Analytical Data
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Gene name
SNX17
- Application
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Species
Human
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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
Q15036
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Expression Region
Met1~Gln195
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Molecular Weight
26kDa
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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
SNX17 (Sorting Nexin 17) is a member of the sorting nexin family, which plays a critical role in endosomal trafficking and the regulation of various cellular processes. Research has increasingly highlighted the significance of SNX17 in influencing the stability and sorting of membrane proteins, particularly in the context of receptor recycling and degradation. Its interactions with various signaling pathways underscore its potential role in cellular homeostasis and disease processes, including cancer and neurodegenerative disorders. Recombinant SNX17 protein has become an important tool for dissecting its biological functions and regulatory mechanisms. By studying SNX17 through recombinant expression systems, researchers aim to elucidate its structural properties, binding characteristics, and functional implications in cellular contexts. This research not only enhances our understanding of membrane dynamics but also opens avenues for potential therapeutic strategies targeting SNX17-related pathways. Overall, the study of SNX17 recombinant protein is pivotal for advancing our knowledge of cellular trafficking processes and their impact on health and disease.
