CLEC12A Protein

C-type lectin domain family 12, member A

CLEC12A Products

CLEC12A Protein, Recombinant

Molecule	Species	Description	Cat. No
CLEC12A	Human	CLEC12A Protein, Recombinant	11896-H07H

CLEC12A cDNA Clone

Molecule	Species	Description	Cat. No
CLEC12A	Mouse	Mouse CLEC12A cDNA Clone / ORF Clone	MG50558-M

CLEC12A Related Areas

Immunology>>Adhesion Molecule>>Lectin>>CLEC12A

CLEC12A Alternative Names

CLEC12A, CLL-1, CLL1, DCAL-2, MGC70602, MICL [Homo sapiens]

Clec12a, CLL-1, D230024O04, KLRL1, Micl [Mus musculus]

CLEC12A Background

CLEC12A is a member of the C-type lectin/C-type lectin-like domain (CTL/CTLD) superfamily. Members of this family share a common protein fold and have diverse functions, such as cell adhesion, cell-cell signaling, glycoprotein turnover, and roles in inflammation and immune response. CLEC12A is a negative regulator of granulocyte and monocyte function. Several alternatively spliced transcript variants of this gene have been described, but the full-length nature of some of these variants has not been determined. C-type lectins are the most diverse and prevalent lectin family in immunity. Using a novel CLEC12A -specific monoclonal antibody, experiments had shown that human CLEC12A was expressed primarily on myeloid cells, including granulocytes, monocytes, macrophages, and dendritic cells. Although CLEC12A was highly N-glycosylated in primary cells, the level of glycosylation was found to vary between cell types. CLEC12A surface expression was down-regulated during inflammatory/activation conditions in vitro, as well as during an in vivo model of acute inflammation. This suggests that CLEC12A may be involved in the control of myeloid cell activation during inflammation.

CLEC12A Related Studies

1. Lahoud MH, et al. (2009) The C-type lectin Clec12A present on mouse and human dendritic cells can serve as a target for antigen delivery and enhancement of antibody responses. J Immunol. 182(12): 7587-94.
2. Pyz E, et al. (2008) Characterisation of murine MICL (CLEC12A) and evidence for an endogenous ligand. Eur J Immunol. 38(4): 1157-63.
3. Marshall AS, et al. (2006) Human MICL (CLEC12A) is differentially glycosylated and is down-regulated following cellular activation. Eur J Immunol. 36(8): 2159-69.