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抗人 MASP1 抗体对
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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.

Human
规格起售价
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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.