Dectin-1, Recombinant, Human (C-type lectin domain family 7 member A, Dendritic cell-associated C-type lectin 1, DC-associated C-type lectin 1, Beta-glucan receptor, C-type lectin superfamily member 12, CLEC7A, BGR, CLECSF12, DECTIN1, UNQ539/PRO1082)

Dectin-1, also known as CLEC7A and the b-glucan receptor, is a 33kD type II transmembrane C-type lectin that participates in the innate immune response to fungal pathogens. Although Dectin-1 structurally resembles other CLEC molecules, it binds its ligands in a calcium-independent manner (1, 2). Mature human Dectin-1 consists of a short N-terminal ITAM-containing cytoplasmic tail, a transmembrane segment, and a C-terminal stalk with carbohydrate recognition domain (CRD) in the extracellular domain (3, 4). Alternate splicing generates one major splice form that lacks the stalk region (3-5). This isoform is expressed on the surface of monocytes, macrophages, myeloid DC, neutrophils, eosinophils, B cells, and CD4+ T cells (6). The CRD selectively binds b-glucan polymers, a major component of yeast and mycobacterial cell walls (5-7). Yeast b-glucan is accessible to Dectin-1 only during the process of cell budding. Dectin-1 does not recognize the filamentous form of yeast (8). Dectin-1 mediates the phagocytosis of zymosan particles and intact yeast (8-10). In the membrane, Dectin-1 co-localizes with TLR2 in the presence of zymosan, and the two receptors cooperate in ligand recognition and the propagation of proinflammatory signaling (9,11-13). Dectin-1 also interacts with tetraspanin CD37. This increases its stability on the cell membrane and inhibits ligand-induced signaling (14). Dectin-1 knockout mice show increased susceptibility to pathogenic infection (15-16). The CRD of human Dectin-1 shares 77%, 60%, and 60% aa sequence identity with that of bovine, mouse and rat Dectin-1, respectively. It shares 29%-39% aa sequence identity with the CRD of other subgroup members, including CLEC-1, CLEC-2, CLEC9A, CLEC12B, LOX-1, and MICL.\n\nSource: \nHuman CD33 signal peptide (Met 1-Ala 16) HHHHHHHHHH Human Dectin-1 (Thr 66-Met 201). A DNA sequence encoding the extracellular domain of human Dectin-1 (amino acid residues 66-201; Accession # NP_072092) was fused to the signal peptide of human CD33 and a 10X histidine tag at the N-terminus. The protein was expressed in a mouse myeloma cell line, NS0.\n\nMolecular Mass: \nThe recombinant human Dectin-1, generated by the removal of the signal peptide region, is a monomeric protein. Based on N-terminal sequencing, the protein begins with the 10X histidine tag and has a calculated molecular mass of approximately 16.8 kD.\n\nEndotoxin Level: \n< 0.1 EU per 1 microg of the protein as determined by the LAL method.\n\nActivity: \nMeasured by its ability to bind biotinylated laminarin (1, 3-b-glucan) with an estimated KD < 5nM.\n\nReconstitution: \nIt is recommended that sterile phosphate-buffered saline be added to the vial to prepare a working stock solution of no less than 100ug/ml. The carrier-free protein should be used immediately upon reconstitution to avoid losses in activity due to non-specific binding to the inside surface of the vial. For long term storage as a dilute solution, a carrier protein (e.g. 0.1% HSA or BSA) should be added to the vial.\n\nStorage and Stability: \nLyophilized samples are stable for up to twelve months at -20 degrees C. Upon reconstitution, this protein, in the presence of a carrier protein, can be stored under sterile conditions at 2-8 degrees C for one month or at -20 degrees C in a manual defrost freezer for three months without detectable loss of activity. Avoid repeated freeze-thaw cycles.

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SPECIFICATIONS

Catalog Number

D1876-48

Size

50ug

Form

Supplied as a lyophilized powder in PBS.

Purity

(same/more than) 90%, as determined by SDS-PAGE and visualized by silver stain.

References

1. Kanazawa, N., 2007, J. Dermatol. Sci. 45:77. \n2. Brown, G.D., 2006, Nat. Rev. Immunol. 6:33. \n3. Hernanz-Falcon, P. et al., 2001, Immunogenetics 53:288. \n4. Yokota, K. et al., 2001, Gene 272:51. \n5. Willment, J.A. et al., 2001, J. Biol. Chem. 276:43818. \n6. Willment, J.A. et al., 2005, Eur. J. Immunol. 35:1539. \n7. Palma, A.S. et al., 2006, J. Biol. Chem. 281:5771. \n8. Gantner, B.N. et al., 2005, EMBO J. 24:1277. \n9. Gantner, B.N. et al., 2003, J. Exp. Med. 197:1107. \n10. Kennedy, A.D. et al., 2007, Eur. J. Immunol. 37:467. \n11. Brown, G.D. et al., 2003, J. Exp. Med. 197:1119. \n12. Yadav, M. and J.S. Schorey, 2006, Blood 108:3168. \n13. Suram, S. et al., 2006, J. Biol. Chem. 281:5506. \n14. Meyer-Wentrup, F. et al., 2007, J. Immunol. 178:154. \n15. Saijo, S. et al., 2007, Nat. Immunol. 8:39. \n16. Taylor, P.R. et al., 2007, Nat. Immunol. 8:31.