Recombinant Mouse DCIR/CLEC4A Protein, CF

Recombinant Mouse DCIR/CLEC4A (Catalog # 9785-CI) supports the adhesion ofJurkat human acute T cell leukemia cells. The ED50 for this effect is typically0.6‑3.6 μg/mL.

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

Recombinant Mouse DCIR/CLEC4A Protein, CF Summary

• Details of Functionality: Measured by its ability of the immobilized protein to support the adhesion of Jurkat human acute T cell leukemia cells. The ED₅₀ for this effect is 0.6-3.6 μg/mL.
• Source: Mouse myeloma cell line, NS0-derived mouse DCIR/CLEC4A protein
  Gln70-Leu238, with an N-terminal 9-His tag
• Accession #: Q9QZ15
• N-terminal Sequence: His
• Protein/Peptide Type: Recombinant Proteins
• Purity: >95%, 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: 21 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: 20-40 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 with Trehalose.
• Purity: >95%, 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 DCIR/CLEC4A Protein, CF

• CD367
• CLEC4A
• CLECSF6
• CLECSF6C-type lectin superfamily member 6
• C-type (calcium dependent, carbohydrate-recognition domain) lectin, superfamilymember 6
• C-type lectin domain family 4 member A
• C-type lectin domain family 4, member A
• DCIR
• DCIRLLIR
• DDB27
• DDB27C-type lectin DDB27
• Dendritic cell immunoreceptor
• Lectin-like immunoreceptor
• LLIR

Background

DCIR (Dendritic Cell Immunoreceptor), also known as Lectin-like Immunoreceptor (LLIR), is a type II membrane protein belonging to the C-type lectin domain family and is designated CLEC4A (previously designated CLECSF6). Four transcript variants encoding distinct isoforms have been identified (1, 2). DCIR contains one carbohydrate recognition domain in its C-terminal extracellular domain and an immunoreceptor tyrosine-based inhibitory motif (ITIM) in its cytoplasmic domain (3). Crystal structure identifies the nonterminal disaccharide GlcNAc beta 1-2Man as its primary binding epitope (4). Mouse DCIR consists of 238 amino acids (aa) with a 48 aa cytoplasmic domain, a 21 aa transmembrane region, and a 169 aa extracellular domain. Mouse DCIR shares approximately 56% amino acid identity with the human version and 69% amino acid identity with the rat version of the protein. Besides dendritic cell, DCIR is expressed on B cells, monocytes/macrophages and granulocytes. It acts as a mannose/fucose lectin and interacts with targets of both endogenous and pathogenic origin (5), binding sugars with broad specificity in a calcium-dependent manner (4). DCIR is critically important for the homeostasis of the immune system. DCIR can inhibit B cell receptor mediated calcium mobilization and protein tyrosine phosphorylation through its intracellular ITIM Motif (6-7). It can interact directly with the HIV-1 virus thus modulate HIV-1 transmission (8). Recent study has demonstrated that DCIR-specific ligands are present on various cancer cell lines and keratinocytes (5).

1. Huang, X. et al. (2001) Biochem. Biophys. Res. Commun. 281:131.
2. Richard, M. et al. (2002) J. Leukoc. Biol. 71:871.
3. Bates, E.E.M. et al. (1999) J. Immunol. 163:1973.
4. Nagae, M. et al. (2016) FEBS Lett. 590:1280.
5. Bloem, K. et al. (2014) Immunol. Lett. 158:33.
6. Kanazawa, N. et al. (2002) Dermatol. 118 (2):261.
7. Maruhashi, T. et al. (2015) J. Immunol. 194(12):5681.
8. Lambert, A. et al. (2008) Blood 112(4):1299.

Bioinformatics

• Uniprot:
  • Q9QZ15()