Product Specifications for Recombinant Mouse TLR1 Protein, CF
Mouse myeloma cell line, NS0-derived mouse TLR1 protein Ser25-Asp581, with a C-terminal 10-His tag
>95%, by SDS-PAGE under reducing conditions and visualized by silver stain
<0.10 EU per 1 μg of the protein by the LAL method.
N-terminal sequence Analysis
Predicted Molecular Mass
Measured by its ability to bind biotinylated Pam3CysSerLys4 (Pam3CSK4).
Formulation, Preparation and Storage
What does CF mean?
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our
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.
What formulation is right for me?
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
Lyophilized from a 0.2 μm filtered solution in PBS.
Reconstitute at 100 μg/mL in sterile PBS.
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.
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.
The Toll-like family of molecules are type I transmembrane proteins that serve as pattern recognition receptors for microbial pathogens. There are at least twelve mouse and ten human TLRs that activate the innate immune system following exposure to a variety of microbial species (1, 2). TLRs contain a large number of leucine-rich repeats (LRRs) and a cytoplasmic tail with one Toll/IL-1 receptor (TIR) domain. Mature mouse TLR1 consists of a 557 amino acid (aa) extracellular domain (ECD) with 20 LRRs, a 21 aa transmembrane segment, and a 192 aa cytoplasmic domain (3, 4). Within the ECD, mouse TLR1 shares 60% aa sequence identity with mouse TLR6 and 19% -27% aa sequence identitity with mouse TLR2, -3, -4, -5, -7, -8, -9, -11, -12, and -13. It shares 73% and 86% aa sequence identity with human and rat TLR1, respectively. TLR1 is expressed on the surface of macrophages, dendritic cells, and tonsillar epithelial cells in ligand-independent association with TLR2 (5 - 8). TLR2 additionally associates with TLR6 to form a functional complex with specificity for distinct but related microbial ligands (9 - 11). TLR1 and TLR2 cooperate in the recognition of bacterial and protozoal triacylated lipopeptides and glycosylphosphatidylinositols (6, 10 - 12). Ligand binding induces TLR1 localization to lipid rafts followed by receptor internalization and activation of NF kappa B (7, 11, 13).
Miyake, K. (2007) Semin. Immunol. 19:3.
Hopkins, P.A. and S. Sriskandan (2005) Clin. Exp. Immunol. 140:395.
SwissProt # Q9EPQ1.
Matsushima, N. et al. (2007) BMC Genomics 8:124.
Ochoa, M.-T. et al. (2003) Immunology 108:10.
Takeuchi, O. et al. (2002) J. Immunol. 169:10.
Triantafilou, M. et al. (2006) J. Biol. Chem. 281:31002.
Sandor, F. et al. (2003) J. Cell Biol. 162:1099.
Nakao, Y. et al. (2005) J. Immunol. 174:1566.
Ozinsky, A. et al. (2000) Proc. Natl. Acad. Sci. 97:13766.
Lee, J.Y. et al. (2004) J. Biol. Chem. 279:16971.
Krishnegowda, G. et al. (2005) J. Biol. Chem. 280:8606.
Nishiya, T. and A.L. DeFranco (2004) J. Biol. Chem. 279:19008.