Analytical Data
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Gene name
thiO
- Application
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Alternative Names
thiO；TRDX；TRX；TRX1；Thioredoxin
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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
P09110
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Expression Region
27-331aa
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AA Sequence
LSGAPQASAADVVVVHGRRTAICRAGRGGFKDTTPDELLSAVMTAVLKDVNLRPEQLGDICVGNVLQPGAGAIMARIAQFLSDIPETVPLSTVNRQCSSGLQAVASIAGGIRNGSYDIGMACGITSENVAERFGISREKQDTFALASQQKAARAQSKGCFQAEIVPVTTTVHDDKGTKRSITVTQDEGIRPSTTMEGLAKLKPAFKKDGSTTAGLTVSDVDIFEINEAFASQAAYCVEKLRLPPEKVNPLGGAVALGHPLGCTGARQVITLLNELKRRGKRAYGVVSMCIGTGMGAAAVFEYPGN
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Molecular Weight
47.9 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
ThiO, a protein involved in thiamine (vitamin B1) biosynthesis, has garnered attention due to its crucial role in the synthesis of thiamine pyrophosphate (TPP), an essential cofactor for various enzymatic reactions in cellular metabolism. Understanding the structure and function of ThiO is vital, as thiamine deficiency can lead to severe neurological disorders and metabolic dysfunctions, impacting health globally. Recent research has focused on the elucidation of ThiO's mechanism and its interaction with other enzymes in the thiamine biosynthetic pathway, as well as its potential applications in biotechnology and medicine. Advances in recombinant protein technology enable the production of ThiO in sufficient quantities for detailed biochemical studies, allowing researchers to explore its catalytic properties and substrate specificity. Additionally, insights gained from ThiO research may contribute to the development of novel therapeutic strategies aimed at combating thiamine-related disorders and enhancing the production of thiamine through metabolic engineering in microorganisms. The exploration of ThiO not only aids in our understanding of vitamin biosynthesis but also opens new avenues for addressing nutritional deficiencies and improving metabolic health in various organisms.
