MASP1 polyclonal antibody

P48740

Mannose (or mannan)-binding lectin (MBL), also known as serum mannose-binding protein (MBP), initiates the lectin branch of the innate immune response by binding to the surface of potentially pathogenic microorganisms and initiating complement fixation through an N-terminal collagen-like domain. MBL is a key component in immune response in that it can directly trigger neutralization of invading microorganisms by an Ab-independent mechanism. Mutations of human MBL are associated with immunodeficiency resulting from a reduction in the ability of the mutant MBL to initiate complement fixation. In human, three types of MBL-associated serine proteases, MASP-1, MASP-2 and MASP-3, and a truncated form of MASP-2 (small MBL-associated protein, sMAP or MAp19) complex with MBL to activate the lectin pathway of the complement system. MASP-3 is an alternatively spliced product from the MASP-1 gene. The heavy/A chains are identical between MASP-1 and MASP-3 but the light/B chains are entirely different. Activated MASPs subsequently cleave and activate downstream components of the complement pathway.

The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen and the purity is > 95% (by SDS-PAGE).

MASP1 pAb detects endogenous levels of MASP1 protein.

ca. 47 kDa

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, MASP1, CRARF, CRARF1, PRSS5