Purity
>85%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining
Endotoxin Level
<1.0 EU per 1 μg of the protein by the LAL method.
Activity
Measured by its ability to bind biotinylated Pam3CysSerLys4 (PAM3CSK4) (2 μg/mL). The 50% maximum binding is achieved at 0.1‑0.5 μg/mL of Recombinant Human TLR2.
Results can vary with different preparations of biotinylated PAM3CSK4.
Optimal dilutions should be determined by each laboratory for each application.Source
Mouse myeloma cell line, NS0-derived Glu21-Leu590, with a C-terminal 10-His tag
Accession #
N-terminal Sequence
AnalysisGlu21
Predicted Molecular Mass
65.7 kDa
SDS-PAGE
75-80 kDa, reducing conditions
2616-TR |
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Formulation Lyophilized from a 0.2 μm filtered solution in PBS. | ||
Reconstitution Reconstitute at 200 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: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Background: TLR2
Human toll-like receptor (TLR) family includes ten members that activate the innate immune response via an ability to recognize molecular structures found in a variety of microbial pathogens (1-3). All TLR family members are type I transmembrane proteins with a large number of extracellular leucine-rich repeats (LRRs) and a cytoplasmic Toll/IL-1 receptor (TIR) domain. Human TLR2 is synthesized as a 784 amino acid precursor (2) that contains a signal sequence (aa 1-18), an extracellular domain (aa 19‑588) with approximately 20 LRRs, a transmembrane segment (aa 589-609), and a cytoplasmic TIR domain (aa 610-784). The receptor is expressed on a number of cell types including monocytes, dendritic cells, neutrophils, B cells endothelial cells, and hepatocytes (1, 2, 4). TLR2 functions as part of a heterodimeric complex with either TLR1 or TLR6, and possibly other co-receptors (1). These complexes recognize lipoproteins and glycolipids from gram-positive and gram-negative bacteria as well as mycoplasma and yeast. TLR2/TLR1 heterodimers bind triacylated lipopeptides, while the TLR2/TLR6 heterodimer preferentially recognizes diacylated lipopeptides (5). Upon ligand recognition, TLR2 delivers an activating signal via the associated adapter molecules, MyD88 and TIRAP (1, 6). TLR2 signaling results in dendritic cell maturation characterized by increased surface expression of class II MHC and the T cell co-stimulators, CD80 and CD86 (1, 2). Activation via TLR2 also results in production of a number of pro‑inflammatory cytokines including TNF-alpha, IL-2, IL-6, IL-12, and MIP-2 (1-3).
References:
Wetzler, L. (2003) Vaccine 21:S2/55.
Kirschning, C. and R. Schumann (2002) Curr. Top. microbiol. Immunol. 270:121.
Netea, M. et al. (2004) J. Leukoc. Biol. 75:749.
Flo T. et al. (2001) J. Leukoc. Biol. 69:474.
Akira S. (2003) Curr. Opin. Immunol. 15:5.
Yamamoto M. et al. (2002) Nature 420:324.
Long Name:
Toll-like Receptor 2
Entrez Gene IDs:
7097 (Human); 24088 (Mouse); 310553 (Rat)
Alternate Names:
CD282 antigen; CD282; TIL4CD282; TLR2; toll/interleukin 1 receptor-like 4; Toll/interleukin-1 receptor-like protein 4; toll-like receptor 2
