Recombinant Human TXNDC/TMX protein (Fc Chimera) is a Human Fragment protein, in the 1 to 180 aa range, expressed in HEK 293, with >90% purity, < 1 EU/µg endotoxin level and suitable for SDS-PAGE.
>90% SDS-PAGE
< 1 EU/µg
HEK 293 cells
Fc tag C-Terminus
SDS-PAGE
No
M A P S G S L A V P L A V L V L L L W G A P W T H G R R S N V R V I T D E N W R E L L E G D W M I E F Y A P W C P A C Q N L Q P E W E S F A E W G E D L E V N I A K V D V T E Q P G L S G R F I I T A L P T I Y H C K D G E F R R Y Q G P R T K K D F I N F I S D K E W K S I E P V S S W F G P G S V L M S S M S A L F Q L S M W I R T C H N Y F I E D L G L P V W G S
Application | Reactivity | Dilution info | Notes |
---|---|---|---|
Application SDS-PAGE | Reactivity Reacts | Dilution info - | Notes - |
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).
TMX, TXNDC, TXNDC1, PSEC0085, UNQ235/PRO268, Thioredoxin-related transmembrane protein 1, Protein disulfide-isomerase TMX1, Thioredoxin domain-containing protein 1, Transmembrane Trx-related protein
Recombinant Human TXNDC/TMX protein (Fc Chimera) is a Human Fragment protein, in the 1 to 180 aa range, expressed in HEK 293, with >90% purity, < 1 EU/µg endotoxin level and suitable for SDS-PAGE.
>90% SDS-PAGE
< 1 EU/µg
HEK 293 cells
Fc tag C-Terminus
SDS-PAGE
No
No
Human
pH: 7.4
Constituents: 100% PBS
M A P S G S L A V P L A V L V L L L W G A P W T H G R R S N V R V I T D E N W R E L L E G D W M I E F Y A P W C P A C Q N L Q P E W E S F A E W G E D L E V N I A K V D V T E Q P G L S G R F I I T A L P T I Y H C K D G E F R R Y Q G P R T K K D F I N F I S D K E W K S I E P V S S W F G P G S V L M S S M S A L F Q L S M W I R T C H N Y F I E D L G L P V W G S
Fragment
44.4 kDa
1 to 180
Recombinant
Fc tag C-Terminus
Lyophilized
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).
Palmitoylated; palmitoylation is required for localization to mitochondria-associated endoplasmic reticulum membrane (MAM).
Ambient - Can Ship with Ice
-20°C
-20°C
Upon delivery aliquot
Avoid freeze / thaw cycle
This supplementary information is collated from multiple sources and compiled automatically.
TXNDC also known as TMX or thioredoxin domain-containing protein is a protein with enzymatic properties. This protein functions as a disulfide isomerase and is involved in the formation and rearrangement of disulfide bonds within proteins. TXNDC weighs around 38 kDa and localizes primarily in the endoplasmic reticulum (ER). TXNDC facilitates oxidative protein folding by catalyzing thiol-disulfide exchange reactions. Its expression is common in tissues with high protein synthesis demand such as liver and pancreas.
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.
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.
Alterations in TXNDC function have connections to several pathological conditions. One such condition is cancer where imbalances in TXNDC expression levels can contribute to tumor progression and chemoresistance often in coordination with other redox proteins like thioredoxin itself. Additionally improper TXNDC function can relate to neurodegenerative diseases such as Alzheimer's as oxidative stress and protein misfolding are common features. In Alzheimer's TXNDC's involvement in redox regulation and protein homeostasis links it to the broader pathology involving proteins like amyloid-beta and tau.
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SDS-PAGE analysis of ab276624
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