Recombinant Human MBL Protein

Newer Version Available: 9086-MB

Discontinued Product

2307-MB has been discontinued and is replaced by 9086-MB.

Product Details
Citations (7)

Recombinant Human MBL Protein Summary

>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Level
<0.10 EU per 1 μg of the protein by the LAL method.
Measured by its ability to bind with Mannan in a functional ELISA.
Mouse myeloma cell line, NS0-derived human MBL protein
Accession #
N-terminal Sequence
Structure / Form
Predicted Molecular Mass
24 kDa (monomer)
29-33 kDa, reducing conditions

Product Datasheets


Formulation Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose and BSA as a carrier protein.
Reconstitution Reconstitute at 100 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin.
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.
Stability & Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
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Background: MBL

Human mannose/mannan-binding lectin (MBL; also 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 bacteria 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 is 63%, 61% and 65% aa identical to mouse, porcine and bovine MBL, respectively.

  1. Gadjeva, M. et al. (2004) Mol. Immunol. 41:113.
  2. Kilpatrick, D.C. (2003) Biochem. Soc. Trans. 31:745.
  3. Presanis, J.S. et al. (2003) Biochem. Soc. Trans. 31:748.
  4. Sastry, K. et al. (1989) J. Exp. Med. 170:1175.
  5. Jensen, P.H. et al. (2005) J. Biol. Chem. 280:11043.
  6. Larsen, F. et al. (2004) J. Biol. Chem. 279:21302.
  7. Teillet, F. et al. (2005) J. Immunol. 174:2870.
  8. Terai, I. et al. (2003) Eur. J. Immunol. 33:2755.
Long Name
Mannose Binding Lectin
Entrez Gene IDs
4153 (Human)
Alternate Names
COLEC1; COLEC1collectin-1; Collectin-1; HSMBPC; Mannan-binding protein; mannose-binding lectin (protein C) 2, soluble (opsonic defect); mannose-binding lectin (protein C) 2, soluble; Mannose-binding lectin; mannose-binding protein C; MBL; MBL2; MBL2D; MBLmannan-binding lectin; MBP; MBP1; MBP1mannose-binding lectin 2, soluble (opsonic defect); MBP-C; MGC116832; MGC116833

Citations for Recombinant Human MBL Protein

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.

7 Citations: Showing 1 - 7
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  1. A New Ligand-Based Method for Purifying Active Human Plasma-Derived Ficolin-3 Complexes Supports the Phenomenon of Crosstalk between Pattern-Recognition Molecules and Immunoglobulins
    Authors: Aleksandra Man-Kupisi
    PLoS ONE, 2016;11(5):e0156691.
    Species: Human
    Sample Types: Plasma
    Applications: ELISA (Standard)
  2. Mannose-Binding Lectin Inhibits the Motility of Pathogenic Salmonella by Affecting the Driving Forces of Motility and the Chemotactic Response
    Authors: J Xu, S Nakamura, MS Islam, Y Guo, K Ihara, R Tomioka, M Masuda, H Yoneyama, E Isogai
    PLoS ONE, 2016;11(4):e0154165.
    Species: Human
    Sample Types: Bacteria
    Applications: Bioassay
  3. Differential ability to resist to complement lysis and invade host cells mediated by MBL in R4 and 860 strains of Trypanosoma cruzi.
    Authors: Evans-Osses I, Mojoli A, Beltrame M, da Costa D, DaRocha W, Velavan T, de Messias-Reason I, Ramirez M
    FEBS Lett, 2014;588(6):956-61.
    Species: Human
    Sample Types: Serum
    Applications: Bioassay
  4. MBL-mediated opsonophagocytosis of Candida albicans by human neutrophils is coupled with intracellular Dectin-1-triggered ROS production.
    Authors: Li D, Dong B, Tong Z, Wang Q, Liu W, Wang Y, Liu W, Chen J, Xu L, Chen L, Duan Y
    PLoS ONE, 2012;7(12):e50589.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  5. 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.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  6. Variant G57E of Mannose Binding Lectin Associated with Protection against Tuberculosis Caused by Mycobacterium africanum but not by M. tuberculosis.
    Authors: Thye T, Niemann S, Walter K, Homolka S, Intemann CD, Chinbuah MA, Enimil A, Gyapong J, Osei I, Owusu-Dabo E, Rusch-Gerdes S, Horstmann RD, Ehlers S, Meyer CG
    PLoS ONE, 2011;6(6):e20908.
    Species: Bacteria
    Sample Types: Bacteria
    Applications: Binding Assay
  7. Pichia pastoris-produced mucin-type fusion proteins with multivalent O-glycan substitution as targeting molecules for mannose-specific receptors of the immune system.
    Authors: Gustafsson A, Sjoblom M, Strindelius L, Johansson T, Fleckenstein T, Chatzissavidou N, Lindberg L, Angstrom J, Rova U, Holgersson J
    Glycobiology, 2011;21(8):1071-86.
    Species: Human
    Sample Types: Recombinant Protein
    Applications: Surface Plasmon Resonance


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