Analytical Data
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Gene name
S100A5
- Application
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Alternative Names
S100-A5; S100D
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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
P33763
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Expression Region
Met1~Lys92
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Molecular Weight
12kDa
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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
S100A5 is a member of the S100 protein family, characterized by its ability to bind calcium and zinc ions, which play crucial roles in various cellular processes. Research into S100A5 has gained attention due to its involvement in several pathological conditions, including cancer progression, inflammation, and neurodegenerative diseases. The protein is believed to participate in regulating cellular growth, differentiation, and migration, making it a potential biomarker and therapeutic target. Notably, studies have shown that S100A5 can influence tumor microenvironments and adjacent signaling pathways, contributing to tumor cell survival and metastasis. Additionally, its expression levels have been correlated with disease prognosis, highlighting its significance in clinical settings. Given this backdrop, recombinant S100A5 protein production has emerged as a pivotal area of research, facilitating the study of the protein's structure-function relationships and its interactions with other biomolecules. Through recombinant technology, the availability of pure S100A5 allows for detailed functional assays and the development of inhibitors or modulators, advancing the understanding of its role in health and disease. Overall, the continued exploration of S100A5 at the molecular level promises to uncover novel therapeutic strategies and improve diagnostic approaches in various diseases.
