Human MBL Antibody
Human MBL Antibody Summary
Accession # AAH96182
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
Human mannose/mannan-binding lectin (MBL; gene name MBL2; also called MBP-C) is a 25 kDa member of the collectin family of pattern-recognition molecules (1‑3). It is a secreted glycoprotein that is synthesized as a 248 amino acid (aa) precursor that contains a 20 aa signal sequence, a 21 aa cysteine-rich region (with three cysteines) a 58 aa collagen-like segment and a 111 aa C-type lectin domain that binds to neutral bacterial carbohydrates (3, 4). The molecule is O-glycosylated and contains multiple hydroxylated prolines and lysines (3, 5). Functionally, the molecule operates as a multimer/oligomer. The basic structural unit is a homotrimer. The homotrimer is created by the formation of interchain disulfide bonds among the cysteine-rich regions, plus a helical interaction of the collagen-like domains of each participating polypeptide (5). Mutations in the collagen region are known to interfere with proper trimer and subsequent oligomer formation (6). Once formed, the trimer, as a unit, oligomerizes with other trimers to form high molecular weight complexes. Although the exact nature of these complexes are unclear, it would appear that a three trimer complex (230 kDa) and a four trimer complex (305 kDa) constitute much of the circulating MBL (7). It is within the context of these oligomers that MBL performs its functions. After secretion by hepatocytes, oligomerized MBL will both associate with serine proteases (MASP-1, 2 & 3) and bind to bacterial carbohydrates. If the MBL complex is small, opsonization of bacreria occurs. If the complex is large, the MASPs are engaged and a complement attack complex is generated, destroying bound bacteria (3, 7, 8). Human MBL shares 63%, 61% and 65% aa identity with mouse, porcine and bovine MBL, respectively.
- Gadjeva, M. et al. (2004) Mol. Immunol. 41:113.
- Kilpatrick, D.C. (2003) Biochem. Soc. Trans. 31:745.
- Presanis, J.S. et al. (2003) Biochem. Soc. Trans. 31:748.
- Sastry, K. et al. (1989) J. Exp. Med. 170:1175.
- Jensen, P.H. et al. (2005) J. Biol. Chem. 280:11043.
- Larsen, F. et al. (2004) J. Biol. Chem. 279:21302.
- Teillet, F. et al. (2005) J. Immunol. 174:2870.
- Terai, I. et al. (2003) Eur. J. Immunol. 33:2755.
Citation for Human MBL Antibody
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
1 Citation: Showing 1 - 1
A single asparagine-linked glycosylation site of the severe acute respiratory syndrome coronavirus spike glycoprotein facilitates inhibition by mannose-binding lectin through multiple mechanisms.
Authors: Zhou Y, Lu K, Pfefferle S, Bertram S, Glowacka I, Drosten C, Pohlmann S, Simmons G
J. Virol., 2011;84(17):8753-64.
Sample Types: Whole Cells
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