Measured by its binding ability in a functional ELISA. When Mannan is immobilized at 0.1 µg/mL
(100 µL/well), the concentration of
Recombinant Human MBL that produces 50% of the optimal binding response is approximately 25-150 ng/mL.
Human embryonic kidney cell, HEK293-derived human MBL protein Glu21-Ile248
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
<0.10 EU per 1 μg of the protein by the LAL method.
24 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
Human mannose/mannan-binding lectin (MBL) is a 25-30 kDa secreted glycoprotein in the collectin family of pattern-recognition molecules (1, 2). Mature human MBL contains a cysteine-rich region, a collagen-like segment, and a C-type lectin domain that binds to neutral bacterial carbohydrates (3). Human MBL shares 61% amino acid sequence identity with mouse and rat MBL and carries variable post-translation modifications including O-glycosylation and proline and lysine hydroxylation (4). Its collagen-like region mediates MBL association into disulfide-stabilized trimers which further associate into complexes containing three or four copies of the basic trimer (4, 5). MBL is secreted by hepatocytes and opsonizes bacteria through interactions with microbial carbohydrates (5). Tetrameric complexes of MBL show greater carbohydrate binding capacity compared to the trimers (5). MBL multimers can associate with the serine proteases MASP-1, -2, and -3 and promote their cleavage of Complement Component C3 (5-8). Proteolytic cleavage of C3 triggers activation of the complement system and formation of the membrane attack complex, leading to destruction of opsonized bacteria (2). In addition, MBL binds to the scavenger receptor CD91 which mediates the clearance of apoptotic material (9).
Scorza, M. et al. (2015) Clin. Chim. Acta 451:78.
Matsushita, M. et al. (2013) Arch. Immunol. Ther. Exp. (Warsz.) 61:273.
Ezekowitz, R.A.B. et al. (1988) J. Exp. Med. 167:1034.
Jensen, P.H. et al. (2005) J. Biol. Chem. 280:11043.
Teillet, F. et al. (2005) J. Immunol. 174:2870.
Moller-Kristensen, M. et al. (2007) Int. Immunol. 19:141.
Thiel, S. et al. (2000) J. Immunol. 165:878.
Vorup-Jensen, T. et al. (2000) J. Immunol. 165:2093.
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