| Reactivity | HuSpecies Glossary |
| Applications | WB |
| Clone | 512505 |
| Clonality | Monoclonal |
| Host | Mouse |
| Conjugate | Unconjugated |
| Concentration | LYOPH |
| Immunogen | NS0 mouse myeloma cell line transfected with human TLR3 Lys27-Ser711 Accession # Q6PCD4 |
| Specificity | Detects human TLR3 in Western blots. |
| Source | N/A |
| Isotype | IgG2b |
| Clonality | Monoclonal |
| Host | Mouse |
| Gene | TLR3 |
| Purity Statement | Protein A or G purified from hybridoma culture supernatant |
| Innovator's Reward | Test in a species/application not listed above to receive a full credit towards a future purchase. |
| Dilutions |
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| Publications |
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| Storage | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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| Buffer | Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied either lyophilized or as a 0.2 µm filtered solution in PBS. |
| Preservative | No Preservative |
| Concentration | LYOPH |
| Reconstitution Instructions | Reconstitute at 0.5 mg/mL in sterile PBS. |
Human TLR3 is a 116 kDa type I transmembrane glycoprotein that belongs to the mammalian Toll-Like Receptor family of pathogen pattern recognition molecules (1, 2). There are at least eleven mouse and ten human members that activate the innate immune system following exposure to a variety of microbial species (3). The human TLR3 cDNA encodes a 904 amino acid (aa) precursor that contains a 23 aa signal sequence, a 681 aa extracellular domain (ECD), a 21 aa transmembrane segment, and a 179 aa cytoplasmic region (4). The horseshoe shaped ECD (5, 6) contains 23 leucine rich repeats, and the cytoplasmic domain contains one Toll/IL-1 receptor (TIR) domain. The ECD of human TLR3 shares 80%, 79%, and 77% aa sequence identity with the ECD of rat, mouse, and bovine TLR3, respectively. TLR3 is found in phagosomes (7), where the acidic pH enables binding of internalized double stranded RNA and mRNA from viruses, parasites, and necrotic virally-infected cells (8‑11). Ligand binding by TLR3 induces receptor dimerization (5, 6, 8) leading to the release of inflammatory cytokines and dendritic cell maturation (9, 11‑13). TLR3 is expressed in dendritic cells, macrophages, microglia, and astrocytes (13‑15) and is upregulated by IFN-beta and LPS (9, 14). TLR3 expression is also induced by lung fibroblasts and epithelial cells by respiratory syncytial virus infection (12).
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Secondary Antibodies |
Isotype Controls |
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Read full blog post. |
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The role of STING/TMEM173 in gamma and encephalitis Herpes Simplex Virus (HSV) Stimulator of interferon genes (STING), also known as TMEM173, promotes the production of the interferon’s IFN-alpha and IFN-beta. STING possesses three functional domains: a cytoplasmic C-terminal tail, a central globular domain, and four N-... Read full blog post. |
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TRIF/TICAM1 and mitochondrial dynamics in the innate immune response TRIF, also known as toll like receptor adaptor molecule 1 or TICAM1, is known for its role in invading foreign pathogens as part of our innate immune response. TRIF/TICAM1 is a TIR-domain adaptor protein (toll/interleukin-1 receptor) that interacts... Read full blog post. |
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The role of TLR4 in breast cancer Toll like receptors (TLRs) are highly conserved proteins that are first known for their role in pathogen recognition and immune response activation. In order to elicit the necessary immune response in reaction to a foreign pathogen, TLRs trigger cy... Read full blog post. |
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![Knocking-down TLR3 suppresses enhancement of c-IAP2 protein expression by poly(I:C). Western blot analysis of protein extracts from HeLa cells treated with poly(I:C) (500 ng/ml for 16 h) with or without pre-treatment with TLR3-specific and control (NS) siRNAs. The same membrane was stained successively with anti-c-IAP2, TLR3 and beta -actin. Note that the control siRNA by itself enhanced TLR3 and c-IAP2 expression. This is consistent with previous observations and possibly related to the interaction of these small double-strand RNAs with the TLR3 itself regardless of their sequence [36]. In our transfection protocol siRNAs are at 100 nM for the first 4 h and 50 nM for the next 44 h. TLR3 inhibition was not complete with the siRNA n°1 which was apparently weaker than the siRNA n°2. However the siRNA n°1 was strong enough to prevent enhancement of TLR3 and c-IAP2 expression in the absence of poly(I:C). Data are representative of two similar experiments. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/20576118), licensed under a CC-BY license. Not internally tested by R&D Systems.](http://images.novusbio.com/fullsize/mab1487_human-tlr3-mab-clone-512505-4120241251268.jpg "Knocking-down TLR3 suppresses enhancement of c-IAP2 protein expression by poly(I:C). Western blot analysis of protein extracts from HeLa cells treated with poly(I:C) (500 ng/ml for 16 h) with or without pre-treatment with TLR3-specific and control (NS) siRNAs. The same membrane was stained successively with anti-c-IAP2, TLR3 and beta -actin. Note that the control siRNA by itself enhanced TLR3 and c-IAP2 expression. This is consistent with previous observations and possibly related to the interaction of these small double-strand RNAs with the TLR3 itself regardless of their sequence [36]. In our transfection protocol siRNAs are at 100 nM for the first 4 h and 50 nM for the next 44 h. TLR3 inhibition was not complete with the siRNA n°1 which was apparently weaker than the siRNA n°2. However the siRNA n°1 was strong enough to prevent enhancement of TLR3 and c-IAP2 expression in the absence of poly(I:C). Data are representative of two similar experiments. Image collected and cropped by CiteAb from the following publication (//pubmed.ncbi.nlm.nih.gov/20576118), licensed under a CC-BY license. Not internally tested by R&D Systems.")
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