Analytical Data
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Gene name
TXNDC
- Application
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Alternative Names
Thioredoxin-related transmembrane Protein 1. Protein disulfide-isomerase TMX1. EC:5.3.4.1. Thioredoxin domain-containing Protein 1. Transmembrane Trx-related Protein
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Species
Human
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Source
E. coli
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Tag
GST-tag at N-terminal
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
Q9H3N1
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Expression Region
1-280 aa
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AA Sequence
MAPSGSLAVPLAVMVPLLWGAPWTHGRRSNVRVITDENWRELLEGDWMIEFYAPWCPACQNLQPEWESFAEWGEDLEVNIAKVDVTEQPGLSGRFIINALPTIYHCKDGEFRRYQGPRTKKDFINFISDKEWKSIEPVSSWFGPGSVLMSSMSALFQLSMWIRTCHNYFIEDLGLPVWGSYTVFALATLFSGLLLGLCMIFVADCLCPSKRRRPQPYPYPSKKLLSESAQPLKKVEEEQEADEEDVSEEEAESKEGTNKDFPQNAIRQRSLGPSLATDKS
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Molecular Weight
58.2 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
TXNDC (thioredoxin domain-containing protein) is a crucial player in cellular redox regulation and protein folding, particularly within the endoplasmic reticulum (ER). Research has shown that TXNDC is involved in the oxidative stress response and the maintenance of protein homeostasis, making it a significant focus in the context of various diseases, including cancer and neurodegenerative disorders. Given the importance of protein misfolding in many pathological conditions, scientists have been motivated to explore the therapeutic potential of TXNDC-based recombinant proteins. Recent studies have suggested that the manipulation of TXNDC function could enhance the efficiency of protein folding and rescue misfolded proteins, offering avenues for biomedical interventions. Furthermore, the role of TXNDC in modulating cellular signaling pathways underscores its potential as a target for drug development. Overall, the investigation of TXNDC recombinant proteins not only aims to unravel the molecular mechanisms underlying protein homeostasis but also seeks to harness this knowledge for therapeutic applications in disease management.
