Recombinant Human TXNDC/TMX protein (Fc Chimera)
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Recombinant Human TXNDC/TMX protein (Fc Chimera) is a Human Fragment protein, in the 1 to 180 aa range, expressed in HEK 293 cells, with >90%, < 1 EU/µg endotoxin level, suitable for SDS-PAGE.
View Alternative Names
TMX, TXNDC, TXNDC1, PSEC0085, UNQ235/PRO268, TMX1, Thioredoxin-related transmembrane protein 1, Protein disulfide-isomerase TMX1, Thioredoxin domain-containing protein 1, Transmembrane Trx-related protein
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant Human TXNDC/TMX protein (Fc Chimera) (AB276624)
SDS-PAGE analysis of ab276624
Complementary Products
Reactivity data
Sequence info
Properties and storage information
Shipped at conditions
Appropriate short-term storage conditions
Appropriate long-term storage conditions
Aliquoting information
Storage information
Supplementary information
This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
Thioredoxin domain-containing protein plays a significant role in maintaining cellular redox homeostasis. It forms part of a complex network with other oxidoreductases contributing to oxidative protein folding processes essential for proper protein maturation and function. Beyond protein folding TXNDC participates in the detoxification of reactive oxygen species helping protect cells from oxidative stress. This function supports normal cellular metabolism and survival under potentially damaging conditions.
Pathways
TXNDC is active within the oxidative protein folding pathway which involves the transfer of electrons from substrate proteins to the molecular oxidant. It collaborates closely with protein disulfide isomerase (PDI) in this pathway to ensure proper protein structure and function. Another significant pathway includes its involvement in the unfolded protein response (UPR) a mechanism that manages protein misfolding stress in the ER. TXNDC modulates the UPR by influencing the levels of reactive oxygen species indirectly impacting the function of pathways regulated by proteins such as IRE1 and PERK.
Specifications
Form
Lyophilized
General info
Function
Thiredoxin domain-containing protein that participates in various redox reactions through the reversible oxidation of its active center dithiol to a disulfide and catalyze dithiol-disulfide exchange reactions (PubMed : 11152479, PubMed : 37648867). Acts as a key inhibitor of the alternative triglyceride biosynthesis pathway by inhibiting the activity of TMEM68/DIESL at the endoplasmic reticulum, thereby restricting accumulation of triacylglycerol (PubMed : 37648867). The alternative triglyceride biosynthesis pathway mediates formation of triacylglycerol from diacylglycerol and membrane phospholipids (PubMed : 37648867). Acts as a protein disulfide isomerase by catalyzing formation or reduction of disulfide bonds (PubMed : 22228764, PubMed : 29932915). Specifically mediates formation of disulfide bonds of transmembrane proteins at the endoplasmic reticulum membrane (PubMed : 22228764). Involved in endoplasmic reticulum-associated degradation (ERAD) via its protein disulfide isomerase activity by acting on folding-defective polypeptides at the endoplasmic reticulum membrane (PubMed : 29932915). Acts as a negative regulator of platelet aggregation following secretion in the extracellular space (PubMed : 30425049). Acts as a regulator of endoplasmic reticulum-mitochondria contact sites via its ability to regulate redox signals (PubMed : 27502484, PubMed : 31304984). Regulates endoplasmic reticulum-mitochondria Ca(2+) flux (PubMed : 27502484).
Post-translational modifications
Palmitoylated; palmitoylation is required for localization to mitochondria-associated endoplasmic reticulum membrane (MAM).
Target data
Product promise
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