€521.00 €442.85
The toll-like receptors (TLRs) in mammals comprise a family of transmembrane proteins characterized by multiple copies of leucine rich repeats in the extracellular domain and an interleukin-1 (IL-1) receptor motif in the cytoplasmic domain. Like their counterparts in Drosophila, TLRs signal through adaptor molecules.{17463} The TLR family is a phylogenetically conserved mediator of innate immunity that is essential for microbial recognition.{17464} Most mammalian species have between ten and fifteen types of TLRs. Ten functional TLRs (TLR1-10) have been identified in human. Humans also encode a TLR11 gene but it contains several stop codons and protein is not expressed. However, mouse and rat TLR11 are functional, and it is thought that human TLR11 function was lost during evolution. TLR2 is differentially expressed in human cells. Historically speaking, TLR expression has been most extensively studied in the immune system. Overall, TLRs are highly expressed in immune competent cells, including macrophages, dendritic cells, neutrophils, mucosal epithelial cells and dermal endothelial cells. However, TLRs have also been identified in many other cell types and anatomical tissue locations where they are expressed either constitutively or induced during infection. In mice, TLR1 interacts with TLR2 and coexpression of TLR1 and TLR2 enhances the NF-kB activation in response to a synthetic lipopeptide. Together, they recognize the lipid configuration of the native mycobacterial lipoprotein as well as several triacylated lipopeptides.
Territorial Availability: Available through Bertin Technologies only in France
| Size | 1 ea |
|---|---|
| Shipping | dry ice |
| Molecular weight | 0 |
| Host | Rabbit |
| Antigen | synthetic peptide from human TLR1 amino acids 400-450 |
| Application(s) | cell surface), FC (intracellular), WB |
| Formulation | 0.1 mg of protein G-purified in 0.2 ml PBS containing 0.05% BSA and 0.05% sodium azide |
| Custom code | 3822.19 |
| UNSPSC code | 12352203 |
Cayman Chemical’s mission is to help make research possible by supplying scientists worldwide with the basic research tools necessary for advancing human and animal health. Our utmost commitment to healthcare researchers is to offer the highest quality products with an affordable pricing policy.
Our scientists are experts in the synthesis, purification, and characterization of biochemicals ranging from small drug-like heterocycles to complex biolipids, fatty acids, and many others. We are also highly skilled in all aspects of assay and antibody development, protein expression, crystallization, and structure determination.
Over the past thirty years, Cayman developed a deep knowledge base in lipid biochemistry, including research involving the arachidonic acid cascade, inositol phosphates, and cannabinoids. This knowledge enabled the production of reagents of exceptional quality for cancer, oxidative injury, epigenetics, neuroscience, inflammation, metabolism, and many additional lines of research.
Our organic and analytical chemists specialize in the rapid development of manufacturing processes and analytical methods to carry out clinical and commercial GMP-API production. Pre-clinical drug discovery efforts are currently underway in the areas of bone restoration and repair, muscular dystrophy, oncology, and inflammation. A separate group of Ph.D.-level scientists are dedicated to offering Hit-to-Lead Discovery and Profiling Services for epigenetic targets. Our knowledgeable chemists can be contracted to perform complete sample analysis for analytes measured by the majority of our assays. We also offer a wide range of analytical services using LC-MS/MS, HPLC, GC, and many other techniques.
Accreditations
ISO/IEC 17025:2005
ISO Guide 34:2009
Cayman is a leader in the field of emerging drugs of abuse, providing high-purity Schedule I-V Controlled Substances to federally-licensed laboratories and qualified academic research institutions for forensic analyses. We are certified by ACLASS Accreditation Services with dual accreditation to ISO/IEC 17025:2005 and ISO Guide 34:2009.
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