Recombinant Mouse Single Ig Il-1-Related Receptor (SIGIRR) Protein (His-SUMO)

Name: Recombinant Mouse Single Ig Il-1-Related Receptor (SIGIRR) Protein (His-SUMO)
Brand: Beta LifeScience
SKU: BLC-08663P
Availability: InStock

Greater than 90% as determined by SDS-PAGE.

Collections: All products, High-quality recombinant proteins, Other recombinant proteins

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Product Overview

Description	Recombinant Mouse Single Ig Il-1-Related Receptor (SIGIRR) Protein (His-SUMO) is produced by our E.coli expression system. This is a protein fragment.
Purity	Greater than 90% as determined by SDS-PAGE.
Uniprotkb	Q9JLZ8
Target Symbol	SIGIRR
Synonyms	Sigirr; Tir8; Single Ig IL-1-related receptor; Single Ig IL-1R-related molecule; Single immunoglobulin domain-containing IL1R-related protein; Toll/interleukin-1 receptor 8; TIR8
Species	Mus musculus (Mouse)
Expression System	E.coli
Tag	N-6His-SUMO
Target Protein Sequence	MAGVCDMAPNFLSPSEDQALGLALGREVALNCTAWVFSRPQCPQPSVQWLKDGLALGNGSHFSLHEDFWVSANFSEIVSSVLVLNLTNAEDYGTFTCSVWNVSSHSFTLWRAGPAGH
Expression Range	1-117aa
Protein Length	Partial
Mol. Weight	28.7kDa
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	Acts as a negative regulator of the Toll-like and IL-1R receptor signaling pathways. Attenuates the recruitment of receptor-proximal signaling components to the TLR4 receptor, probably through an TIR-TIR domain interaction with TLR4. Through its extracellular domain interferes with the heterodimerization of Il1R1 and IL1RAP.
Subcellular Location	Membrane; Single-pass type III membrane protein.
Protein Families	Interleukin-1 receptor family
Database References	KEGG: mmu:24058 STRING: 10090.ENSMUSP00000095571 UniGene: PMID: 28347403 Commensal flora depletion and IL-1R1 deficiency abated platelet hyperactivity and the increased platelet/neutrophil aggregation observed in Il1r8(-/-) mice in vitro and in vivo, suggesting a key role of IL-1R8 in regulating platelet TLR and IL-1R1 function PMID: 27297888 Tir8/SIGIRR acts anti-inflammatory on different immune responses,its function in allergic asthma is a controversial issue, since anti- as well as pro-inflammatory effects have been reported PMID: 26561030 Expression of SIGIRR(N86/102S) in the colonic epithelium of mice increases expression of inflammatory cytokines and formation and size of colitis-associated tumors. PMID: 26344057 IL-37 requires IL-18Ralpha and SIGIRR/IL-1R8 to diminish allergic airway inflammation in mice PMID: 25557042 IL-37 requires the receptors IL-18Ralpha and IL-1R8 to carry out its multifaceted anti-inflammatory program upon innate signal transduction. PMID: 25729923 impairs the antibacterial host defense during pneumonia and sepsis caused by S. pneumoniae PMID: 24556793 IL-37 acts as an extracellular cytokine by binding to the IL-18 receptor but using the IL-1R8 for its anti-inflammatory properties. PMID: 25654981 Thus, SIGIRR expression by IEC reflects a strategy that sacrifices maximal innate responsiveness by IEC in order to promote commensal microbe based colonization resistance against bacterial pathogens. PMID: 23950714 This study identifies TIR8/SIGIRR as a novel intrinsic negative regulator of innate IL-17A expression PMID: 23945140 Absence of TIR8 reduces house dust mite-induced allergic airway inflammation in mice. PMID: 23614768 data suggest that TIR8 is an important negative regulator of an LPS-mediated inflammatory response in tubular epithelial cells and dampens an effective antibacterial host response during pyelonephritis PMID: 22890991 TIR8 has a nonredundant effect in modulating the inflammation caused by Pseudomonas aeruginosa, in particular, by negatively regulating IL-1RI signaling, which plays a major role in the pathogenesis of bacterial pneumonia. PMID: 22025515 in the absence of TIR8 the appearance of monoclonal B-cell expansions is accelerated and mouse life span is shortened in chronic lymphocytic leukemia PMID: 21652674 Data argue against a significant role of SIGIRR in renal fibrosis. PMID: 21544241 These findings highlight the functional role of SIGIRR in regulating inflammatory-mediated synaptic and cognitive decline PMID: 21389242 modulating the expression level of SIGIRR may be a promising potential treatment for acute lung injury. PMID: 20661180 SIGIRR is expressed constitutively in intestinal epithelial cells to maintain gut innate immunity and then down-regulated during inflammation by inhibition of an SP1-mediated pathway. PMID: 21077278 we set out to establish whether the absence of SIGIRR was associated with inflammatory changes in the brain PMID: 20394816 Loss of single immunoglobulin interlukin-1 receptor-related molecule leads to enhanced colonic polyposis in Apc(min) mice. PMID: 20416302 Our results demonstrate an important mechanism by which SIGIRR controls Th17 cell expansion and effector function through the IL-1-induced mTOR signaling pathway. PMID: 20060329 regulatory functions in inflammation and Th1/Th2 cell polarization (Review) PMID: 19699681 TIR8 represents a negative pathway of regulation of the IL-1 receptor/TLR system, expressed in epithelial cells and DC, crucial for tuning inflammation in the gastrointestinal tract. PMID: 14993616 SIGIRR is critical in resistance to Pseudomonas aeruginosa corneal infection by down-regulating type 1 immunity and negative regulation of IL-1 and TLR4 signaling. PMID: 16785552 Theses results indicate that epithelium-derived SIGIRR is critical in controlling the homeostasis and innate immune responses of the colon to enteric microflora. PMID: 17398123 resident myeloid cells contribute to TLR-mediated antimicrobial immunity in the kidney, controlled by Tir8. Tir8 does not suppress TLR signaling in tubular epithelial cells, which supports their role as sensors of microbial infection in the kidney. PMID: 17495864 TIR8, by negatively regulating intestinal inflammation, plays a nonredundant role in the control of the protumor activity of chronic inflammation in the gut PMID: 17616656 TIR8/SIGIRR plays a key role in damping inflammation and tissue damage in M. tuberculosis infection. PMID: 17709526 As a consequence of its interaction with the orphan receptor, single Ig IL-1R-related molecule (SIGIRR)/TIR8, IL-1F5 mediates anti-inflammatory effects in brain tissue. PMID: 18284608 Tir8 acts as a negative regulator of the Th17 pathway in fungal infections and is essentially required to fine-tune the inflammatory and adaptive immune response to Candida albicans and Aspergillus fumigatus. PMID: 18322211 lack of Sigirr enhanced the activation and proliferation of B cells, including the production of autoantibodies against multiple nuclear lupus autoantigens. These data identify Sigirr as a novel SLE susceptibility gene. PMID: 18644972 SIGIRR plays an important role in the regulation of T helper (Th)2 cell response in vivo, possibly through its impact on interleukin-33-ST2-mediated signaling. PMID: 19234154 SIGIRR prevents overshooting tissue injury by suppressing the postischemic activation of intrarenal myeloid cells. PMID: 19692646 TIR8 acts locally as a key regulator of allogeneic immune response in the kidney; in a mouse model of kidney graft acceptance induced by costimulation blockade, most Tir8-deficient grafts are acutely rejected. PMID: 19734209

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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.