Analytical Data
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Gene name
TRS
- Application
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Alternative Names
TRS；KIAA1012；Trafficking Protein particle complex subunit 8
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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
Q75006
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Expression Region
1-107aa
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AA Sequence
MAGRSGDSDEELLKAVRIIKILYQSNPYPTPEGTRQARRNRRRRWRARQRQIHTLSERILSNFLGRPAEPVPLQLPPLERLNLDCSEDSGTSGTQQSQGTTEGVGNP
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Molecular Weight
38.7 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
TRS (Targeted Recombination System) recombinant proteins have gained significant attention in the field of biotechnology and molecular biology due to their diverse applications in research and therapeutics. This system allows for the precise manipulation of genetic material, enabling researchers to produce proteins with specific modifications or functional domains. The background of TRS recombinant protein research is rooted in the need for high-efficiency protein expression and purification techniques to study protein functions, interactions, and dynamics in cellular systems. Traditional methods of protein production can be time-consuming and yield low amounts of functional protein, thus prompting the exploration of advanced recombination technologies. TRS leverages synthetic biology approaches and homologous recombination to facilitate the generation of proteins that are often difficult to produce using conventional expression systems. These recombinant proteins are invaluable for developing targeted therapies, understanding disease mechanisms, and advancing vaccine development. Furthermore, the ability to produce proteins with enhanced characteristics, such as improved stability or increased specificity, opens new avenues for biomedical research. As the demand for tailored biopharmaceuticals continues to rise, the study of TRS recombinant proteins represents a promising frontier that integrates genetic engineering with practical applications in health and disease management.
