>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
Endotoxin Note
<0.01 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Binding Activity
Theoretical MW
29.6 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
40-43 kDa, reducing conditions
Publications
Read Publications using 4888-CL in the following applications:
CLEC10A, also known as macrophage galactose/N-acetyl-galactosamine (GalNAc) specific lectin (MGL), CD301, DC-ASGPR, and HML, is a 40 kDa type II transmembrane glycoprotein that belongs to the C-type lectin family (1). Human and rat carry a single gene for CLEC10A/MGL, while mouse has two closely related MGL1 and MGL2 genes. Human CLEC10A/MGL consists of a 39 amino acid (aa) cytoplasmic region, a 21 aa transmembrane segment and a 256 aa extracellular domain (ECD) with one carbohydrate recognition domain (CRD) and a neck region (2). Within the CRD, human CLEC10A/MGL shares 64% - 70% aa sequence identity with mouse MGL1, mouse MGL2, and rat MGL. Alternate splicing generates multiple isoforms of human CLEC10A/MGL with 27 aa, 3 aa, and/or 4 aa deletions within the ECD (3, 4). CLEC10A/MGL is expressed on immature myleloid dendritic cells and alternatively activated (tolerogenic) macrophages and is upregulated by the immunosuppressant dexamethasone (3 - 7). CLEC10A/MGL selectively binds and internalizes terminal nonsialylated alpha - or beta -linked GalNAc moieties on O-linked carbohydrates, including the Tn carcinoma antigen (2 - 4, 8, 9). Similar ligand preference is exhibited by mouse MGL2 but not MGL1 (10). CLEC10A/MGL expressed on tolerogenic dendritic cells binds carbohydrate determinants on CD45 (RA, RB, and RC but not RO isoforms) expressed by T, NK, and B cells (6). This interaction inhibits effector T cell activation and induces their apoptosis (6). CLEC10A/MGL also binds the GP envelope glycoprotein on Marburg and Ebola viruses and enhances viral entry and infectivity (11).
Zelensky, A.N. and J.E. Gready (2005) FEBS J. 272:6179.
Suzuki, N. et al. (1996) J. Immunol. 156:128.
Higashi, N. et al. (2002) J. Biol. Chem. 277:20686.
Valladeau, J. et al. (2001) J. Immunol. 167:5767.
van Vliet, S.J. et al. (2006) Immunobiology 211:577.
van Vliet, S.J. et al. (2006) Nat. Immunol. 7:1200.
Raes, G. et al. (2005) J. Leukoc. Biol. 77:321.
van Vliet, S.J. et al. (2005) Int. Immunol. 17:661.
Higashi, N. et al. (2002) Int. Immunol. 14:545.
Tsuiji, M. et al. (2002) J. Biol. Chem. 277:28892.
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