Recombinant Human CLEC-1 Protein, CF Summary
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Carrier Free
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.
1704-CL
| Formulation | Lyophilized from a 0.2 μm filtered solution in PBS. |
| Reconstitution | Reconstitute at 250 μg/mL in sterile PBS. |
| Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. |
| Stability & Storage: | Store the unopened product at -20 to -70 °C. Use a manual defrost freezer and avoid repeated freeze-thaw cycles. Do not use past expiration date. |
Reconstitution Calculator
Background: CLEC-1
CLEC-1 (C-type lectin-like receptor-1) is a type 2 transmembrane protein that belongs to the Dectin-1 family of C-type lectins (1, 2). It consists of a 52 amino acid (aa) cytoplasmic domain, a 21 aa transmembrane segment, and a 207 aa extracellular domain (ECD) (3). The ECD contains a carbohydrate recognition domain (CRD) that includes cysteine residues with conserved spacing (4). In other C-type lectins, these cysteines form intrachain disulfide bonds that stabilize the CRD protein fold (4). CLEC-1 is a nonclassical C-type lectin in that its CRD lacks consensus amino acids which mediate calcium dependent carbohydrate binding in other C-type lectins (2, 3). The cytoplasmic domain contains one tyrosine, multiple serine and threonine, and a cluster of aspartic acid residues. The CLEC-1, CLEC-2, Dectin-1, and LOX-1 genes are located within the NK gene complex that also encodes several receptors involved in regulating NK cell activation (3, 5). CLEC-1 is most highly expressed in activated dendritic cells and at lower levels in endothelial cells and monocytes (3, 5). Within the CRD, human CLEC-1 shares 65% aa sequence identity with mouse and rat CLEC-1 and 26% - 36% with the other human Dectin-1 family lectins CLEC-2, CLEC9A, CLEC12B, Dectin-1, LOX-1, and MICL.
- Kanazawa, N. (2007) J. Dermatol. Sci. 45:77.
- Pyz, E. et al. (2006) Ann. Med. 38:242.
- Colonna, M. et al. (2000) Eur. J. Immunol. 30:697.
- Zelensky, A.N. and J.E. Gready (2005) FEBS J. 272:6179.
- Sobanov, Y. et al. (2001) Eur. J. Immunol. 31:3493.
Citations for Recombinant Human CLEC-1 Protein, CF
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
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CLEC-1 is a death sensor that limits antigen cross-presentation by dendritic cells and represents a target for cancer immunotherapy
Authors: M Drouin, J Saenz, V Gauttier, B Evrard, G Teppaz, S Pengam, C Mary, A Desselle, V Thepenier, E Wilhelm, E Merieau, C Ligeron, I Girault, MD Lopez, C Fourgeux, D Sinha, I Baccelli, A Moreau, C Louvet, R Josien, J Poschmann, N Poirier, E Chiffoleau
Science Advances, 2022-11-18;8(46):eabo7621.
Species: Human, Mouse
Sample Types: In Vivo, Protein
Applications: ELISA Capture, ELISA Detection, Immunoprecipitation, In Vivo -
Cell-surface C-type lectin-like receptor CLEC-1 dampens dendritic cell activation and downstream Th17 responses
Authors: MD Lopez Robl, A Pallier, V Huchet, L Le Texier, S Remy, C Braudeau, L Delbos, A Moreau, C Louvet, C Brosseau, PJ Royer, A Magnan, F Halary, R Josien, MC Cuturi, I Anegon, E Chiffoleau
Blood Adv, 2017-03-22;1(9):557-568.
Species: Human
Sample Types:
Applications: ELISA (Standard)
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Average Rating: 4 (Based on 1 Review)
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Reason for Rating: Our request for a custom bottling (large amount) was fulfilled very quickly. When we had questions about the quality of the protein, R&D was quick to share their own internal QC and explain their findings.
