
人 CHORDC1 抗体对
01AB02597
Cysteine and histidine rich domain containing 1 (CHORDC1), also known as Morgana or CHP-1, is a highly conserved protein characterized by tandem CHORD domains, each about 60 amino acids long, that bind two zinc ions and are essential for its structural integrity and function as a co-chaperone. CHORDC1 primarily interacts with the molecular chaperone HSP90 in a nucleotide-dependent manner, facilitating chaperone-mediated protein folding, centrosome duplication, and the negative regulation of Rho-dependent kinase activity. It is specifically required for the proper trafficking and maturation of the epidermal growth factor receptor (EGFR), ensuring its localization to the plasma membrane; loss of CHORDC1 leads to EGFR accumulation in the endoplasmic reticulum and impaired MAPK pathway signaling, as demonstrated in both C. elegans and human cells. In disease contexts, elevated CHORDC1 expression in cancer cells has been linked to aberrant NF-κB signaling, promotion of metastatic behavior, and modulation of the tumor microenvironment by affecting immune cell recruitment and cytokine production.
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技术参数
- 靶点基因名
- CHORDC1
- 基因别名
- CHP1
- 蛋白别名
- cysteine and histidine rich domain containing 1; CHORDC1
- UniProt
- Q9UHD1
- 物种
- Human
产品详情
- 靶点名称
- CHORDC1
- 蛋白名称
- cysteine and histidine rich domain containing 1
- 蛋白别名
- Cysteine and histidine-rich domain-containing protein 1; CHORD domain-containing protein 1; CHORD-containing protein 1; CHP-1; Protein morgana
- 靶点基因名
- CHORDC1
- 基因别名
- CHP1
- UniProt
- Q9UHD1
- 来源物种
- Homo sapiens (Human)
- 物种反应性
- Human
背景介绍
Cysteine and histidine rich domain containing 1 (CHORDC1), also known as Morgana or CHP-1, is a highly conserved protein characterized by tandem CHORD domains, each about 60 amino acids long, that bind two zinc ions and are essential for its structural integrity and function as a co-chaperone. CHORDC1 primarily interacts with the molecular chaperone HSP90 in a nucleotide-dependent manner, facilitating chaperone-mediated protein folding, centrosome duplication, and the negative regulation of Rho-dependent kinase activity. It is specifically required for the proper trafficking and maturation of the epidermal growth factor receptor (EGFR), ensuring its localization to the plasma membrane; loss of CHORDC1 leads to EGFR accumulation in the endoplasmic reticulum and impaired MAPK pathway signaling, as demonstrated in both C. elegans and human cells. In disease contexts, elevated CHORDC1 expression in cancer cells has been linked to aberrant NF-κB signaling, promotion of metastatic behavior, and modulation of the tumor microenvironment by affecting immune cell recruitment and cytokine production.