Analytical Data
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Gene name
X347S,X348S,X509S,X538S
- Application
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Alternative Names
HA; Hemagglutinin [Cleaved into: Hemagglutinin HA1 chain; Hemagglutinin HA2 chain]; Fragment
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Species
Influenza A virus
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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
P03441
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Expression Region
330-550aa(X347S,X348S,X509S,X538S)
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Molecular Weight
27.3 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 study of recombinant proteins such as X347S, X348S, X509S, and X538S has gained significant attention due to their potential applications in various fields, including biotechnology, medicine, and environmental science. These specific recombinant proteins are characterized by their unique structural and functional properties, which can be manipulated through genetic engineering techniques. Understanding their biological functions is crucial for elucidating their roles in metabolic pathways, disease mechanisms, and organismal development. The X347S and X348S proteins, for instance, may exhibit specific enzymatic activities or binding affinities that are pivotal in biocatalysis or pharmaceutical applications. On the other hand, X509S and X538S may be investigated for their structural stability and interaction with other biomolecules, providing insights into protein folding, stability, and interactions vital for therapeutic interventions. Additionally, research on these proteins aids in designing novel drugs, improving the efficiency of bioprocesses, and developing biosensors. The recombinant expression systems employed for their production, such as bacteria, yeast, or mammalian cells, also highlight the flexibility and scalability of manufacturing these proteins for research and industrial purposes. Overall, the exploration of X347S, X348S, X509S, and X538S recombinant proteins represents a promising frontier in biosciences, promising advancements in health care and environmental stewardship.
