masp2

Serum protease that plays an important role in the activation of the complement system via mannose-binding lectin. After activation by auto-catalytic cleavage it cleaves C2 and C4, leading to their activation and to the formation of C3 convertase. MASP2 Protein, Rat, Recombinant (His) is expressed in Baculovirus insect cells with C-6xHis tag. The predicted molecular weight is 79.2 kDa and the accession number is Q9JJS8.

MASP2 Protein, Mouse, Recombinant (His) is expressed in E. coli expression system with C-His tag. The predicted molecular weight is 46.6 kDa and the accession number is Q91WP0.

MASP2 Protein, Rat, Recombinant (E. coli, His) is expressed in E. coli expression system with C-His tag. The predicted molecular weight is 46.7 kDa and the accession number is A2VCV7.

MASP2 Protein (Primary Amine Labeling), Rat, Recombinant (His), Biotinylated is expressed in E. coli expression system with C-His tag. The predicted molecular weight is 46.7 kDa and the accession number is A2VCV7.

The pathogenesis of severe acute respiratory disease syndrome (SARS) is not fully understood. One case-control study has reported an association between susceptibility to SARS and mannan-binding lectin (MBL) in China. As the downstream protein of MBL, variants of the MBL-associated serine protease-2 (MASP2) gene may be associated with SARS coronavirus (SARS-CoV) infection in the same population.

MASP2 Protein, Cynomolgus, Recombinant (His) is expressed in E. coli expression system with C-His tag. The predicted molecular weight is 46.8 kDa and the accession number is A0A2K5UJY0.

MASP3 is a member of the MASPs involved in mannan-binding lectin (MBL) complement pathway. The MBL pathway is initiated by the binding of MBL to specific carbohydrate structures found on the surface of a variety of microorganisms. Activation of the complement pathway via MBL is initiated by specific MASPs. Three MASPs have been identified and all have domain structures similar to those of C1r and C1s with a heavy chain (chain A) and a light chain (chain B). Chain A is composed of CUB1, EGF, CUB2, CCP1 and CCP2 while chain B corresponds to the catalytic domain found in many serine proteases. MASP1 and MASP3 are two alternatively spliced products of a single gene, which contain the same A chains but entirely different B chains. Distinct MASPs found in different MBL oligomers may have different biological activities. For example, MASP3, found together with MASP2, downregulates the C4 and C2 cleaving activity of MASP2. The protease activity of MASP3 is first revealed here using rhMASP3CD, which is inhibited by serine protease inhibitors such as Ecotin and AEBSF.