Reactivity | HuSpecies Glossary |
Applications | Bioactivity |
Format | Carrier-Free |
Details of Functionality | Measured by its ability to bind biotinylated Pam3CysSerLys4 (PAM3CSK4). |
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Source | Mouse myeloma cell line, NS0-derived human TLR1 protein
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Accession # | |||||||
N-terminal Sequence | Ser22 |
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Structure / Form | Disulfide linked homodimer |
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Protein/Peptide Type | Recombinant Proteins |
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Gene | TLR1 |
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Purity | >90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
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Endotoxin Note | <0.10 EU per 1 μg of the protein by the LAL method. |
Dilutions |
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Theoretical MW | 89.9 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors. |
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SDS-PAGE | 95-105 kDa, reducing conditions |
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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. |
Purity | >90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining. |
Reconstitution Instructions | Reconstitute at 100 μg/mL in PBS. |
The Toll-like family of molecules are type I transmembrane proteins that serve as pattern recognition receptors for microbial pathogens. There are at least eleven 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 human TLR1 consists of a 556 amino acid (aa) extracellular domain (ECD) with 20 LRRs, a 21 aa transmembrane segment, and a 185 aa cytoplasmic domain (3, 4). Within the ECD, human TLR1 shares 63% aa sequence identity with human TLR6 and 20% -43% aa sequence identitity with human TLR2, -3, -4, -5, -7, -8, -9, and -10. It shares 73% and 71% aa sequence identity with mouse 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).
Toll-like receptor 2 activation contributes to oral squamous cell carcinoma development and miRNA-mediated drug resistance By Jamshed Arslan, Pharm. D., PhD. Squamous cell carcinoma is the most common cancer in the oral cavity.1 The tumor surface biofilms in oral cancers contain high levels of aerobic and anaerobic microorganisms.1,2 Peri... Read full blog post. |
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. |
TLR1 TLR1 belongs to the Toll-like receptor (TLR) family, and is a key player in the recognition of pathogens as well as the activation of the innate immunity system. TLRs are highly conserved proteins with a high degree of structural and functional homolo... Read full blog post. |
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