Analytical Data
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Gene name
TXNDC17
- Application
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Alternative Names
14KDA thioredoxin-related protein ;TRP14Protein 42-9-9Thioredoxin-like protein 5
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Species
Human
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Source
E. coli
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Tag
N- GST
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9BRA2
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Expression Region
1-123aa
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Molecular Weight
40.9 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
Related Products
Protein Description
TXNDC17, or Thioredoxin Domain Containing 17, is a protein implicated in several critical cellular processes, including protein folding, redox regulation, and stress response. As a member of the thioredoxin family, TXNDC17 plays a pivotal role in maintaining the balance of oxidized and reduced states within the cell, which is essential for proper cellular function. Research has shown that TXNDC17 is involved in various biological phenomena, such as apoptosis, cell proliferation, and the response to oxidative stress, indicating its potential relevance in various diseases, including cancer and neurodegenerative disorders. The protein has gained attention as a therapeutic target due to its regulatory role in these pathways. Furthermore, the development of recombinant TXNDC17 has opened new avenues for studying its structure-function relationships and interactions with other biomolecules, enhancing our understanding of its physiological and pathological roles. Investigating the properties of TXNDC17 through recombinant technologies may also facilitate the identification of novel therapeutic strategies aimed at modulating its activity to treat diseases associated with protein misfolding and oxidative damage. Overall, the study of TXNDC17 and its recombinant forms represents a significant area of research that bridges molecular biology and clinical applications, potentially leading to advancements in medical treatments and therapeutic interventions.











