Analytical Data
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Gene name
ha17
- Application
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Alternative Names
/
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Species
Clostridium botulinum
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Source
Yeast
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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
A5HZZ5
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Expression Region
2-146aa
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Molecular Weight
18.9 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
HA17 is a recombinant protein derived from the hemagglutinin (HA) protein of the influenza virus, particularly known for its role in viral entry into host cells. The study of HA17 has gained significant attention due to its potential applications in vaccine development and therapeutic interventions against influenza. Hemagglutinin is a key surface antigen that elicits robust immune responses, making it a prime target for influenza vaccines. By exploring the structure and function of HA17, researchers aim to enhance the understanding of the virus-host interaction, improve vaccine efficacy, and develop novel antiviral strategies. Additionally, the recombinant production of HA17 allows for the generation of specific immune responses without the risks associated with live attenuated viruses. This research is critical in the context of emerging influenza strains and the ongoing threat of pandemics, as it provides insights into the mechanisms of antigenic variation and immune evasion employed by the virus. By characterizing HA17 and exploring its immunological properties, scientists hope to contribute to the development of more effective vaccines and therapeutics to combat influenza infections, ultimately improving public health outcomes.
