Human CLEC9a Antibody
Human CLEC9a Antibody Summary
Accession # Q6UXN8
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
CLEC9a (C-type lectin domain family 9 member A), also known as DNGR-1, is a type II transmembrane glycoprotein member of the C‑type lectin superfamily (1, 2). Mature human CLEC9a consists of a 35 amino acid (aa) cytoplasmic domain with an ITAM-like motif, a 21 aa transmembrane segment, and a 185 extracellular domain (ECD) that contains a stalk region and one C-type lectin domain (CTLD) (3‑5). Within the ECD, human CLEC9a shares 57% aa sequence identity with mouse and rat CLEC9a. Although the CTLD of CLEC9a structurally resembles that of other C-type lectins, it lacks the conserved residues that typically mediate calcium and carbohydrate binding. CLEC9a is expressed as a disulfide-linked homodimer of approximately 50 kDa N-glycosylated subunits (3, 5). Human CLEC9a expression is restricted to a subpopulation of BDCA-3+ conventional dendritic cells (cDC) and CD16- monocytes (3‑5). BDCA-3+ cDC are analagous to mouse CD8+ cDC which are specialized in antigenic cross-presentation in complex with MHC class I molecules (6). In mouse, CLEC9a is additionally expressed on plasmacytoid dendritic cells (4, 5). CLEC9a ligation enhances antigen uptake and processing, leading to presentation on MHC class I and cytotoxic T cell (CTL) priming (3‑5). In mouse, CLEC9a recognizes normally intracellular determinant(s) of necrotic cells and mediates their uptake by the dendritic cell (7). The subsequent antigenic cross-presentation to CTL is important for clearing necrotic cellular debris (7). CLEC9a signaling triggers activation of the tyrosine kinase Syk (3, 7).
- Huysamen, C. and G.D. Brown (2009) FEMS Microbiol. Lett. 290:121.
- Geijtenbeek, T.B.H. et al. (2004) Annu. Rev. Immunol. 22:33.
- Huysamen, C. et al. (2008) J. Biol. Chem. 283:16693.
- Caminschi, I. et al. (2008) Blood 112:3264.
- Sancho, D. et al. (2008) J. Clin. Invest. 118:2098.
- Dudziak, D. et al. (2007) Science 315:107.
- Sancho, D. et al. (2009) Nature 458:899.
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