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AB276624

重组人TXNDC/TMX蛋白(Fc Chimera)

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.

查看别名

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

1 Images
SDS-PAGE - Recombinant Human TXNDC/TMX protein (Fc Chimera) (AB276624)
  • SDS-PAGE

Supplier Data

SDS-PAGE - Recombinant Human TXNDC/TMX protein (Fc Chimera) (AB276624)

SDS-PAGE analysis of ab276624

关键信息

纯度

>90% SDS-PAGE

内毒素水平

< 1 EU/µg

表达系统

HEK 293 cells

标签

Fc tag C-Terminus

应用

SDS-PAGE

applications

生物活性

No

访问

Q9H3N1

不含动物源

No

不含载体蛋白

No

种属

Human

存储溶液

pH: 7.4 Constituents: PBS

storage-buffer

反应性数据

{ "title": "Reactivity Data", "filters": { "stats": ["", "Reactivity", "Dilution Info", "Notes"] }, "values": { "SDS-PAGE": { "reactivity":"TESTED_AND_REACTS", "dilution-info":"", "notes":"<p></p>" } } }

序列信息

[{"linker":null,"sequence":"MAPSGSLAVPLAVLVLLLWGAPWTHGRRSNVRVITDENWRELLEGDWMIEFYAPWCPACQNLQPEWESFAEWGEDLEVNIAKVDVTEQPGLSGRFIITALPTIYHCKDGEFRRYQGPRTKKDFINFISDKEWKSIEPVSSWFGPGSVLMSSMSALFQLSMWIRTCHNYFIEDLGLPVWGS","proteinLength":"Fragment","predictedMolecularWeight":"44.4 kDa","actualMolecularWeight":null,"aminoAcidEnd":180,"aminoAcidStart":1,"nature":"Recombinant","expressionSystem":"HEK 293 cells","accessionNumber":"Q9H3N1","tags":[{"tag":"Fc","terminus":"C-Terminus"}]}]

性能和储存信息

形式
Lyophilized
运输条件
Ambient - Can Ship with Ice
推荐的短期储存条件
-20°C
推荐的长期储存条件
-20°C
分装信息
Upon delivery aliquot
储存信息
Avoid freeze / thaw cycle
False

补充信息

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.
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.

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.

常规信息

功能

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).

翻译后修饰

Palmitoylated; palmitoylation is required for localization to mitochondria-associated endoplasmic reticulum membrane (MAM).

亚细胞定位

Mitochondrion membrane

产品实验方案

靶点信息

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).
See full target information TMX1

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