Analytical Data
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Gene name
HE/Hemagglutinin-esterase
- Application
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Alternative Names
E3 glycoprotein
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Species
Human coronavirus HKU1
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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
Q14EB1
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Expression Region
12-385aa
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Molecular Weight
45.9 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
Hemagglutinin-esterase (HE) is a vital glycoprotein found in certain viruses, notably in the family of coronaviruses and certain influenza strains. It plays a crucial role in viral entry into host cells by mediating the binding of the virus to sialic acid-containing receptors. The HE protein is characterized by two major functions: hemagglutination, which facilitates viral attachment to red blood cells, and esterification, which is involved in the hydrolysis of sialic acid from glycoconjugates. Research on recombinant HE proteins has gained significance due to their potential application in vaccine development and antiviral therapies. By utilizing recombinant DNA technology, scientists can produce HE proteins in a laboratory setting, allowing for detailed study of their structure, function, and immunogenicity. Understanding the molecular interactions of HE can lead to the identification of novel targets for therapeutic intervention, enhancing our ability to combat viral infections. Additionally, recombinant HE proteins can be used as immunogens in vaccine formulations, promoting the development of broader and more effective vaccines against virus strains that possess HE. This research is essential not just for virology but also for public health, especially in light of emerging infectious diseases and the need for rapid responses to viral outbreaks. Overall, the study of recombinant HE proteins holds promise for advancing both our fundamental understanding of viral biology and the development of effective preventive and therapeutic measures against viral diseases.
