人 Extracellular Matrix Protein 1 抗体对
01AB02069
Extracellular matrix protein 1 (Extracellular Matrix Protein 1) is a secreted glycoprotein that plays a critical role in regulating basement membrane integrity, angiogenesis, and endochondral bone formation. It interacts with various extracellular matrix components, including perlecan, laminin 332, fibulin-1C/D, fibulin-3, and heparin, to modulate structural stability and signaling. The protein exists in multiple isoforms that influence AKT/FAK signaling pathways and cellular stemness. Pathogenic biallelic loss-of-function mutations in the ECM1 gene cause lipoid proteinosis, a rare condition characterized by hyaline deposits in the skin and mucosa, hoarseness, and temporal lobe calcifications. Additionally, overexpression of this protein is frequently associated with epithelial–mesenchymal transition, tumor progression, and poor prognosis in several malignancies, such as ovarian and breast carcinomas.
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技术参数
- 靶点基因名
- ECM1
- 蛋白别名
- extracellular matrix protein 1; Extracellular Matrix Protein 1
- UniProt
- Q16610
- 物种
- Human
产品详情
- 靶点名称
- Extracellular Matrix Protein 1
- 蛋白名称
- extracellular matrix protein 1
- 蛋白别名
- Extracellular matrix protein 1; Secretory component p85
- 靶点基因名
- ECM1
- UniProt
- Q16610
- 来源物种
- Homo sapiens (Human)
- 物种反应性
- Human
背景介绍
Extracellular matrix protein 1 (Extracellular Matrix Protein 1) is a secreted glycoprotein that plays a critical role in regulating basement membrane integrity, angiogenesis, and endochondral bone formation. It interacts with various extracellular matrix components, including perlecan, laminin 332, fibulin-1C/D, fibulin-3, and heparin, to modulate structural stability and signaling. The protein exists in multiple isoforms that influence AKT/FAK signaling pathways and cellular stemness. Pathogenic biallelic loss-of-function mutations in the ECM1 gene cause lipoid proteinosis, a rare condition characterized by hyaline deposits in the skin and mucosa, hoarseness, and temporal lobe calcifications. Additionally, overexpression of this protein is frequently associated with epithelial–mesenchymal transition, tumor progression, and poor prognosis in several malignancies, such as ovarian and breast carcinomas.