Recombinant Mouse MDL-1/CLEC5A Protein, CF Summary
Details of Functionality |
Measured by its binding ability in a functional ELISA. When Recombinant Mouse Galectin-9 is immobilized at 0.5 μg/mL (100 μL/well), the concentration of Recombinant Mouse MDL-1/CLEC5A that produces 50% optimal binding response is approximately 0.1-0.5 μg/mL. |
Source |
Mouse myeloma cell line, NS0-derived mouse MDL-1/CLEC5A protein Tyr26-Lys190, with an N-terminal 9-His tag |
Accession # |
|
N-terminal Sequence |
His |
Protein/Peptide Type |
Recombinant Proteins |
Gene |
Clec5a |
Purity |
>90%, by SDS-PAGE with silver staining |
Endotoxin Note |
<0.10 EU per 1 μg of the protein by the LAL method. |
Applications/Dilutions
Dilutions |
|
Theoretical MW |
20 kDa. 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 |
34-45 kDa, reducing conditions |
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 |
>90%, by SDS-PAGE with silver staining |
Reconstitution Instructions |
Reconstitute at 100 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 Mouse MDL-1/CLEC5A Protein, CF
Background
MDL-1 (Myeloid DAP12-associating lectin 1), also known as CLEC5A, is an approximately 40 kDa member of the C-type lectin family (1). Mature mouse MDL-1 is a glycosylated type 2 transmembrane protein that associates into a homodimer on the cell surface (2). It consists of a 165 amino acid (aa) extracellular domain (ECD) with one C-type lectin (CTL) domain and a juxtamembrane stalk region, a 21 aa transmembrane segment, and a 4 aa cytoplasmic domain (3). Within the ECD, mouse MDL-1 shares 67% and 81% aa sequence identity with human and rat MDL-1, respectively. The transmembrane segment contains a lysine residue that mediates interactions with the signaling protein DAP12 (3). Alternative splicing generates a short isoform of mouse MDL-1 that lacks 25 aa of the stalk region (3, 4). MDL-1 is expressed on monocytes, macrophages, and neutrophils (3, 4). Its expression is up-regulated on monocytes in rheumatoid arthritis (5). MDL-1 functions as a cell attachment receptor for all four serotypes of dengue virus as well as Japanese encephalitis virus, although the short isoform binds significantly more weakly (2, 6, 7). These interactions trigger DAP12 phosphorylation, the production of multiple inflammatory cytokines, vascular leakage, and disruption of the blood-brain barrier (6-8). This recombinant protein corresponds to the long isoform of mouse MDL-1.
- Hoving, J.C. et al. (2014) Cell. Microbiol. 16:185.
- Watson, A.A. et al. (2011) J. Biol. Chem. 286:24208.
- Bakker, A.B.H. et al. (1999) Proc. Natl. Acad. Sci. USA 96:9792.
- Aoki, N. et al. (2009) J. Leukoc. Biol. 85:508.
- Chen, D.-Y. et al. (2014) PLoS ONE 9:e86105.
- Chen, S.-T. et al. (2012) PLoS Pathogens 8:e1002655.
- Chen, S.-T. et al. (2008) Nature 453:672.
- Wu, M.-F. et al. (2013) Blood 121:95.
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