Analytical Data
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Gene name
X477S
- Application
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Alternative Names
Nucleocapsid protein;Nucleocapsid protein;Protein N
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Species
Influenza A virus
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
A0A6G5UZV1
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Expression Region
1-498aa(X477S)
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Molecular Weight
63.4 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 X477S recombinant protein has emerged as a focal point of research due to its potential applications in various biotechnological and biomedical fields. Derived from engineered variants of existing proteins, X477S exhibits unique structural and functional properties that may enhance its utility in therapeutic and industrial processes. Researchers are particularly intrigued by its role in the modulation of specific biological pathways, which could lead to advancements in drug development, particularly for diseases caused by protein misfolding and aggregation. The development of X477S involves intricate techniques such as site-directed mutagenesis and advanced purification methods, enabling scientists to study its interactions at a molecular level. Additionally, preliminary studies have suggested that X477S may possess enhanced stability and activity compared to its wild-type counterparts, making it a promising candidate for further investigation. As research progresses, the implications of X477S in protein engineering, therapeutic interventions, and its potential to serve as a model for understanding protein dynamics are being explored, highlighting the importance of this recombinant protein in modern scientific inquiry.
