MASP-1, Human, clone 3/3

The anti MASP-1 monoclonal antibody clone 3/3 recognize the unique MASP-1 serine protease (SP) domain. Mannan-binding lectin serine protease 1 or mannose-associated serine protease 1 (MASP-1) is an enzyme that is encoded by the MASP1 gene. Three types of human MASP have been reported, MASP-1, MASP-2 and MASP-3. MASP-1 is a serine protease that functions as a component of the lectin pathway of the complement system. The lectin pathway can be activated by the pathogen recognition receptors (PRRs) collectins (such as MBL and collectin kidney 1 (CL-K1 or CL-11) or by ficolins (ficolin-1 or M-ficolin, ficolin-2 or L-ficolin, and ficolin-3 or H-ficolin). The PRRs recognize carbohydrate and acetylated residues on the surface of pathogens and altered cells. After binding, MASP-1 zymogen auto activates and trans activates MASP-2. MASP-2 further cleaves the C4 complement component, whereas both MASP-1 and MASP-2 cleave C2. This leads to the formation of the C3 convertase (C4bC2b). The C3 convertase cleaves C3 leading to complement terminal pathway activation and thus mediating the destruction of infectious agents.