Analytical Data
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Gene name
TXNDC5
- Application
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Alternative Names
TXNDC5；TLP46；Thioredoxin domain-containing Protein 5
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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
Q8NBS9
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Expression Region
1-324aa
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AA Sequence
MEDAKVYVAKVDCTAHSDVCSAQGVRGYPTLKLFKPGQEAVKYQGPRDFQTLENWMLQTLNEEPVTPEPEVEPPSAPELKQGLYELSASNFELHVAQGDHFIKFFAPWCGHCKALAPTWEQLALGLEHSETVKIGKVDCTQHYELCSGNQVRGYPTLLWFRDGKKVDQYKGKRDLESLREYVESQLQRTETGATETVTPSEAPVLAAEPEADKGTVLALTENNFDDTIAEGITFIKFYAPWCGHCKTLAPTWEELSKKEFPGLAGVKIAEVDCTAERNICSKYSVRGYPTLLLFRGGKKVSEHSGGRDLDSLHRFVLSQAKDEL
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Molecular Weight
63.2 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
TXNDC5, a member of the thioredoxin domain-containing protein family, has garnered significant attention due to its potential roles in various biological processes, including oxidative stress response, protein folding, and cell signaling. Research has indicated that TXNDC5 may be implicated in the regulation of cellular redox states and has been linked to important pathways in diseases such as cancer, neurodegenerative disorders, and metabolic syndromes. The study of TXNDC5 recombinant proteins is crucial for understanding its structural and functional properties, which can provide insights into its mechanisms of action. By utilizing recombinant DNA technology, researchers can produce TXNDC5 in a controlled laboratory environment, allowing for detailed characterization and analysis of its enzymatic activities, interaction with other proteins, and role in cellular processes. Additionally, the recombinant form of TXNDC5 can serve as a valuable tool for therapeutic development, as it may aid in the design of inhibitors or modulators that target its activity in pathological conditions. Overall, the exploration of TXNDC5 recombinant proteins holds promise for elucidating the protein's biological significance and advancing our understanding of its contributions to health and disease.
