Analytical Data
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Gene name
tar
- Application
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Alternative Names
tar；TA4；TAR4；TRAR4；Trace amine-associated receptor 6
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Species
E.coli
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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
P07017
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Expression Region
212-553aa
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AA Sequence
IRRMLLTPLAKIIAHIREIAGGNLANTLTIDGRSEMGDLAQSVSHMQRSLTDTVTHVREGSDAIYAGTREIAAGNTDLSSRTEQQASALEETAASMEQLTATVKQNADNARQASQLAQSASDTAQHGGKVVDGVVKTMHEIADSSKKIADIISVIDGIAFQTNILALNAAVEAARAGEQGRGFAVVAGEVRNLASRSAQAAKEIKALIEDSVSRVDTGSVLVESAGETMNNIVNAVTRVTDIMGEIASASDEQSRGIDQVALAVSEMDRVTQQNASLVQESAAAAAALEEQASRLTQAVSAFRLAASPLTNKPQTPSRPASEQPPAQPRLRIAEQDPNWETF
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Molecular Weight
52.0 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 research on tar-derived recombinant proteins has gained significant attention due to their potential applications in various fields, including biotechnology, medicine, and environmental science. Tar, a complex mixture of organic compounds produced during the pyrolysis of biomass or fossil fuels, contains numerous bioactive molecules and proteins. The study of these proteins is crucial as they may possess unique enzymatic properties and functional characteristics that can be harnessed for industrial processes, such as bioremediation and biofuel production. Additionally, the recombinant technology enables the expression of tar proteins in easier, more controlled systems, allowing for large-scale production and detailed functional studies. This has opened avenues for exploring their characteristics, such as stability, activity under extreme conditions, and interaction with other biomolecules. Through genetic engineering, researchers can modify these proteins to enhance their functionality or tailor them for specific applications. The insights gained from this research can lead to innovative solutions for environmental challenges, novel therapeutic agents, and improved industrial processes, highlighting the importance of tar-derived recombinant proteins in contemporary scientific inquiry.
