Recombinant Mouse TLR11 Fc Chimera Protein, CF Summary
Product Specifications
Mouse TLR11 (Trp31-Glu721) Accession # Q6R5P0 |
IEGRMDP | Mouse IgG2A (Glu98-Lys330) |
N-terminus | C-terminus | |
Analysis
Product Datasheets
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.
7640-TR
Formulation | Lyophilized from a 0.2 μm filtered solution in PBS. |
Reconstitution | Reconstitute at 100 μg/mL in PBS. |
Shipping | The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below. |
Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Reconstitution Calculator
Background: TLR11
TLR11 is a type I transmembrane receptor of the Toll‑like receptor family that is primarily expressed in epithelial cells in the liver, kidney, bladder and intestines, as well as in dendritic cells and macrophages (1‑3). The 926 amino acid (aa) mouse TLR11 transcript encodes a 30 aa signal sequence, a 691 aa extracellular domain (ECD) with 10 leucine-rich repeats and 9 potential N‑glycosylation sites, a 21 aa transmembrane domain, and a 184 aa cytoplasmic domain with a TIR domain (1). Within the ECD, mouse and rat TLR11 share 86% aa sequence identity. Human TLR11 is a pseudogene that is not expressed. Some researchers have found TLR11 in the dendritic cell plasma membrane, where it cooperates with MyD88 to take up antigen and initiate cell signaling (3‑5). Others have found it in the endoplasmic reticulum (ER), where it interacts with the multispan ER protein UNC93B1 (6). TLR11 recognizes profilin proteins on Toxoplasma gondii and other intracellular parasites (3, 7). Binding of profiln activates dendritic cell subsets to expand, mature, produce IL‑12, and present antigenic profilin peptides to T cells (2‑4). TLR11 is also reported to recognize pathogenic bacteria in the urinary tract (1). In the intestines, it is expressed on M cells, where its recognition of pathogenic salmonella blocks their entry into Peyer’s patches (8). TLR11 allows mice to be resistant to Salmonella typhi, the organism causing typhoid fever, while humans are sensitive (9).
- Zhang, D. et al. (2004) Science 303:1522.
- Pepper, M. et al. (2008) J. Immunol. 180:6229.
- Yarovinsky, F. et al. (2005) Science 308:1626.
- Yarovinsky, F. et al. (2006) Immunity 25:655.
- Liu, B. et al. (2010) Nat. Commun. 1:79.
- Pifer, R. et al. (2011) J. Biol. Chem. 286:3307.
- Kucera, K. et al. (2010) J. Mol. Biol. 403:616.
- Shi, Z. et al. (2012) J. Biol. Chem. 287:43417.
- Mathur, R. et al. (2012) Cell 151:590.
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