Analytical Data
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Gene name
SLC19A3
- Application
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Alternative Names
(ThTr-2)(ThTr2)(Solute carrier family 19 member 3)
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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
Q9BZV2
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Expression Region
208-273aa
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Molecular Weight
11.4 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
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Protein Description
SLC19A3 is a gene encoding a sodium-dependent transporter responsible for the transport of thiamine (vitamin B1) across cell membranes. Mutations in SLC19A3 are associated with a rare neurological disorder known as biotin-responsive basal ganglia disease (BRBGD) and an infantile-onset form of megaloblastic anemia. Research into recombinant SLC19A3 protein is crucial for understanding its structure-function relationships and elucidating the mechanisms behind its transport activity and substrate specificity. By producing and studying this protein in a recombinant form, researchers can investigate its role in thiamine metabolism and the impact of mutations on its function. This research not only contributes to the understanding of SLC19A3-related disorders but also holds implications for nutritional therapies and potential treatments for affected individuals. Efforts to characterize the recombinant SLC19A3 protein can aid in the development of pharmacological interventions and enhance our understanding of thiamine deficiency-related pathologies. Furthermore, exploring the interactions between SLC19A3 and its substrates can lay the groundwork for future studies aimed at designing targeted therapies for disorders associated with its dysfunction.
