
抗人 MASP1 抗体对
01AB01525
MBL associated serine protease 1 (MASP1) is a modular serine protease that plays a central role in the lectin pathway of the complement system, a key component of innate immunity responsible for recognizing and eliminating pathogens through carbohydrate pattern recognition. Structurally, MASP1 belongs to the C1r/C1s/MASP family and features a serine protease domain that is evolutionarily distinct, with a substrate-binding groove resembling that of trypsin, which accounts for its relatively broad substrate specificity. Unique structural elements, such as an unusually large 60-loop and an internal salt bridge between Asp189 and Arg224, modulate its activity and restrict its specificity compared to trypsin, ensuring controlled proteolytic function in blood. MASP1 is multifunctional, acting not only in complement activation but also cleaving non-complement substrates like fibrinogen and factor XIII, linking it to coagulation processes. Clinically, MASP1 gene variants have been associated with altered protein function, and deficiencies or mutations can influence susceptibility to infections and may contribute to rare developmental disorders.
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技术参数
- 靶点基因名
- MASP1
- 基因别名
- CRARF; CRARF1; PRSS5
- 蛋白别名
- MBL associated serine protease 1; MASP1
- UniProt
- P48740
- 物种
- Human
产品详情
- 靶点名称
- MASP1
- 蛋白名称
- MBL associated serine protease 1
- 蛋白别名
- Mannan-binding lectin serine protease 1; Complement factor MASP-3; Complement-activating component of Ra-reactive factor; Mannose-binding lectin-associated serine protease 1; MASP-1; Mannose-binding protein-associated serine protease; Ra-reactive factor serine protease p100; RaRF; Serine protease 5) [Cleaved into: Mannan-binding lectin serine protease 1 heavy chain; Mannan-binding lectin serine protease 1 light chain]
- 靶点基因名
- MASP1
- 基因别名
- CRARF; CRARF1; PRSS5
- UniProt
- P48740
- 来源物种
- Homo sapiens (Human)
- 物种反应性
- Human
背景介绍
MBL associated serine protease 1 (MASP1) is a modular serine protease that plays a central role in the lectin pathway of the complement system, a key component of innate immunity responsible for recognizing and eliminating pathogens through carbohydrate pattern recognition. Structurally, MASP1 belongs to the C1r/C1s/MASP family and features a serine protease domain that is evolutionarily distinct, with a substrate-binding groove resembling that of trypsin, which accounts for its relatively broad substrate specificity. Unique structural elements, such as an unusually large 60-loop and an internal salt bridge between Asp189 and Arg224, modulate its activity and restrict its specificity compared to trypsin, ensuring controlled proteolytic function in blood. MASP1 is multifunctional, acting not only in complement activation but also cleaving non-complement substrates like fibrinogen and factor XIII, linking it to coagulation processes. Clinically, MASP1 gene variants have been associated with altered protein function, and deficiencies or mutations can influence susceptibility to infections and may contribute to rare developmental disorders.