Recombinant Human MBL Protein, CF

  (1 citations)     
Datasheet / CoA / SDS
Product Details
Citations (1)
Supplemental Products
  • Purity
    >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
  • Endotoxin Level
    <0.10 EU per 1 μg of the protein by the LAL method.
  • Activity
    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.
  • Source
    Human embryonic kidney cell, HEK293-derived human MBL protein
  • Accession #
  • N-terminal Sequence
  • Predicted Molecular Mass
    24 kDa
    31-36 kDa, reducing conditions
Product Datasheets

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Formulation Lyophilized from a 0.2 μm filtered solution in PBS and Trehalose.
Reconstitution Reconstitute at 500 μg/mL in PBS.
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.
Data Image
When Mannan is coated at 0.1 µg/mL (100 µL/well), Recombinant Human MBL (Catalog # 9086-MB) binds with a typical ED50 of 25-150 ng/mL.
Background: MBL
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).
  • References:
    1. Scorza, M. et al. (2015) Clin. Chim. Acta 451:78.
    2. Matsushita, M. et al. (2013) Arch. Immunol. Ther. Exp. (Warsz.) 61:273.
    3. Ezekowitz, R.A.B. et al. (1988) J. Exp. Med. 167:1034.
    4. Jensen, P.H. et al. (2005) J. Biol. Chem. 280:11043.
    5. Teillet, F. et al. (2005) J. Immunol. 174:2870.
    6. Moller-Kristensen, M. et al. (2007) Int. Immunol. 19:141.
    7. Thiel, S. et al. (2000) J. Immunol. 165:878.
    8. Vorup-Jensen, T. et al. (2000) J. Immunol. 165:2093.
    9. Duus, K. et al. (2010) FEBS J. 277:4956.
  • 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
Related Research Areas

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 Citations: Showing 1 - 1

  1. Expression of Lewis-a glycans on polymorphonuclear leukocytes augments function by increasing transmigration
    Authors: JC Brazil, R Sumagin, SR Stowell, G Lee, NA Louis, RD Cummings, CA Parkos
    J. Leukoc. Biol., 2017;0(0):.
    Species: Human
    Sample Type: Whole Cells
    Application: Bioassay


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