Analytical Data
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Gene name
CALPRO
- Application
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Alternative Names
MRP-8/MRP-14; S100A8/A9
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Species
Mouse
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P27005；P31725
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Expression Region
Met1~Glu89 and Met1~Lys113
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Molecular Weight
11/15kDa
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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
CALPRO, a recombinant protein, emerged from the need for innovative solutions in molecular biology and biopharmaceuticals. As researchers explore advanced therapeutic methodologies, the development of recombinant proteins like CALPRO plays a critical role in various applications, including drug discovery, diagnostics, and therapeutic interventions. CALPRO is designed to mimic natural proteins, facilitating studies on protein interactions, enzymatic functions, and immune responses. Its production through recombinant DNA technology offers advantages such as enhanced purity, consistency, and scalability compared to traditional protein extraction methods. The growing demand for specific proteins in research and medicine has propelled the need for optimized recombinant systems, making CALPRO a vital tool in the landscape of protein engineering. Advances in bioinformatics and synthetic biology further improve the design and functionality of CALPRO, leading to its potential use in treating diseases, studying cellular mechanisms, and developing vaccines. As the field of biotechnology continues to evolve, CALPRO represents a significant step toward improving therapeutic protein development and understanding complex biological processes.
