Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Level
<0.10 EU per 1 μg of the protein by the LAL method.
Activity
Measured by its binding ability in a functional ELISA. When Recombinant Mouse Podoplanin Fc Chimera (Catalog # ) is coated at 0.5 µg/mL (100 μL/well), Recombinant Mouse
CLEC-2/CLEC1B binds with a typical ED 50 of
0.1-0.5 μg/mL.Source
Mouse myeloma cell line, NS0-derived Met53-Leu229, with an N-terminal 6-His tag
Accession #
N-terminal Sequence
AnalysisHis
Predicted Molecular Mass
21 kDa
SDS-PAGE
24-39 kDa, reducing conditions
9117-CL |
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Formulation Lyophilized from a 0.2 μm filtered solution in PBS. | ||
Reconstitution Reconstitute at 100 μg/mL in PBS. | ||
Shipping The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. | ||
Stability & Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Data Images
Bioactivity
| When Recombinant Mouse Podoplanin Fc Chimera (Catalog # ) is coated at 0.5 µg/mL, Recombinant Mouse CLEC-2/ CLEC1B (Catalog # 9117-CL) binds with a typical ED50 of 0.1-0.5 μg/mL. |
Background: CLEC-2/CLEC1B
C-type lectin-like receptor 2, also known as CLEC-1B, is a 32 kDa type II transmembrane glycoprotein that is expressed on platelets, megakaryocyte, and liver sinusoidal cells (1-4). Mature mouse CLEC-2 consists of a 31 amino acid (aa) cytoplasmic domain, a 21 aa transmembrane segment, and a 177 aa extracellular domain (ECD) with one C-type lectin domain. Within the ECD, mouse CLEC-2 shares 59% and 90% aa sequence identity with human and rat CLEC-2, respectively. Alternative splicing generates a short isoform that lacks the transmembrane segment. CLEC-2 binding to Podoplanin trigger platelet activation, shedding of GPVI, and cleavage of Fcg RIIA/CD32a (5-8). CLEC-2 expression on platelets is required for the development of lymphatic vessels and valves as well as the maintenance of lymph node high endothelial veinules (HEV) during lymphocyte crossing (7-10). CLEC-2 additionally binds to fucoidan, HIV-1, and the platelet-aggregating snake venom protein Rhodocytin/Aggretin (2, 3, 11). In the liver, soluble CLEC-2 promotes M2 macrophage differentiation and limits inflammatory cytokine production (12).
References:
Lee, R.H. and W. Bergmeier (2016) J. Thromb. Haemost. Epub PMID 26749528.
Suzuki-Inoue, K. et al. (2006) Blood 107:542.
Chaipan, C. et al. (2006) J. Virol. 80:8951.
Gitz, E. et al. (2014) Blood 124:2262.
Suzuki-Inoue, K. et al. (2007) J. Biol. Chem. 282:25993.
Christou, C.M. et al. (2008) Biochem. J. 411:133.
Herzog, B.H. et al. (2013) Nature 502:105.
Sweet, D.T. et al. (2015) J. Clin. Invest. 125:2995.
Hess, P.R. et al. (2014) J. Clin. Invest. 124:273.
Osada, M. et al. (2012) J. Biol. Chem. 287:22241.
Manne, B.K. et al. (2013) J. Biol. Chem. 288:7717.
Wu, X. et al. (2015) EbioMedicine 2:214.
Long Name:
C-type Lectin-like Receptor 2
Entrez Gene IDs:
51266 (Human); 56760 (Mouse)
Alternate Names:
1810061I13Rik; CLEC1B; CLEC2; CLEC-2; CLEC2B; CLEC2PRO1384; C-type lectin domain family 1 member B; C-type lectin domain family 1, member B; C-type lectin-like receptor 2; C-type lectin-like receptor-2; QDED721
