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抗人 TXNDC5 抗体对
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抗人 TXNDC5 抗体对

01AB00619

Thioredoxin domain containing 5 (TXNDC5) is a member of the protein disulfide isomerase (PDI) family, primarily located in the endoplasmic reticulum (ER) but also found in other cellular compartments. It is a 48 kDa protein with three thioredoxin-like domains (Trx1, Trx2, and Trx3) that can independently catalyze the formation, isomerization, and degradation of disulfide bonds in proteins, thereby influencing protein conformation, activity, and stability. TXNDC5 is highly expressed in hypoxic conditions and has been associated with various diseases, including inflammatory diseases such as rheumatoid arthritis, fibrosis, and tumors, due to its role in redox homeostasis and protein folding. Its unique molecular architecture, with long flexible loops connecting the Trx-like domains, allows for rapid and promiscuous introduction of disulfide bonds into unfolded substrates.

Human
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技术参数

靶点基因名
TXNDC5
基因别名
TLP46
蛋白别名
thioredoxin domain containing 5; TXNDC5
UniProt
Q8NBS9
物种
Human

产品详情

靶点名称
TXNDC5
蛋白名称
thioredoxin domain containing 5
蛋白别名
Thioredoxin domain-containing protein 5; Endoplasmic reticulum resident protein 46; ER protein 46; ERp46; Thioredoxin-like protein p46
靶点基因名
TXNDC5
基因别名
TLP46
UniProt
Q8NBS9
来源物种
Homo sapiens (Human)
物种反应性
Human

背景介绍

Thioredoxin domain containing 5 (TXNDC5) is a member of the protein disulfide isomerase (PDI) family, primarily located in the endoplasmic reticulum (ER) but also found in other cellular compartments. It is a 48 kDa protein with three thioredoxin-like domains (Trx1, Trx2, and Trx3) that can independently catalyze the formation, isomerization, and degradation of disulfide bonds in proteins, thereby influencing protein conformation, activity, and stability. TXNDC5 is highly expressed in hypoxic conditions and has been associated with various diseases, including inflammatory diseases such as rheumatoid arthritis, fibrosis, and tumors, due to its role in redox homeostasis and protein folding. Its unique molecular architecture, with long flexible loops connecting the Trx-like domains, allows for rapid and promiscuous introduction of disulfide bonds into unfolded substrates.