Analytical Data
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Gene name
NIS
- Application
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Alternative Names
SLC5A5; Solute Carrier Family 5 Member 5; Na(+)/I(-) cotransporter
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Species
Human
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Source
E. coli
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Tag
N- His & GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q92911
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Expression Region
Ser547~Leu643
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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
NIS (Sodium/Iodide Symporter) is a crucial membrane protein primarily expressed in thyroid follicular cells, playing a significant role in thyroid hormone synthesis by facilitating iodine uptake. Research into NIS has garnered interest due to its potential implications in both thyroid-related diseases and cancer treatment. In thyroid cancer, for instance, the functionality of NIS can be compromised, leading to reduced iodine uptake which poses challenges for radioiodine therapy. Consequently, understanding the structural and functional aspects of NIS, including its protein folding and trafficking mechanisms, is essential for developing strategies to enhance radioiodine therapy effectivity. Moreover, NIS has garnered attention as a potential therapeutic target in non-thyroid cancers, where it may be exploited for selective delivery of iodine-based therapeutics. Recent advancements in recombinant protein technology enable the production of NIS in sufficient quantities for detailed structural studies, which are critical for elucidating its transport mechanisms and interactions with various ligands. These studies aim to improve our understanding of NIS function and its regulation, facilitating the development of innovative treatments for both thyroid dysfunctions and malignancies. As research evolves, the insights gained from NIS studies promise to enhance the precision of therapies and improve patient outcomes, highlighting the necessity for continued exploration of this vital protein.
