Recombinant Rat CLEC10A/CD301 Protein, CF

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Product Details

Summary
Reactivity RtSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

Order Details

Recombinant Rat CLEC10A/CD301 Protein, CF Summary

Details of Functionality
Measured by its binding ability in a functional ELISA. When Recombinant Rat CLEC10A/CD301 is immobilized at 2.5 µg/mL (100 µL/well), the concentration of biotinylated Recombinant Viral EBOV GP that produces 50% of the optimal binding response is approximately 1-6 μg/mL
Source
Chinese Hamster Ovary cell line, CHO-derived rat CLEC10A/CD301 protein
Gln59-Ser306, with an N-terminal 6-His tag
Accession #
N-terminal Sequence
His
Protein/Peptide Type
Recombinant Proteins
Purity
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Bioactivity
Theoretical MW
29 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
34-42 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 visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 500 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 Rat CLEC10A/CD301 Protein, CF

  • CD301 antigen
  • CD301
  • CD301C-type lectin domain family 10 member A
  • CLEC10A
  • CLECSF13
  • CLECSF14
  • CLECSF14macrophage C-type lectin
  • C-type (calcium dependent, carbohydrate-recognition domain) lectin, superfamilymember 14 (macrophage-derived)
  • C-type lectin domain family 10, member A
  • C-type lectin superfamily member 14
  • HML2
  • HMLC-type (calcium dependent, carbohydrate-recognition domain) lectin, superfamilymember 13 (macrophage-derived)
  • macrophage lectin 2 (calcium dependent)
  • Macrophage lectin 2
  • MGL

Background

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 in 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. Rat CLEC10A consists of a 37 amino acid (aa) cytoplasmic region, a 21 aa transmembrane segment, and a 248 aa extracellular domain (ECD) with one carbohydrate recognition domain and a neck region (2). Within the ECD, rat CLEC10A shares 56% and 79% aa sequence identity with human CLEC10A and mouse CLEC10A/MGL1, respectively. CLEC10A is expressed on immature myleloid dendritic cells, Langerhans cells, and alternatively activated (tolerogenic) macrophages and is upregulated by the immunosuppressant dexamethasone (3-8). It is up-regulated on pro-inflammatory monocytes in obesity and promotes their trafficking to adipose tissue (9). CLEC10A selectively binds and internalizes terminal nonsialylated alpha - or beta -linked GalNAc moieties on O-linked carbohydrates including the Tn carcinoma antigen (3, 4, 10-12). Similar ligand preference is exhibited by mouse MGL2 but not MGL1 (13). CLEC10A expressed on tolerogenic dendritic cells binds carbohydrate determinants on CD45 (RA, RB, and RC but not RO isoforms) on T, NK, and B cells (6). This interaction inhibits effector T cell activation and induces their apoptosis (6). CLEC10A also binds the GP envelope glycoprotein on Marburg and Ebola viruses and enhances viral entry and infectivity (14).
  1. Zelensky, A.N. and J.E. Gready (2005) FEBS J. 272:6179.
  2. Ii, M. et al. (1990) J. Biol. Chem. 265:11295.
  3. Higashi, N. et al. (2002) J. Biol. Chem. 277:20686.
  4. Valladeau, J. et al. (2001) J. Immunol. 167:5767.
  5. van Vliet, S.J. et al. (2006) Immunobiology 211:577.
  6. van Vliet, S.J. et al. (2006) Nat. Immunol. 7:1200.
  7. Raes, G. et al. (2005) J. Leukoc. Biol. 77:321.
  8. Dupasquier, M. et al. (2006) J. Leukoc. Biol. 80:838.
  9. Westcott, D.J. et al. (2009) J. Exp. Med. 206:3143.
  10. Suzuki, N. et al. (1996) J. Immunol. 156:128.
  11. van Vliet, S.J. et al. (2005) Int. Immunol. 17:661.
  12. Higashi, N. et al. (2002) Int. Immunol. 14:545.
  13. Tsuiji, M. et al. (2002) J. Biol. Chem. 277:28892.
  14. Takada, A. et al. (2004) J. Virol. 78:2943.

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