人 ERp57 抗体对
01AB01279
Protein disulfide isomerase family A member 3 (PDIA3) is an endoplasmic reticulum-resident thiol oxidoreductase that catalyzes the formation, isomerization, and reduction or oxidation of disulfide bonds in newly synthesized proteins, ensuring their proper folding and structural stability. PDIA3 interacts with lectin chaperones such as calreticulin and calnexin, playing a crucial role in the calnexin/calreticulin cycle and the assembly of the major histocompatibility complex (MHC) class I peptide loading complex, which is essential for antigen presentation. It also acts as a redox sensor, modulating cell growth and death in response to oxygen levels, and participates in cytoskeletal organization and cytokine-dependent signaling pathways, including STAT3 signaling. Beyond its protein-folding functions, PDIA3 is upregulated during cellular stress and is implicated in diseases such as cancer, where its elevated expression is associated with tumor progression, and in viral infections, where it facilitates viral entry and replication.
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技术参数
- 靶点基因名
- PDIA3
- 基因别名
- ERP57; ERP60; GRP58
- 蛋白别名
- protein disulfide isomerase family A member 3; ERp57
- UniProt
- P30101
- 物种
- Human
产品详情
- 靶点名称
- ERp57
- 蛋白名称
- protein disulfide isomerase family A member 3
- 蛋白别名
- Protein disulfide-isomerase A3; 58 kDa glucose-regulated protein; 58 kDa microsomal protein; p58; Disulfide isomerase ER-60; Endoplasmic reticulum resident protein 57; ER protein 57; ERp57; Endoplasmic reticulum resident protein 60; ER protein 60; ERp60
- 靶点基因名
- PDIA3
- 基因别名
- ERP57; ERP60; GRP58
- UniProt
- P30101
- 来源物种
- Homo sapiens (Human)
- 物种反应性
- Human
背景介绍
Protein disulfide isomerase family A member 3 (PDIA3) is an endoplasmic reticulum-resident thiol oxidoreductase that catalyzes the formation, isomerization, and reduction or oxidation of disulfide bonds in newly synthesized proteins, ensuring their proper folding and structural stability. PDIA3 interacts with lectin chaperones such as calreticulin and calnexin, playing a crucial role in the calnexin/calreticulin cycle and the assembly of the major histocompatibility complex (MHC) class I peptide loading complex, which is essential for antigen presentation. It also acts as a redox sensor, modulating cell growth and death in response to oxygen levels, and participates in cytoskeletal organization and cytokine-dependent signaling pathways, including STAT3 signaling. Beyond its protein-folding functions, PDIA3 is upregulated during cellular stress and is implicated in diseases such as cancer, where its elevated expression is associated with tumor progression, and in viral infections, where it facilitates viral entry and replication.