Dectin-1, Recombinant, Mouse (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 43kD type II transmembrane C-type lectin that functions in the innate immune response to fungal pathogens. Although Dectin-1 resembles other CLEC molecules structurally, it binds ligands in a calcium-independent manner (1, 2). Mature mouse Dectin-1 is a 244 aa glycoprotein that consists of a short ITAM-containing cytoplasmic tail, a transmembrane segment, and a stalk and carbohydrate recognition domain (CRD) in the extracellular domain (3). The CRD of mouse Dectin-1 shares 61%, 60%, and 87% aa sequence identity with that of bovine, human, and rat Dectin-1, respectively. It shares 25%-34% aa sequence identity with the CRD of other subgroup members CLEC-1, CLEC-2, CLEC9A, CLEC12B, LOX-1, and MICL. Mouse Dectin-1 is alternately spliced, generating a variant that lacks the stalk region (4). Mouse Dectin-1 is expressed on monocytes, macrophages, and neutrophils, and on some populations of dendritic cells and T cells (5). It is upregulated on macrophages by GM-CSF, IL-4, or IL-13 and downregulated by dexamethasone, IL-10, or LPS (6). The CRD selectively binds b- glucan polymers, a major component of yeast and mycobacterial cell walls (7). Yeast b-glucan is accessible to Dectin-1 only at sites of cell budding, and Dectin-1 does not recognize the filamentous form of yeast (8). Dectin-1 mediates the phagocytosis of zymosan particles and intact yeast (8-10). It 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 interaction with the tetraspanin CD37 increases its stability on the cell membrane and inhibits ligand-induced signaling (14). Genetic knockout of Dectin-1 in mice increases their susceptibility to pathogenic infection (15, 16).\n\nSource: \nHuman CD33 signal peptide, (Met 1-Ala 16), HHHHHHHHHH, Mouse Dectin-1 (Phe 69-Leu 244). A DNA sequence encoding the extracellular domain of mouse Dectin-1 (Phe 69-Leu 244; Genbank Accession # NP_064392) 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: \nBased on N-terminal sequencing, the recombinant mouse Dectin-1, generated by the removal of the signal peptide, starts at the histidine tag and has a predicted molecular mass of 21.6 kD. As a result of glycosylation the recombinant mouse Dectin-1 migrates as an approximately 27-37kD protein in SDS-PAGE under reducing conditions.\n\nEndotoxin Level: \n< 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 < 6nM.\n\nReconstitution:\nIt is recommended that sterile PBS 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

D1876-48B

Size

50ug

Form

Supplied as a lyophilized powder in PBS.

Purity

(same/more than) 95%, 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. Ariizumi, K. et al., 2000, J. Biol. Chem. 275:20157. \n4. Heinsbroek, S.E.M. et al., 2006, J. Immunol. 176:5513. \n5. Taylor, P.R. et al., 2002, J. Immunol. 169:3876. \n6. Willment, J.A. et al., 2003, J. Immunol. 171:4569. \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.