Analytical Data
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Gene name
D15
- Application
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Alternative Names
exo5
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Species
Others
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Source
E. coli
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Tag
Tag Free
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P06229
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Expression Region
M1-Q291
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Protein Length
Full Length
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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 D15 recombinant protein has garnered significant attention in the field of biochemistry and molecular biology due to its potential applications in vaccine development and therapeutic interventions. This protein is derived from the D15 antigen, which is associated with certain pathogenic microorganisms. Previous studies have highlighted its role in eliciting an immune response, making it a candidate for further exploration in immunotherapy and vaccine formulation. Researchers are particularly interested in D15 because of its ability to induce both humoral and cellular immunity, which are critical for an effective immune response. The recombinant production of D15 utilizes advanced genetic engineering techniques, allowing for its purification and characterization in controlled laboratory settings. This approach not only improves the yield of the protein but also enhances its stability and efficacy. As global health challenges continue to evolve, particularly with emerging infectious diseases, the development of robust vaccines incorporating D15 recombinant protein could provide a strategic advantage in immunization efforts. Ongoing investigations are focused on optimizing the immunogenicity of this protein and understanding its mechanisms of action within the immune system. Through these research initiatives, the D15 recombinant protein stands at the forefront of translational research, with the potential to significantly impact public health by enabling the design of novel vaccines and therapeutic strategies against various infectious agents.
