Analytical Data
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Gene name
S100A16
- Application
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Alternative Names
S100-A16; AAG13; DT1P1A7; S100F; S100-F; Aging-associated gene 13 protein
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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
Q96FQ6
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Expression Region
Ser2~Ser103
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Molecular Weight
14kDa
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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
S100A16 is a member of the S100 protein family, which is known for their role in cellular processes such as calcium binding, cell proliferation, differentiation, and apoptosis. Research into S100A16 has garnered significant attention due to its involvement in various pathological conditions, including cancer, inflammation, and cardiovascular disorders. This protein is expressed in a wide range of tissues and has been implicated in the regulation of cellular growth and migration, suggesting its potential role as a biomarker for certain diseases. The reconstitution of S100A16 in vitro offers opportunities to study its structural, functional, and interaction properties in detail. Understanding the mechanisms through which S100A16 exerts its effects at the molecular level could provide insights into its potential therapeutic applications and its role in disease processes. Recent studies have highlighted the importance of S100A16 in modulating the tumor microenvironment and its association with poor prognostic outcomes in various cancer types. Thus, the development and characterization of recombinant S100A16 protein are crucial for elucidating its biological functions and may pave the way for novel approaches in the treatment of diseases where S100A16 is involved.
