Analytical Data
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Gene name
CNT3
- Application
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Alternative Names
CNT3
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Species
Human
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Source
Baculovirus
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Tag
Strep;His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9HAS3-1
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Expression Region
M70-F691
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Protein Length
Partial
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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
CNT3, or "Cystine Transporter 3," is a member of the solute carrier (SLC) family of proteins that plays a critical role in cellular amino acid transport, particularly in the uptake of cysteine and cystine. The importance of CNT3 in cellular metabolism and its implications in various physiological and pathological conditions have spurred research interest. Dysfunction of cysteine transport is linked to numerous diseases, including neurodegenerative disorders and certain types of cancer. To better understand the structural and functional properties of CNT3, researchers have focused on the production and characterization of recombinant CNT3 proteins. This involves the use of molecular cloning techniques to generate CNT3 cDNA, followed by expression in suitable host cells, such as bacteria or mammalian cells, to obtain sufficient quantities of the functional protein for biochemical studies. The recombinant CNT3 protein allows researchers to investigate its transport mechanisms, substrate specificity, and regulation under different physiological conditions. Additionally, studying the recommended structure of CNT3 through techniques such as X-ray crystallography or cryo-electron microscopy can provide valuable insights into its functional dynamics. The findings from CNT3 research not only enhance our understanding of amino acid transport but may also offer potential therapeutic targets for diseases associated with cysteine metabolism, highlighting the protein's significance in both basic and applied biomedical research.
