Recombinant Mouse CLEC4E Fc Chimera Protein, CF

WhenTrehalose 6, 6'-Dimycolate is immobilized at 1 µg/mL (100 µL/well), Recombinant Mouse CLEC4E Fc Chimera (Catalog# 9238-CL) binds with an ED50 of 8-48 ng/mL.

• Reactivity: Mu
• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Mouse CLEC4E Fc Chimera Protein, CF Summary

• Details of Functionality: Measured by its binding ability in a functional ELISA. When Trehalose 6, 6'-Dimycolate is immobilized at 1 µg/mL (100 µL/well), the concentration of Recombinant Mouse CLEC4E Fc Chimera that produces 50% of the optimal binding response is approximately 8-48 ng/mL.
• Source: Chinese Hamster Ovary cell line, CHO-derived mouse CLEC4E protein
  

  MDP	Mouse IgG2A (Glu98-Lys330)	IEGR	Mouse CLEC4E (Thr46-Asp214) Accession # Q9R0Q8
  N-terminus			C-terminus

• Accession #: Q9R0Q8
• N-terminal Sequence: Met
• Structure / Form: Disulfide-linked homodimer
• 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: 47 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: 54-63 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 Mouse CLEC4E Fc Chimera Protein, CF

• CLEC4E
• CLECSF9
• C-type (calcium dependent, carbohydrate-recognition domain) lectin, superfamilymember 9
• C-type lectin domain family 4 member E
• C-type lectin domain family 4, member E
• Macrophage-inducible C-type lectin
• MINCLE
• MINCLEC-type lectin superfamily member 9

Background

CLEC4E, also known as Mincle, is an approximately 30 kDa type 2 transmembrane C-type lectin that functions as an activating innate immune receptor (1). Mouse CLEC4E consists of a 19 amino acid (aa) cytoplasmic domain, a 21 aa transmembrane segment, and a 174 aa extracellular domain (ECD) that contains the C-type lectin domain (2). Within the ECD, mouse CLEC4E shares 65% and 87% aa sequence identity with human and rat CLEC4E, respectively. CLEC4E is expressed on monocytes, macrophages, and immature dendritic cells (2-5). It associates with CLEC4D/MCL and the gamma chain signaling subunits of Fc receptors (mediated by an Arg residue in the CLEC4E transmembrane segment) (3, 5, 6). Human CLEC4E binds to mycobacterial glycolipids including the immune adjuvant TDM (cord factor), its synthetic analog TDB, and GroMM (3, 4, 7-10). It also binds the nuclear protein SAP130 which can be released from necrotic cells (5) and cholesterol crystals deposited in atherosclerotic plaques (11). Mouse CLEC4E, in contrast, does not appear to interact with TDB, GroMM, or cholesterol crystals (7, 8, 11). CLEC4E ligation triggers phagocytosis and the production of inflammatory chemokines and cytokines (3-6, 8, 10). The fungus Fonsecaea monophora may evade immune clearance through binding to CLEC4E and suppressing IL-12 production and Th1 cell differentiation instead of promoting inflammation (9).

1. Richardson, M.B. and S.J. Williams (2014) Front. Immunol. 5:288.
2. Matsumoto, M. et al. (1999) J. Immunol. 163:5039.
3. Ishikawa, E. et al. (2009) J. Exp. Med. 206:2879.
4. Wells, C.A. et al. (2008) J. Immunol. 180:7404.
5. Yamasaki, S. et al. (2008) Nat. Immunol. 9:1179.
6. Lobato-Pascual, A. et al. (2013) Eur. J. Immunol. 43:3167.
7. Hattori, Y. et al. (2014) J. Biol. Chem. 289:15405.
8. Ostrop, J. et al. (2015) J. Immunol. 195:2417.
9. Wevers, B.A. et al. (2014) Cell Host Microbe 15:494.
10. Ishikawa, T. et al. (2013) Cell Host Microbe 13:477.
11. Kiyotake, R. et al. (2015) J. Biol. Chem. 290:25322.

Bioinformatics

• Uniprot:
  • Q9R0Q8()