Analytical Data
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Gene name
Trx
- Application
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Alternative Names
Trx；TRDX；TRX；TRX1；Thioredoxin
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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
P10599
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Expression Region
1-105aa
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AA Sequence
MVKQIESKTA FQEALDAAGD KLVVVDFSAT WCGPCKMIKP FFHSLSEKYS NVIFLEVDVD DCQDVASECE VKCMPTFQFF KKGQKVGEFS GANKEKLEAT INELV
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Molecular Weight
12 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 Trx (thioredoxin) recombinant proteins has garnered significant attention due to their crucial role in various biological processes, including redox regulation, antioxidant defense, and protein folding. Thioredoxins are small proteins that possess a characteristic active site, facilitating the reduction of disulfide bonds in proteins, which is fundamental for maintaining cellular homeostasis and responding to oxidative stress. Research in this area has expanded, as recombinant Trx proteins are leveraged for therapeutic applications, including cancer treatment and enhancing the immune response. Additionally, Trx has been utilized as a fusion tag in protein expression systems, streamlining the purification and characterization of target proteins. The ability to produce Trx as recombinant proteins in various expression systems, including bacteria, yeast, and mammalian cells, has accelerated the exploration of its functional properties and potential applications. Investigations into the structural and functional dynamics of Trx have revealed insights into its mechanism of action and interactions with other cellular components. Moreover, the manipulation of Trx pathways holds promise in the development of novel strategies for disease intervention and biotechnological applications, making it a focal point of ongoing research in molecular biology and therapeutic development.
