Analytical Data
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Gene name
HN
- Application
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Alternative Names
HN；HN；Humanin
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q8IVG9
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Expression Region
1-24aa
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AA Sequence
MAPRGFSCLLLLTSEIDLPVKRRA
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Molecular Weight
2.6 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
The research on recombinant HN (hemagglutinin-neuraminidase) proteins primarily stems from their significance in understanding and combating viral infections, particularly those caused by paramyxoviruses, such as the Newcastle disease virus and human respiratory syncytial virus. HN proteins play a crucial role in the viral life cycle by facilitating viral entry into host cells and promoting immune evasion. The ability to produce HN proteins in a recombinant form provides an invaluable tool for studying their structure-function relationships and interactions with host receptors. Additionally, recombinant HN proteins serve as potential candidates for vaccine development, as they can elicit strong immune responses. The increasing global concerns over viral outbreaks and the need for effective vaccines have intensified research efforts focusing on the molecular characterization of HN proteins. This includes employing biotechnology methods for the large-scale production, purification, and functional analysis of HN recombinant proteins. These advancements not only enhance our understanding of viral pathology but also contribute to the development of novel therapeutic strategies and vaccines, offering hope for better management of viral diseases.
