Unique ELISA to elucidate the role of human MASP-3
Hycult Biotech presents a specific assay for the quantification of human MASP-3 in plasma (Cat.# HK339)
The mannan-binding lectin (MBL) pathway of the complement system is initiated by the binding of MBL or ficolin to specific carbohydrate structures found on the surface of a variety of microorganisms. This binding is followed by the activation of MBL-associated serine proteases (MASPs).
MASP-3 is an alternatively spliced product from the MASP-1 gene, containing an identical A chain, but an entirely different B chain. MASP-3 is an approximately 100 kD protein and associates with both MBL and L-ficolin in the presence of Ca2+. The MASP-3 dimer can be disrupted by EDTA.
MASP-3 function
Unlike MASP-2, no proteolytic activity on complement proteins C2, C3 and C4 for MASP-3 has been detected. MASP-3 exerts inhibitory activity on MASP-2 function. However, no natural substrates of MASP-3 are known.
MASP-3 expression
MASP-3 is expressed mainly but not exclusively in the liver and is secreted into the blood. The high expression of MASP-3 in astrocytes indicates that MASP-3 might also be involved in other functions that could be important in the brain.
MASP-3 concentration in healthy human blood is normally distributed with a mean value of 3796 ng/ml. MASP-3 is present at birth at approximately 80% of the level measured 6, 9 and 12 months after birth. The MASP-3 level is stable throughout a 1-year period. The role of MASP-3 in biological processes is not clear. In multiple sclerosis (MS) patients, MASP-3 levels seem to be negatively correlated with MS-associated human endogenous retrovirus HERV-H (median MASP-3 levels: 4539 ng/ml). MASP-3 deficiencies have not yet been reported.
Special features of the assay
1. Thiel, S. et al; An assay for mannan-binding lectin (MBL) associated serine protease 3, MASP-3
2. Zundel, S. et al; Characterization of recombinant mannan-binding lectin-associated serine protease (MASP)-3 suggests an activation mechanisms different from that of MASP-1 and MASP-2. J Immunol 2004, 172: 4342
3. Moller-Kristensen, M. et al; Cooperation between MASP-1 and MASP-2 in the generation of C3 convertase through the MBL pathway. Int Immunol 2006, 19: 141
4. Kuraya, M. et al; Expression of H-ficolin/Hakata antigen, mannose-binding lectin-associated serine protease (MASP)-1 and MASP-3 by human glioma cell line T98G. Int Immunol 2003, 15: 109
5. Sorensen, R. et al; Mannan-binding-lectin-associated serine protease, characteristics and disease associations. Springer Semin Immun 2005, 27: 299
6. Christensen, T. et al; Gene-environment interactions in multiple sclerosis: innate and adaptive immune responses to human endogenous retrovirus and herpesvirus antigens and the lectin complement activation pathway. J Neuroimmunol 2007, 183: 175
Available reagents for MASP-3 related research:
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Cat. No. |
Product |
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MBL, Human, ELISA |
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MASP-2, Human, ELISA |
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MBL/MASP-2, functional, Human, ELISA |
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L-Ficolin, Human, ELISA |
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H-Ficolin, Human, ELISA |