Analytical Data
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Gene name
SNX15
- Application
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Alternative Names
Clone iota unknown protein; HSAF001435; SNX 15; SNX15; SNX15_HUMAN; Sorting nexin 15; Sorting nexin-15
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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
Q9NRS6
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Expression Region
1-342 aa
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AA Sequence
MSRQAKDDFL RHYTVSDPRT HPKGYTEYKV TAQFISKKDP EDVKEVVVWK RYSDFRKLHG DLAYTHRNLF RRLEEFPAFP RAQVFGRFEA SVIEERRKGA EDLLRFTVHI PALNNSPQLK EFFRGGEVTR PLEVSRDLHI LPPPLIPTPP PDDPRLSQLL PAERRGLEEL EVPVDPPPSS PAQEALDLLF NCESTEEASG SPARGPLTEA ELALFDPFSK EEGAAPSPTH VAELATMEVE SARLDQEPWE PGGQEEEEDG EGGPTPAYLS QATELITQAL RDEKAGAYAA ALQGYRDGVH VLLQGVPSDP LPARQEGVKK KAAEYLKRAE EILRLHLSQL PP
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Molecular Weight
38.2 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
SNX15, a member of the sorting nexin family, has garnered attention in recent years for its potential roles in intracellular trafficking and membrane dynamics. Research indicates that SNX15 participates in the endosomal-lysosomal pathway, where it is involved in the sorting and recycling of membrane proteins. The protein is characterized by the presence of a phosphoinositide-binding PH domain, which suggests its function in recognizing and binding to specific lipid environments within the cell. Understanding the biological functions and mechanisms of SNX15 is crucial, as dysregulation of sorting nexins has been implicated in various diseases, including cancer and neurodegenerative disorders. Recent studies utilizing recombinant SNX15 protein have aimed to elucidate its structure-function relationship and interaction partners, providing insights into its role in membrane trafficking. Moreover, the production of SNX15 as a recombinant protein allows for detailed biochemical and biophysical analyses, such as crystallography or binding assays, to further explore its potential as a therapeutic target. The ongoing research into SNX15 aims to unravel its contributions to cellular homeostasis and its implications in pathophysiological conditions, ultimately seeking to leverage this knowledge for developing novel strategies in disease management.
