TLR2 Mouse
Sf9, Baculovirus cells.
Toll-like receptor 2, CD282.
Greater than 85.0% as determined by SDS-PAGE.
Description
TLR2 Mouse Recombinant produced in Sf9 Baculovirus cells is a single, glycosylated polypeptide chain containing 805 amino acids (25-587a.a.) and having a molecular mass of 90.7kDa. (Molecular size on SDS-PAGE will appear at approximately 70-100kDa).
TLR2 is expressed with a 239 amino acid hIgG-His tag at C-Terminus and purified by proprietary chromatographic techniques.
Product Specs
Toll-like receptor 2 (TLR2) is a key player in the immune system's ability to recognize and respond to pathogens. It is part of a family of proteins called Toll-like receptors (TLRs), which are evolutionarily conserved and share similar structures and functions. TLRs identify specific molecules associated with pathogens, known as pathogen-associated molecular patterns (PAMPs). Upon recognizing PAMPs, TLRs trigger the production of signaling molecules called cytokines, which are essential for mounting an effective immune response. Different TLRs are expressed on various cell types, and TLR2 is primarily found on immune cells like peripheral blood leukocytes. TLR2 specifically recognizes components of Gram-positive bacteria and yeast, leading to the activation of the NF-kappaB pathway, a crucial signaling pathway in immune responses.
Recombinant TLR2 protein, derived from mice, is produced using Sf9 insect cells infected with a baculovirus expression system. This process generates a single, glycosylated polypeptide chain containing 805 amino acids (specifically, amino acids 25 to 587). The resulting TLR2 protein has a molecular weight of 90.7 kDa. However, due to glycosylation, it appears as a band between 70-100 kDa on SDS-PAGE. For purification and detection purposes, a 239 amino acid human IgG-His tag is fused to the C-terminus of the protein. Proprietary chromatographic techniques are employed to purify the TLR2 protein.
The TLR2 protein is provided as a solution at a concentration of 0.25 mg/ml. The solution is prepared in Phosphate Buffered Saline (PBS) with a pH of 7.4 and contains 10% glycerol.
Adding a carrier protein like HSA or BSA (0.1%) is recommended for long-term storage.
Avoid repeated freezing and thawing cycles.
The purity of TLR2 protein is greater than 85%, as determined by SDS-PAGE analysis.
Toll-like receptor 2, CD282.
Sf9, Baculovirus cells.
ADLQESLSCD ASGVCDGRSR SFTSIPSGLT AAMKSLDLSF NKITYIGHGD LRACANLQVL MLKSSRINTI EGDAFYSLGS LEHLDLSDNH LSSLSSSWFG PLSSLKYLNL MGNPYQTLGV TSLFPNLTNL QTLRIGNVET FSEIRRIDFA GLTSLNELEI KALSLRNYQS QSLKSIRDIH HLTLHLSESA FLLEIFADIL SSVRYLELRD TNLARFQFSP LPVDEVSSPM KKLAFRGSVL TDESFNELLK LLRYILELSE VEFDDCTLNG LGDFNPSESD VVSELGKVET VTIRRLHIPQ FYLFYDLSTV YSLLEKVKRI TVENSKVFLV PCSFSQHLKS LEFLDLSENL MVEEYLKNSA CKGAWPSLQT LVLSQNHLRS MQKTGEILLT LKNLTSLDIS RNTFHPMPDS CQWPEKMRFL NLSSTGIRVV KTCIPQTLEV LDVSNNNLDS FSLFLPRLQE LYISRNKLKT LPDASLFPVL LVMKIRENAV STFSKDQLGS FPKLETLEAG DNHFVCSCEL LSFTMETPAL AQILVDWPDS YLCDSPPRLH GHRLQDARPS VLECHQLEPK SCDKTHTCPP CPAPELLGGP SVFLFPPKPK DTLMISRTPE VTCVVVDVSH EDPEVKFNWY VDGVEVHNAK TKPREEQYNS TYRVVSVLTV LHQDWLNGKE YKCKVSNKAL PAPIEKTISK AKGQPREPQV YTLPPSRDEL TKNQVSLTCL VKGFYPSDIA VEWESNGQPE NNYKTTPPVL DSDGSFFLYS KLTVDKSRWQ QGNVFSCSVM HEALHNHYTQ KSLSLSPGKH HHHHH.
Product Science Overview
Toll-like receptors (TLRs) are a family of pattern recognition receptors (PRRs) that play a crucial role in the innate immune system by recognizing pathogen-associated molecular patterns (PAMPs) and danger-associated molecular patterns (DAMPs). Among these, Toll-like receptor 2 (TLR2) is particularly significant due to its ability to recognize a wide range of microbial components.
TLR2 was first identified as a receptor similar to the Drosophila Toll protein in 1998 . The TLR2 gene, located on chromosome 4, encodes the TLR2 protein, which is a type I transmembrane protein. The initial understanding of TLR2’s function came from studies showing its role in recognizing components of gram-positive bacteria .
TLR2 consists of three main domains:
TLR2 is expressed in various immune cells, including dendritic cells and macrophages. It recognizes a broad spectrum of microbial components, including lipoproteins, peptidoglycans, and lipoteichoic acids from gram-positive bacteria . Upon ligand binding, TLR2 forms heterodimers with either TLR1 or TLR6, which is essential for its function .
The activation of TLR2 triggers the myeloid differentiation primary-response protein 88 (MyD88)-dependent signaling pathway. This leads to the production of pro-inflammatory cytokines and type I interferons, which are crucial for initiating and regulating the immune response .
TLR2 has been implicated in various diseases, including infections, inflammatory conditions, and autoimmune disorders. For instance, TLR2 signaling is involved in the immune response to Clostridioides difficile infection . Overactivation of TLR2 can lead to chronic inflammation and tissue damage, making it a potential target for therapeutic interventions .
Recombinant TLR2 proteins, such as those derived from mice, are widely used in research to study the receptor’s function, signaling pathways, and role in disease. These recombinant proteins are produced using genetic engineering techniques and are essential tools for understanding TLR2’s mechanisms and developing new therapeutic strategies.
