Analytical Data
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Gene name
THI2.3
- Application
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Alternative Names
THI2.3；Viscotoxin-A2
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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
P32880
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Expression Region
1-46aa
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AA Sequence
KSCCPNTTGRNIYNTCRFGGGSREVCASLSGCKIISASTCPSYPDK
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Molecular Weight
17.8 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
Related Products
Protein Description
THI2.3 is a recombinant protein that plays a crucial role in the biosynthesis of thiamine (vitamin B1) in organisms such as plants and microorganisms. The gene encoding THI2.3 is particularly interesting due to its involvement in the regulation of thiamine levels, which are essential for fundamental processes such as energy metabolism and enzymatic functions. Research indicates that THI2.3 may have significant implications in plant growth, stress responses, and overall health. With the increasing interest in nutritional enhancement of crops and the potential linkage between thiamine deficiency and various health issues, studies on THI2.3 can contribute valuable insights into strategies for improving thiamine content in food crops. Recombinant production of THI2.3 facilitates detailed functional studies and allows researchers to explore its biochemical properties and interactions within the cellular environment. Furthermore, understanding the structural and functional dynamics of this protein could pave the way for biotechnological applications in enhancing crop resilience and nutritional profile, addressing both food security and health challenges associated with micronutrient deficiencies. Overall, THI2.3 serves as an important model in the ongoing exploration of how specific proteins can influence metabolic pathways and contribute to agricultural science and nutrition.
