Recombinant Human DCIR/CLEC4A Protein, CF
Recombinant Human DCIR/CLEC4A Protein, CF Summary
Gln70-Leu237, with an N-terminal 10-His tag
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
|Formulation||Lyophilized from a 0.2 μm filtered solution in PBS.|
|Reconstitution||Reconstitute at 250 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.
Recombinant Human DCIR/CLEC4A (Catalog # 9784-CI) supports the adhesion of SW480 human fibroblast carcinoma cells. The ED50 for this effect is 0.8-6.4 μg/mL.
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). Human DCIR consists of 237 amino acids (aa) with a 48 aa cytoplasmic domain, a 21 aa transmembrane region, and a 168 aa extracellular domain. Human DCIR shares approximately 56% amino acid identity with the mouser version and 55% 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).
- Huang, X. et al. (2001) Biochem. Biophys. Res. Commun. 281:131.
- Richard, M. et al. (2002) J. Leukoc. Biol. 71:871.
- Bates E.E. et al. (1999) J. Immunol. 163:1973.
- Nagae, M. et al. (2016) FEBS Lett. 590:1280.
- Bloem, K. et al. (2014) Immunol. Lett. 158:33.
- Kanazawa, N. et al. (2002) Dermatol. 118(2):261.
- Maruhashi, T. et al. (2015) J. Immunol. 194(12):5681.
- Lambert, A. et al. (2008) Blood 112(4):1299.
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