Analytical Data
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Gene name
TG
- Application
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Alternative Names
TG；Thyroglobulin
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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
P01266
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Expression Region
全长
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AA Sequence
full
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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
TG (Transglutaminase) recombinant proteins have garnered significant attention in the fields of biochemistry and molecular biology due to their diverse functional roles and potential biotechnological applications. Transglutaminases are enzymes that catalyze the formation of covalent bonds between proteins and peptides through the cross-linking of ε-(γ-glutamyl) lysine residues, which enhances protein stability, texture, and functionality. The study of TG recombinant proteins has been driven by their importance in various physiological processes, including blood coagulation, wound healing, and cellular signaling. Additionally, the ability to produce TGs through recombinant DNA technology allows for the generation of proteins with tailored properties for specific applications in food technology, pharmaceuticals, and tissue engineering. Recent advancements in synthetic biology and protein engineering have enabled researchers to optimize TGs for improved yield, activity, and specificity, paving the way for innovative uses in the production of functional foods, biotherapeutics, and regenerative medicine. As the understanding of TGs continues to evolve, their potential as versatile tools in both industrial applications and fundamental research remains a promising area of exploration.
