Description: Rabbit polyclonal Dectin 1 antibody

Description: Dectin1, also known as CLEC7A and the β-glucan receptor, is a 43 kDa type II transmembrane C-type lectin that functions in the innate immune response to fungal pathogens. Although Dectin1 resembles other CLEC molecules structurally, it binds ligands in a calciumindependent manner. Mature mouse Dectin1 is a 244 amino acid (aa) glycoprotein that consists of a short ITAMcontaining cytoplasmic tail, a transmembrane segment, and a stalk and carbohydrate recognition domain (CRD) in the extracellular domain. The CRD of mouse Dectin1 shares 61%, 60%, and 87% aa sequence identity with that of bovine, human, and rat Dectin1, respectively. It shares 25% 34% aa sequence identity with the CRD of other subgroup members CLEC1, CLEC2, CLEC9A, CLEC12B, LOX1, and MICL. Mouse Dectin1 is alternately spliced, generating a variant that lacks the stalk region. Mouse Dectin1 is expressed on monocytes, macrophages, and neutrophils, and on some populations of dendritic cells and T cells. It is upregulated on macrophages by GM-CSF, IL4, or IL13 and downregulated by dexamethasone, IL10, or LPS. The CRD selectively binds βglucan polymers, a major component of yeast and mycobacterial cell walls. Yeast βglucan is accessible to Dectin1 only at sites of cell budding, and Dectin1 does not recognize the filamentous form of yeast. Dectin1 mediates the phagocytosis of zymosan particles and intact yeast. It colocalizes with TLR2 in the presence of zymosan, and the two receptors cooperate in ligand recognition and the propagation of proinflammatory signaling. Dectin1 interaction with the tetraspanin CD37 increases its stability on the cell membrane and inhibits ligandinduced signaling. Genetic knockout of Dectin1 in mice increases their susceptibility to pathogenic infection.

Description: Dectin2α or Dectin2, also known as CLEC6A, CLECSF10, and NKCL, belongs to the Ctype lectin family of transmembrane immune regulatory glycoproteins. Dectin 2α, CLEC4A/DCIR, CLEC4B/DCAR, CLEC4C/DLEC, CLEC4D/MCL, and CLEC4E/mincle constitute a subgroup of these molecules that exhibit approximately 40% amino acid (aa) sequence identity in their extracellular domains (ECD) and have a conserved cysteine spacing in their carbohydrate recognition domains (CRD). Mature mouse Dectin2α consists of a short cytoplasmic tail, a transmembrane segment, and an ECD with a stalk region and one CRD. Alternate splicing leads to partial deletion of the transmembrane segment and stalk ( β isoform) or a portion of the CRD (γ isoform). The full length Dectin2α isoform is a 27 kDa molecule that is primarily expressed on the surface of tissue macrophages and their precursors. The CRD of Dectin2α contains an EPN motif which is characteristic of calciumdependent mannosebinding lectins. Dectin2α selectively interacts with high mannose structures in the Man9GlcNAc2 configuration. It mediates the recognition of a variety of microorganisms, particularly the filamentous forms of yeast and fungii. The short cytoplasmic tail does not contain signaling motifs but mediates association with the ITAMcontaining Fc receptor γ subunit in macrophages. Ligation of Dectin2α induces tyrosine phosphorylation of the γ subunit, activation of NFκB, and enhanced release of TNFα and IL1ra. Macrophage Dectin2α is upregulated in vivo by inflammatory stimuli and UVB irradiation. It mediates the breaking of UVinduced tolerance by interacting with CD4+CD25+ regulatory T cells which then induce dendritic cells to release IL4, IL10, and TGFβ. Within the ECD, mouse Dectin2α shares 71% aa sequence identity with human and bovine Dectin2.