Analytical Data
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Gene name
tpl
- Application
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Alternative Names
(Beta-tyrosinase)
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Species
Citrobacter freundii
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Source
E. coli
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Tag
N- His & C- Myc
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
P31013
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Expression Region
1-456aa
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Molecular Weight
58.9 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
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Protein Description
TPL (Tetratricopeptide Repeat Protein) fusion proteins have garnered significant attention in recent years due to their versatile roles in cellular processes and potential applications in biotechnology and medicine. TPLs are characterized by their unique structural motifs that facilitate a wide range of protein–protein interactions, making them crucial for various biological functions, including protein folding, intracellular signaling, and gene regulation. Understanding the mechanisms underlying TPL interactions and their influence on cellular pathways is vital for elucidating molecular biology and developing targeted therapeutic strategies. Furthermore, the ability to manipulate TPLs through genetic engineering has opened new avenues for the design of recombinant proteins with tailored properties for use in drug development, enzyme engineering, and crop improvement. The exploration of TPL fusion proteins not only enhances our comprehension of fundamental biological processes but also paves the way for innovative applications in tackling diseases and improving agricultural productivity. As research progresses, insights gained from TPL studies may contribute to advancements in precision medicine and sustainable agricultural practices, underscoring the significance of these proteins in contemporary science.
