Analytical Data
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Gene name
NPG3
- Application
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Alternative Names
PG-3
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Species
Pig
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P32196
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Expression Region
131-148aa
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Molecular Weight
18.1 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
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Protein Description
NPG3 recombinant protein, derived from the NPG3 gene of specific pathogenic organisms, has garnered significant research interest due to its potential implications in understanding disease mechanisms and developing therapeutic strategies. This protein is known for its unique structural and functional properties that may play a critical role in various biological processes, including cell signaling and immune response modulation. Previous studies have indicated that NPG3 may be involved in pathogen-host interactions, making it a valuable target for vaccine development and drug discovery. Additionally, the ability to produce NPG3 as a recombinant protein in suitable expression systems allows for detailed biochemical and biophysical characterization, paving the way for elucidating its functional roles. Researchers are focused on exploring the protein's interaction with host immune cells and its potential use in immunotherapeutic applications. Furthermore, understanding the structure-function relationship of NPG3 may lead to insights into its mechanisms of action, thereby contributing to advancements in targeted therapies against diseases where NPG3 is implicated. This research not only enhances our knowledge of pathogen biology but also holds promise for innovative approaches in combating infectious diseases and improving human health. The ongoing exploration of NPG3 recombinant protein continues to reveal its relevance in contemporary biomedical research, making it a topic of considerable interest in the fields of microbiology, immunology, and therapeutic development.
