Recombinant Human CLEC9a Fc Chimera Protein, CF Summary
Details of Functionality |
Measured by flow cytometry for its ability to bind a ligand expressed in FasL-treated mouse B cells. Sancho, D. et al. (2009) Nature 458:899. At 100 ng/mL, >50% of necrotic cells bind to Recombinant Human CLEC9a. |
Source |
Mouse myeloma cell line, NS0-derived human CLEC9a protein
Met-Asp
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Human IgG1 (Pro100-Lys330)
|
IEGR |
Human CLEC9a (Lys57-Val241) Accession # Q6UXN8 |
N-terminus |
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C-terminus |
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Accession # |
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N-terminal Sequence |
Met |
Structure / Form |
Disulfide-linked homodimer |
Protein/Peptide Type |
Recombinant Proteins |
Gene |
CLEC9A |
Purity |
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain. |
Endotoxin Note |
<0.10 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
Dilutions |
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Theoretical MW |
47.8 kDa (monomer). Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
SDS-PAGE |
55-65 kDa, reducing conditions |
Reviewed Applications |
Read 1 Review rated 5 using 6049-CL in the following application:
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Publications |
Read Publications using 6049-CL in the following applications:
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Packaging, Storage & Formulations
Storage |
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 3 months, -20 to -70 °C under sterile conditions after reconstitution.
|
Buffer |
Lyophilized from a 0.2 μm filtered solution in PBS. |
Purity |
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain. |
Reconstitution Instructions |
Reconstitute at 200 μg/mL in PBS. |
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human CLEC9a Fc Chimera Protein, CF
Background
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). Mature mouse 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) (2-4). 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 (2, 4). Human CLEC9A expression is restricted to a subpopulation of BDCA-3
+ conventional dendritic cells (cDC) and CD16
- monocytes (2-5). 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 (3, 4). CLEC9A ligation enhances antigen uptake and processing, leading to presentation on MHC class I and cytotoxic T cell (CTL) priming (2-5, 7). Its recognition of filamentous actin in dead cells is important for triggering an immune response to necrotic cell debris (8-10). CLEC9A is also required for the presentation of viral proteins and the subsequent CTL-mediated killing of virus-infected cells (11, 12). CLEC9A signaling triggers activation of the tyrosine kinase Syk (2, 8).
- Kerrigan, A.M. and G.D. Brown (2010) Immunol. Rev. 234:335.
- 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.
- Schreibelt, G. et al. (2012) Blood 119:2284.
- Dudziak, D. et al. (2007) Science 315:107.
- Poulin, L.F. et al. (2010) J. Exp. Med. 207:1261.
- Sancho, D. et al. (2009) Nature 458:899.
- Ahrens, S. et al. (2012) Immunity 36:635.
- Zhang, J.-G. et al. (2012) Immunity 36:646.
- Iborra, S. et al. (2012) J. Clin. Invest. 122:1628.
- Zelenay, S. et al. (2012) J. Clin. Invest. 122:1615.
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