Analytical Data
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Gene name
TXNDC12
- Application
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Alternative Names
Endoplasmic reticulum resident protein 18 ;ER protein 18 ;ERp18Endoplasmic reticulum resident protein 19 ;ER protein 19 ;ERp19Thioredoxin-like protein p19hTLP19
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Species
Human
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Source
E. coli
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Tag
N- His-SUMO
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
O95881
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Expression Region
27-172aa
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Molecular Weight
32.4 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
The TXNDC12 protein, a member of the thioredoxin-like family, has attracted significant interest due to its potential role in redox regulation and cellular processes such as apoptosis and stress response. Emerging research indicates that TXNDC12 may be involved in various pathological conditions, including cancer and neurodegenerative diseases, where it may affect protein folding and antioxidant defense mechanisms. Studies have shown that TXNDC12 can modulate the activity of crucial signaling pathways, thus influencing cell survival and proliferation. Given its involvement in these processes, understanding the structure and function of TXNDC12 is essential for uncovering its biological roles and therapeutic potentials. Efforts to produce recombinant TXNDC12 protein have focused on elucidating its biochemical properties and interactions with other cellular molecules. By employing techniques such as site-directed mutagenesis and crystallography, researchers aim to characterize the protein's active sites and functional domains. This research not only contributes to a deeper understanding of thioredoxin family proteins but also paves the way for developing targeted interventions in diseases where TXNDC12 is implicated. Overall, studying TXNDC12's molecular characteristics and biological functions could reveal critical insights into the maintenance of cellular redox homeostasis and the broader implications for human health.
