Analytical Data
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Gene name
Tn
- Application
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Alternative Names
Transposase for transposon Tn552; ORF 480
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Species
Staphylococcus aureus
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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
P18416
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Expression Region
1-480aa
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Molecular Weight
72.3 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
The study of Tn recombinant proteins has emerged as a significant area of research in the field of biotechnology and immunology. Tn antigen, a carbohydrate structure consisting of N-acetylgalactosamine, is normally expressed on the surface of certain human cells but is aberrantly overexpressed in various cancer types. This aberrant expression has led to considerable interest in Tn as a potential target for cancer immunotherapy. Researchers are investigating Tn recombinant proteins for their ability to elicit specific immune responses against tumors. By genetically engineering these proteins to present Tn antigens, scientists aim to stimulate the body's immune system to recognize and eliminate cancer cells. Additionally, Tn recombinant proteins can be utilized in vaccine development, diagnostics, and targeted therapies, enhancing their therapeutic potential. The ongoing research focuses on optimizing the expression systems and purification techniques for these proteins to ensure their efficacy and safety for clinical applications. Given the increasing prevalence of cancer globally, the exploration of Tn recombinant proteins holds promise for developing novel strategies to combat this disease, offering hope for improved therapeutic outcomes in patients suffering from different types of cancer.
