Recombinant Human Ficolin-3 Protein, CF


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Product Details

Reactivity HuSpecies Glossary
Applications Binding Activity

Order Details

Recombinant Human Ficolin-3 Protein, CF Summary

Details of Functionality
Measured by its ability to bind biotinylated a-D-Mannose-Polyacrylamide in a functional ELISA.
Mouse myeloma cell line, NS0-derived human Ficolin-3 protein
Lys22-Arg299, with a C-terminal 10-His tag
Accession #
N-terminal Sequence
Protein/Peptide Type
Recombinant Proteins
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.


  • Binding Activity
Theoretical MW
30.7 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.
37 kDa, reducing conditions
Read Publications using
2367-FC in the following applications:

Packaging, Storage & Formulations

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 opening.
  • 3 months, -20 to -70 °C under sterile conditions after opening.
Supplied as a 0.2 μm filtered solution in PBS and NaCl.
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain.


This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Human Ficolin-3 Protein, CF

  • FCN3
  • FCNH
  • Ficolin3
  • Ficolin-3
  • HAKA1
  • H-Ficolin


Human Ficolin-3 (fibrinogen/collagen-like), also called H-ficolin and, previously, Hakata antigen or thermolabile beta -2 macroglycoprotein, is a member of the ficolin family of secreted pattern recognition proteins that belong to the lectin complement activation pathway (1, 2). Ficolin-3 is expressed by bile duct epithelial cells and hepatocytes, and is released into the bile and circulation, where it averages 18 μg/mL (3, 4). It is also secreted by bronchial and alveolar epithelial cells in the lung (3). Mature human Ficolin-3 shares 46% and 52% amino acid (aa) identity with human Ficolin-1 and Ficolin-2, respectively. Ficolin-3 has only been identified in primates and is likely a pseudogene in other species (5). The 35 kDa, 288 aa human Ficolin-3 (isoform 2) contains a signal sequence, an N-terminal collagen domain and a C-terminal fibrinogen-like domain that includes a calcium binding site and two potential N-glycosylation sites. Isoform 1 contains an additional 11 aa between the collagen and fibrinogen-like domains. The collagen domain mediates trimer formation, and a ~650 kDa, 18 subunit oligomer is formed by disulfide links at the N-terminus (2, 6, 7). Ficolin-3 binds a limited set of carbohydrates containing mannose, galactose or D-fucose (2, 6). Binding of microbial carbohydrates has been clearly demonstrated only for the PSA antigen of Aerococcus viridans (4, 8, 9). Pathogen recognition initiates an immune response involving the calcium-dependent interaction of Ficolin-3 with the MBL-associated serine protease (MASP) complex. This cleaves C4 to activate the complement pathway (4, 9). In a secondary role, Ficolins 2 and 3 bind apoptotic cells, activating complement cascades that assist in clearance of the cells (10). Circulating antibodies to Ficolin-3 have been identified in systemic lupus erythematosus (7).

  1. Endo, Y. et al. (2006) Adv. Exp. Med. Biol. 586:265.
  2. Sugimoto, R. et al. (1998) J. Biol. Chem. 273:20721.
  3. Akaiwa, M. et al. (1999) J. Histochem. Cytochem. 47:777.
  4. Krarup, A. et al. (2005) Inf. Immun. 72:1052.
  5. Endo, Y. et al. (2004) Genomics 84:737.
  6. Garlatti, V. et al. (2007) EMBO J. 26:623.
  7. Yae, Y. et al. (1991) Biochim. Biophys. Acta 1078:369.
  8. Tsujimura, M. et al. (2001) Clin. Diag. Lab. Immunol. 8:454.
  9. Matsushita, M. et al. (2002) J. Immunol. 168:3502.
  10. Kuraya, M. et al. (2005) Immunobiology 209:689.

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Publications for Ficolin-3 Isoform 2 (2367-FC)(5)

We have publications tested in 2 confirmed species: Human, Bacteria.

We have publications tested in 3 applications: Binding Assay, Bioassay, ELISA (Standard).

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Binding Assay
ELISA (Standard)
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Showing Publications 1 - 5 of 5.
Publications using 2367-FC Applications Species
H Jang, Y Jun, S Kim, E Kim, Y Jung, BJ Park, J Lee, J Kim, S Lee, J Kim FCN3 functions as a tumor suppressor of lung adenocarcinoma through induction of endoplasmic reticulum stress Cell Death & Disease, 2021;12(4):407. 2021 [PMID: 33859174] (Bioassay, Human) Bioassay Human
D Wolf, N Anto-Miche, H Blankenbac, A Wiedemann, K Buscher, JD Hohmann, B Lim, M Bäuml, A Marki, M Mauler, D Duerschmie, Z Fan, H Winkels, D Sidler, P Diehl, DM Zajonc, I Hilgendorf, P Stachon, T Marchini, F Willecke, M Schell, B Sommer, C von Zur Mu, J Reinöhl, T Gerhardt, EF Plow, V Yakubenko, P Libby, C Bode, K Ley, K Peter, A Zirlik A ligand-specific blockade of the integrin Mac-1 selectively targets pathologic inflammation while maintaining protective host-defense Nat Commun, 2018;9(1):525. 2018 [PMID: 29410422] (Bioassay, Human) Bioassay Human
Aleksandra Man-Kupisi 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 PLoS ONE, 2016;11(5):e0156691. 2016 [PMID: 27232184] (ELISA (Standard), Human) ELISA (Standard) Human
Michalski M, St Swierzko A, Lukasiewicz J, Man-Kupisinska A, Karwaciak I, Przygodzka P, Cedzynski M Ficolin-3 activity towards the opportunistic pathogen, Hafnia alvei. Immunobiology, 2015;220(1):117-23. 2015 [PMID: 25178935] (Bioassay, Bacteria) Bioassay Bacteria
Swierzko A, Lukasiewicz J, Cedzynski M New functional ligands for ficolin-3 among lipopolysaccharides of Hafnia alvei. Glycobiology, 2012;22(2):267-80. 2012 [PMID: 21890891] (Binding Assay, Bacteria) Binding Assay Bacteria

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Gene Symbol FCN3