Recombinant Mouse Toll-Like Receptor 11 (TLR11) Protein (His&Myc)

Beta LifeScience SKU/CAT #: BLC-01713P
Greater than 90% as determined by SDS-PAGE.
Greater than 90% as determined by SDS-PAGE.

Recombinant Mouse Toll-Like Receptor 11 (TLR11) Protein (His&Myc)

Beta LifeScience SKU/CAT #: BLC-01713P
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Product Overview

Description Recombinant Mouse Toll-Like Receptor 11 (TLR11) Protein (His&Myc) is produced by our E.coli expression system. This is a protein fragment.
Purity Greater than 90% as determined by SDS-PAGE.
Uniprotkb Q6R5P0
Target Symbol TLR11
Synonyms Toll-like receptor 12
Species Mus musculus (Mouse)
Expression System E.coli
Tag N-10His&C-Myc
Target Protein Sequence RGQFNYDVFISYCEEDQAWVLEELVPVLEKAPPEGEGLRLCLPARDFGIGNDRMESMIASMGKSRATLCVLTGQALASPWCNLELRLATYHLVARPGTTHLLLLFLEPLDRQRLHSYHRLSRWLQKEDYFDLSQGKVEWNSFCEQLKRRLSKAGQERD
Expression Range 769-926aa
Protein Length Partial
Mol. Weight 25.7 kDa
Research Area Immunology
Form Liquid or Lyophilized powder
Buffer Liquid form: default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol. Lyophilized powder form: the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
Reconstitution Briefly centrifuged the vial prior to opening to bring the contents to the bottom. Reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL. It is recommended to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20°C/-80°C. The default final concentration of glycerol is 50%.
Storage 1. Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. 2. Avoid repeated freeze-thaw cycles. 3. Store working aliquots at 4°C for up to one week. 4. In general, protein in liquid form is stable for up to 6 months at -20°C/-80°C. Protein in lyophilized powder form is stable for up to 12 months at -20°C/-80°C.
Notes Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.

Target Details

Target Function Participates in the innate immune response to microbial agents. Acts via MYD88 and TRAF6, leading to NF-kappa-B activation, cytokine secretion and the inflammatory response.
Subcellular Location Membrane; Single-pass type I membrane protein.
Protein Families Toll-like receptor family
Database References

KEGG: mmu:239081

STRING: 10090.ENSMUSP00000068906

UniGene: PMID: 26859749

  • Data show that TLR11 expression is induced in astrocytes, neurons, and microglia in the immune response to T. gondii infection PMID: 24704432
  • TLR11 mediates innate immune function of male germ cells in response to T. gondii profilin and uropathogenic escherichia coli stimulations. PMID: 24403550
  • Biochemical experiments revealed that TLR11 and TLR12 directly bind to Toxoplasma gondii profilin and are capable of forming a heterodimer complex. PMID: 24078692
  • Selective elimination of neutrophils in TLR11-deficient mice infected with Toxoplasma gondii results in acute susceptibility similar to that observed in IFN-gamma-deficient mice. PMID: 23754402
  • a potentially important role for TLR11 in preventing murine intestinal infection and modulating antigen transportation in the gut and imply an important role for various TLRs in cooperation with tight control of pathogens penetrating into Peyer patches. PMID: 23135279
  • association with UNC93B1 and the intracellular localization of TLRs are not unique features of nucleic acid-sensing TLRs but is also essential for TLR11-dependent recognition of T. gondii profilin and for host protection against this parasite PMID: 21097503
  • Data demonstrate that transcription of the Tlr11 gene is regulated through epithelium-specific transcription factors and IRF-8. PMID: 19801549
  • displays a distinct pattern of expression in macrophages and liver, kidney, and bladder epithelial cells; mice lacking TLR11 are highly susceptible to infection of the kidneys by uropathogenic bacteria PMID: 15001781
  • Toxoplasma gondii profilin activates dendritic cells through TLR11 and is the first chemically defined ligand for this TLR; TLR11 is required in vivo for parasite-induced IL-12 production and optimal resistance to infection PMID: 15860593
  • The immunogenicity of Toxoplasma gondii profilin was entirely dependent on both TLR11 recognition and signaling through the adaptor myeloid differentiation factor 88 (MyD88). PMID: 17000122
  • TLR11-deficient mice develop an abnormal immunopathological response to Toxoplasma gondii, as the result of non-toll-like receptor dependent activation of interferon-gamma secretion by natural killer cells in response to the infection. PMID: 19050265
  • TLRs 11-13 are expressed in normal and parasite infected mouse brains. This suggests a role for them in central nervous system infections. PMID: 19077284

    • FAQs

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    Proteins are sensitive to heat, and freeze-drying can preserve the activity of the majority of proteins. It improves protein stability, extends storage time, and reduces shipping costs. However, freeze-drying can also lead to the loss of the active portion of the protein and cause aggregation and denaturation issues. Nonetheless, these adverse effects can be minimized by incorporating protective agents such as stabilizers, additives, and excipients, and by carefully controlling various lyophilization conditions.

    Commonly used protectant include saccharides, polyols, polymers, surfactants, some proteins and amino acids etc. We usually add 8% (mass ratio by volume) of trehalose and mannitol as lyoprotectant. Trehalose can significantly prevent the alter of the protein secondary structure, the extension and aggregation of proteins during freeze-drying process; mannitol is also a universal applied protectant and fillers, which can reduce the aggregation of certain proteins after lyophilization.

    Our protein products do not contain carrier protein or other additives (such as bovine serum albumin (BSA), human serum albumin (HSA) and sucrose, etc., and when lyophilized with the solution with the lowest salt content, they often cannot form A white grid structure, but a small amount of protein is deposited in the tube during the freeze-drying process, forming a thin or invisible transparent protein layer.

    Reminder: Before opening the tube cap, we recommend that you quickly centrifuge for 20-30 seconds in a small centrifuge, so that the protein attached to the tube cap or the tube wall can be aggregated at the bottom of the tube. Our quality control procedures ensure that each tube contains the correct amount of protein, and although sometimes you can't see the protein powder, the amount of protein in the tube is still very precise.

    To learn more about how to properly dissolve the lyophilized recombinant protein, please visit Lyophilization FAQs.

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