Anti-MASP1 Antibody Picoband® Cy3 Conjugated

This gene encodes a serine protease that functions as a component of the lectin pathway of complement activation. The complement pathway plays an essential role in the innate and adaptive immune response. The encoded protein is synthesized as a zymogen and is activated when it complexes with the pathogen recognition molecules of lectin pathway, the mannose-binding lectin and the ficolins. This protein is not directly involved in complement activation but may play a role as an amplifier of complement activation by cleaving complement C2 or by activating another complement serine protease, MASP-2. The encoded protein is also able to cleave fibrinogen and factor XIII and may may be involved in coagulation. A splice variant of this gene which lacks the serine protease domain functions as an inhibitor of the complement pathway. Alternate splicing results in multiple transcript variants.

MASP1; CRARF; CRARF1; PRSS5; Mannan-binding lectin serine protease 1; EC 3.4.21.-; 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]

E.coli-derived human MASP1 recombinant protein (Position: R169-E580) . Human MASP1 shares 84.5% and 83.3% amino acid (aa) sequence identity with mouse and rat MASP1, respectively.

1. Dahl, M. R., Thiel, S., Matsushita, M., Fujita, T., Willis, A. C., Christensen, T., Vorup-Jensen, T., Jensenius, J. C. MASP-3 and its association with distinct complexes of the mannan-binding lectin complement activation pathway. Immunity 15: 127-135, 2001. 2. Degn, S. E., Jensen, L., Hansen, A. G., Duman, D., Tekin, M., Jensenius, J. C., Thiel, S. Mannan-binding lectin-associated serine protease (MASP) -1 is crucial for lectin pathway activation in human serum, whereas neither MASP-1 nor MASP-3 is required for alternative pathway function. J. Immun. 189: 3957-3969, 2012. 3. Dobo, J., Harmat, V., Beinrohr, L., Sebestyen, E., Zavodszky, P., Gal, P. MASP-1, a promiscuous complement protease: structure of its catalytic region reveals the basis of its broad specificity. J. Immun. 183: 1207-1214, 2009.