Analytical Data
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Gene name
SNX9
- Application
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Alternative Names
SDP1; SH3PX1; SH3PXD3A; WISP; SH3 and PX domain-containing protein 1; SH3 and PX domain-containing protein 3A
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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
Q9Y5X1
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Expression Region
Phe250~Met595
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Molecular Weight
44kDa
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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
SNX9 (Sorting Nexin 9) is a member of the sorting nexin family, which plays a crucial role in endocytic and membrane trafficking processes within cells. It is characterized by its BAR (Bin-Amphiphysin-Rvs) domain, which is involved in membrane curvature and the formation of vesicles. Research has shown that SNX9 is essential for maintaining cellular homeostasis and is implicated in various physiological and pathological processes, including cellular signaling, synaptic functions, and cancer progression. Given its pivotal functions, SNX9 has emerged as a potential target for therapeutic interventions. The study of recombinant SNX9 proteins allows for the detailed exploration of its structural and functional properties, and the elucidation of its interactions with other cellular components. This research is vital for understanding the mechanisms by which SNX9 contributes to cellular dynamics and how its dysregulation may lead to disease. Consequently, producing and characterizing recombinant SNX9 proteins provides a foundation for future studies aimed at developing targeted therapies that could mitigate the adverse effects associated with its dysfunction.
