Analytical Data
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Gene name
SLC19A2
- Application
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Alternative Names
SLC19A2；THT1；TRMA；Thiamine transporter 1
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Species
Human
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Source
E. coli
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Tag
His tag N-Terminus
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O60779
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Expression Region
215-293aa
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AA Sequence
LFFHHIPSTCQRVNGIKVQNGGIVTDTPASNHLPGWEDIESKIPLNMEEPPVEEPEPKPDRLLVLKVLWNDFLMCYSSR
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Molecular Weight
16.5 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
SLC19A2, a member of the solute carrier family, encodes a high-affinity thiamine transporter critical for cellular uptake of thiamine (vitamin B1). Mutations in the SLC19A2 gene have been implicated in a variety of metabolic disorders, most notably Beriberi and a rare form of Thiamine Responsive Megaloblastic Anemia (TRMA), which is characterized by anemia, diabetes, and sensorineural hearing loss. Investigating SLC19A2 recombinant proteins is essential for understanding the structure-function relationships of the transporter and its role in thiamine metabolism. This can offer insights into potential therapeutic strategies for conditions associated with thiamine deficiency. Through the expression and purification of SLC19A2 recombinant proteins, researchers aim to elucidate the transport mechanism, substrate specificity, and the impact of identified mutations on function. Additionally, studying these recombinant proteins in various cellular models provides an opportunity to explore their physiological relevance and the downstream effects of disrupted thiamine transport. The findings from such studies may also contribute to developing novel treatment modalities for SLC19A2-related disorders, ultimately improving patient outcomes in affected populations.
