSHFLEEIKE QEVVDKVMETLDNDGDGECDFQEFMAFVAMVTTACHEFFEHE
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Molecular Weight
12 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 S100 protein family comprises a diverse group of low-molecular-weight proteins known for their ability to bind calcium and zinc ions, playing crucial roles in various cellular processes. Discovered in the early 1980s, S100 proteins are predominantly expressed in the brain and numerous other tissues, where they are implicated in cell differentiation, growth, and motility. Their involvement in numerous pathological conditions, including neurodegenerative diseases, cancer, and inflammation, has heightened interest in understanding their functional roles and regulatory mechanisms. Recent advancements in recombinant protein technology have facilitated the study of S100 proteins in a controlled environment, allowing researchers to investigate their specific interactions with target proteins and the molecular pathways they influence. This research is vital not only for elucidating the physiological functions of S100 proteins but also for exploring their potential as biomarkers for disease diagnosis and therapeutic targets. As a result, the recombinant production of S100 proteins is critical for advancing our understanding of their roles in health and disease.
