
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.
| 规格 | 起售价 |
|---|---|
| 登录后可查看 | |
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.