Analytical Data
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Gene name
SLC23A2
- Application
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Alternative Names
(Na(+)/L-ascorbic acid transporter 2)(Nucleobase transporter-like 1 protein)(Sodium-dependent vitamin C transporter 2)(hSVCT2)(Yolk sac permease-like molecule 2)
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Species
Human
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Source
E. coli
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Tag
C- His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9UGH3
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Expression Region
1-650aa
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Molecular Weight
71.3 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
SLC23A2, a member of the solute carrier family, encodes a sodium-dependent transporter primarily responsible for the uptake of ascorbic acid (vitamin C) in various tissues. The protein plays a crucial role in cellular antioxidant defense and the regulation of collagen synthesis, impacting processes such as wound healing and the prevention of oxidative stress-related diseases. Research on SLC23A2 has gained importance due to its implications in human health, including its association with conditions such as scurvy, psychiatric disorders, and cancer. Recombinant SLC23A2 protein production facilitates the study of its functional properties, interaction with ligands, and the elucidation of its transport mechanism. Using techniques such as molecular cloning, expression in suitable systems like E. coli or mammalian cells, and subsequent purification, researchers can analyze the structure-function relationship of this transporter. Investigating SLC23A2 at the protein level also aids in the development of potential therapeutic strategies targeting vitamin C transport-related disorders. The research underscores the significance of SLC23A2 in maintaining cellular homeostasis and its potential as a biomarker for various diseases, making it a valuable target for ongoing biomedical research.
