Analytical Data
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Gene name
tar
- Application
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Alternative Names
Aspartate chemoreceptor protein
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Species
Escherichia coli
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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
P07017
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Expression Region
212-553aa
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Molecular Weight
52 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 tar recombinant proteins has gained significant attention due to their potential applications in various fields, including biotechnology, medicine, and environmental science. Tar proteins, which are derived from microorganisms, play crucial roles in catalyzing biochemical reactions and facilitating metabolic processes. Their unique structural properties and functionalities make them suitable candidates for applications such as bioremediation, where they can be employed to detoxify pollutants, and in the production of biofuels, enhancing the efficiency of biomass conversion. Additionally, the ability to engineer tar proteins through recombinant DNA technology opens new avenues for the design of tailored enzymes with improved stability and specificity for industrial processes. These advances not only contribute to a deeper understanding of microbial physiology and biochemistry but also pave the way for innovative solutions to global challenges, such as energy sustainability and environmental conservation. The intersection of tar protein research with synthetic biology further underscores its relevance, as researchers seek to harness and optimize these proteins for enhanced performance in diverse applications, ultimately leading to breakthroughs that could significantly impact health, industry, and ecological restoration.
