Anti-hTLR2 Detection and Neutralizing mAb
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Anti-human TLR2 mAb (clone B4H2)
Human TLR2 Detection and Neutralizing Antibody (clone B4H2) - Monoclonal Human IgA2
Anti-hTLR2-IgA (clone B4H2) is a recombinant monoclonal antibody specific for human Toll-like receptor 2 (TLR2, CD282). It was generated by combining the constant domains of the human IgA molecule with murine variable regions. This antibody has been produced in Chinese hamster ovary (CHO) cells and purified by affinity chromatography.
Anti-hTLR2-IgA has been selected for its ability to efficiently neutralize the biological activity of TLR2. The neutralizing activity was determined using HEK-Blue™ hTLR2 cells. This antibody can also be used to detect hTLR2 using flow cytometry. TLR2 plays an essential role in detecting a diverse range of microbial pathogen-associated molecular patterns (PAMPs) . An essential feature of TLR2 is its ability to form heterodimers with TLR1 and TLR6. TLR2 cooperates with TLR6 in response to diacylated mycoplasmal lipoproteins , and associates with TLR1 to recognize triacylated lipoproteins [3,4].
- Reacts with human TLR2
- Provided azide-free
- Each lot is functionally tested
Read our review on TLR2
1. Oliveira-Nascimento L. et al., 2012. The Role of TLR2 in Infection and Immunity. Front Immunol 3:79.
2. Girard R. et al., 2003. Lipopolysaccharides from Legionella and Rhizobium stimulate mouse bone marrow granulocytes via Toll-like receptor 2. J Cell Sci. 116:293-302.
3. Ozinsky A. et al., 2000. The repertoire for pattern recognition of pathogens by the innate immune system is defined by cooperation between toll-like receptors. PNAS USA. 97:13766-71.
4. Thakran S. et al., 2008. Identification of Francisella tularensis lipoproteins that stimulate the Toll-like receptor (TLR) 2/TLR1 heterodimer. J Biol Chem 283:3751-9.
Target: Human TLR2 (hTLR2)
Specificity: No cross-reactivity with murine TLR2
Clonality: Monoclonal antibody
Isotype: Human IgA2, kappa
Control: Human IgA2 Control
Source: CHO cells
Formulation: 0.2 μm filtered solution in Tris HCl buffer with saccharose, glycine, and stabilizing agents
Application: Neutralization/block; Flow cytometry
- This product has been validated for neutralization using cellular assays.
- Binding of Anti-hTLR2-IgA to hTLR2 on cells has been validated using flow cytometry.
- The absence of bacterial contamination (e.g. lipoproteins and endotoxins) has been confirmed using HEK-Blue™ TLR2 and HEK‑Blue™ TLR4 cells.
- 100 μg purified Anti-hTLR2-IgA antibody, provided azide-free and lyophilized
Product is shipped at room temperature.
Upon receipt, store lyophilized antibody at -20 °C.
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Toll-Like receptors (TLRs) play a critical role in early innate immunity to invading pathogens by sensing microorganisms. These evolutionarily conserved receptors recognize highly conserved structural motifs only expressed by microbial pathogens, called pathogen-associated microbial patterns (PAMPs). Stimulation of TLRs by PAMPs initiates a signaling cascade leading to the secretion of proinflammatory cytokines following NF-κB activation. To date ten human and twelve murine TLRs have been characterized, TLR1 to TLR10 in humans, and TLR1 to TLR9, TLR11, TLR12, and TLR13 in mice, the homolog of TLR10 being a pseudogene.
TLR2 is involved in the recognition of a wide array of microbial molecules. TLR2 recognizes lipoteichoic acid and lipoprotein from Gram-positive bacteria, lipoarabinomannan from mycobacteria, and zymosan from yeast cell wall. Moreover, TLR2 participates in the recognition of some types of LPS. TLR2 is known to heterodimerize with other TLRs, a property believed to extend the range of microbial molecules that TLR2 can recognize. TLR2 cooperates with TLR6 in response to diacylated mycoplasmal lipopeptides , and associates with TLR1 to recognize triacylated lipopeptides . Furthermore, pathogen recognition by TLR2 is strongly enhanced by CD14 .
1. Girard R et al., 2003. Lipopolysaccharides from Legionella and Rhizobium stimulate mouse bone marrow granulocytes via Toll-like receptor 2. J Cell Sci. 116(Pt 2):293-302.
2. Ozinsky A. et al., 2000. The repertoire for pattern recognition of pathogens by the innate immune system is defined by cooperation between toll-like receptors. PNAS. 97(25):13766-71.
3. Lotz S. et al., 2004. Highly purified lipoteichoic acid activates neutrophil granulocytes and delays their spontaneous apoptosis via CD14 and TLR2. J Leukoc Biol. 75(3):467-77.