Analytical Data
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Gene name
TBCEL
- Application
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Alternative Names
Leucine-rich repeat-containing protein 35
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Species
Human
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q5QJ74
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Expression Region
1-424aa
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Molecular Weight
64.2 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
TBCEL, or Trehalose-6-phosphate synthase-like protein, has garnered attention in the field of biotechnology and molecular biology due to its potential role in carbohydrate metabolism and stress response in organisms. Trehalose is a disaccharide that serves as a protective and energy-storing molecule in various organisms, particularly in fungi, bacteria, and plants. Research has shown that TBCEL is involved in trehalose biosynthesis, which is crucial for stress tolerance, particularly in scenarios involving desiccation and extreme environmental conditions. Understanding the functional mechanisms of TBCEL can lead to insights into how organisms adapt to stress, providing valuable information for agricultural applications, such as enhancing crop resilience. In addition, the recombinant expression of TBCEL in heterologous systems allows for the exploration of its biochemical properties and potential industrial applications, including its use in developing stress-resistant transgenic plants or producing trehalose as a beneficial additive in food and pharmaceutical industries. The ongoing research aims to elucidate the structure-function relationship of TBCEL and to harness its properties for biotechnological advancements.
