Analytical Data
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Gene name
TXNL1
- Application
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Alternative Names
TXNL1；TRP32；Thioredoxin-like Protein 1
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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
O43396
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Expression Region
1-289aa
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AA Sequence
MGSSHHHHHHSSGLVPRGSHMVGVKPVGSDPDFQPELSGAGSRLAVVKFT MRGCGPCLRIAPAFSSMSNKYPQAVFLEVDVHQCQGTAATNNISATPTFL FFRNKVRIDQYQGADAVGLEEKIKQHLENDPGSNEDTDIPKGYMDLMPFI NKAGCECLNESDEHGFDNCLRKDTTFLESDCDEQLLITVAFNQPVKLYSM KFQGPDNGQGPKYVKIFINLPRSMDFEEAERSEPTQALELTEDDIKEDGI VPLRYVKFQNVNSVTIFVQSNQGEEETTRISYFTFIGTPVQATNMNDFKR VVGKKGESH
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Molecular Weight
34 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
TXNL1, or Thioredoxin-like 1, is a vital protein involved in various cellular processes, including redox signaling, cellular stress response, and regulation of apoptosis. Its primary function revolves around maintaining the redox balance within cells, acting as an essential component of the thioredoxin system. Research on TXNL1 has gained momentum due to its implications in multiple diseases, such as cancer, where altered redox status contributes to tumor progression and resistance to therapy. Additionally, TXNL1 has been associated with neurodegenerative diseases, cardiovascular disorders, and inflammatory conditions, highlighting its importance in cellular homeostasis and pathological states. The ability to express and purify recombinant TXNL1 protein has become crucial for advancing our understanding of its biological roles and mechanisms of action. By employing methods such as molecular cloning and expression in suitable host systems, researchers aim to obtain functional TXNL1 protein to investigate its interactions with other biomolecules, elucidate its enzymatic activities, and explore its potential as a therapeutic target. Overall, the study of TXNL1 recombinant protein not only deepens our understanding of its fundamental biological functions but also opens new avenues for therapeutic interventions in diseases linked to redox imbalances.
