Recombinant Human Single Ig IL-1-related receptor(SIGIRR),partial

Code CSB-MP743558HU
Size $228
  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
  • The purity of Human SIGIRR was greater than 95% as determined by SEC-HPLC.
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Product Details

Greater than 95% as determined by SDS-PAGE.
Not Test
Target Names
Uniprot No.
Research Area
Alternative Names
Single Ig IL-1R-related molecule;Single immunoglobulin domain-containing IL1R-related protein;Toll/interleukin-1 receptor 8 (TIR8)
Homo sapiens (Human)
Mammalian cell
Expression Region
Target Protein Sequence
Note: The complete sequence including tag sequence, target protein sequence and linker sequence could be provided upon request.
Mol. Weight
14.8 kDa
Protein Length
Tag Info
C-terminal 6xHis-tagged
Liquid or Lyophilized powder
Note: We will preferentially ship the format that we have in stock, however, if you have any special requirement for the format, please remark your requirement when placing the order, we will prepare according to your demand.
If the delivery form is liquid, the default storage buffer is Tris/PBS-based buffer, 5%-50% glycerol.If the delivery form is lyophilized powder, the buffer before lyophilization is Tris/PBS-based buffer, 6% Trehalose, pH 8.0.
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Please reconstitute protein in deionized sterile water to a concentration of 0.1-1.0 mg/mL.We recommend to add 5-50% of glycerol (final concentration) and aliquot for long-term storage at -20℃/-80℃. Our default final concentration of glycerol is 50%. Customers could use it as reference.
Troubleshooting and FAQs
Storage Condition
Store at -20°C/-80°C upon receipt, aliquoting is necessary for mutiple use. Avoid repeated freeze-thaw cycles.
Shelf Life
The shelf life is related to many factors, storage state, buffer ingredients, storage temperature and the stability of the protein itself.
Generally, the shelf life of liquid form is 6 months at -20°C/-80°C. The shelf life of lyophilized form is 12 months at -20°C/-80°C.
Lead Time
Delivery time may differ from different purchasing way or location, please kindly consult your local distributors for specific delivery time.
Repeated freezing and thawing is not recommended. Store working aliquots at 4℃ for up to one week.
Datasheet & COA
Please contact us to get it.

A DNA fragment encoding the extracellular domain (1-118aa) of the human SIGIRR was fused with a C-terminal 6xHis-tag and expressed in mammalian cells. The resulting product is the recombinant human single Ig IL-1-related receptor (SIGIRR) protein. The purity of the recombinant human SIGIRR protein was determined to be greater than 95% using SDS-PAGE and SEC-HPLC analyses. This recombinant human SIGIRR protein can be used in immunology-related research, including studies on IL-1 signaling, TLR signaling, and the NF-κB pathway. The SIGIRR protein acts as a negative regulator of immune responses and inflammation, providing a mechanism to fine-tune and balance the immune system. Its function is to inhibit IL-1 signaling, attenuate TLR signaling, and regulate the NF-κB pathway, thereby maintaining immune homeostasis and preventing inflammatory disorders.

Customer Reviews and Q&A

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What validations or detections have you performed for this protein SIGIRR?


Normally, we provide molecular weight, electrophoretic results (SDS-PAGE), concentration, purity, etc. For this protein, we have also done HPLC verification. If you have special demand, we can also provide electrophoretic parameters, activity evaluation, sequence identification, tag removal service, endotoxin removal service, WB and MS validations. You can learn more from this link:


What is the impact of the tag on any potential biological activity of the SIGIRR protein?


Theoretically small tags generally have very small influence on protein activity. However, the specific impact on protein activity can't be concluded (There is no impact on some proteins, small impact on some proteins, and relatively great impact on some proteins).


Can you remove the endotoxin?


Not all endotoxin can be removed. Please contact us in advance if you need to remove endotoxin, which takes 2-3 business days. We could offer endotoxin removal service free of charge using PMB affinity chromatography, use LAL reagent to semi-quantitatively detect the content of endotoxin and guarantee endotoxin level within 0.1 ng/μg (1 EU/μg).


Why is the actual band size different from the predicted one?


a. Post-translational modification. Phosphorylation, glycosylation, etc which increases the size of the protein.
b. Post-translational cleavage. Many proteins are synthesized as pro-proteins, and then cleaved to give the active form.
c. Splice variants. Alternative splicing may create different sized proteins from the same gene.
d. Relative charge. The composition of amino acids have different relative charge which will affect the electrophoretic mobility.
e. Multimers such as dimerization of a protein. This is usually prevented in reducing conditions, although strong interactions can result in the appearance of higher bands.
f. Protein structure such as disulfide bond, protein secondary structure, or protein 3D structure formation.
g. Hydrophobic proteins, such as transmembrane proteins, may have difficulties in migrating into the gel and thus resulting in different multi-banded patterns.


Can this protein be used in ELISA/WB experiments?


ELISA/WB is mainly aimed at protein immunoreactivity. In theory, this protein is applicable to ELISA/WB experiments, but it is necessary to confirm whether your antibody-antigen information matches, including sequence, expression system, etc., mainly to determine whether the sequence information of the protein (antigen) is consistent with the immunogenic sequence information of the antibody.


Is this SIGIRR protein cell-component-free?


The protein expressed in the body, regardless of the system, is expressed by cell, and the cell expression can be divided into intracellular expression and secretory expression.
The E. coli system only has intracellular expression and needs to be broken, so the cell components are relatively more secreted than other systems.
Yeast, Baculovirus, and Mammalian cell systems can be expressed both in the cell and in the secretory expression, and the secreted expression of the protein component remains relatively less intracellular.
In vitro expression means that cell-free, and the E. coli cell extract is also added, so that the cell component remains.
Therefore, no matter which expression system and which way the protein is expressed, there will be residual cell components, but we finally use affinity chromatography to purify. In theory, the residual of the cell components will be very small, but 100% of no residue cannot be guaranteed. (Nor does any company dare to guarantee).


How long can I get the products after I place an order?


We have enough quantity of this protein in stock and can be shipped out in 3-7 business days once passing our Quality Control process. Each of our proteins will undergo a strict QC process before being delivered.

Target Background

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.
Gene References into Functions
  1. SIGIRR is both a negative regulator of TLR4 and a positive regulator of TLR7/8. PMID: 28869081
  2. Our results indicate that high IL-1R8 expression acts as a novel immunomodulatory mechanism leading to dysregulated immunity with important implications for breast cancer immunotherapy. PMID: 28533483
  3. show by flow cytometry analysis, western blot, confocal microscopy, and quantitative real-time polymerase chain reaction that IL-1R8 is expressed on human and mouse platelets at high levels and on megakaryocytes. IL-1R8-deficient mice show normal levels of circulating platelets PMID: 27297888
  4. 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
  5. SIGIRR plays an important role in the negative regulation of LPS response and tolerance in human bladder epithelial cells, possibly through its impact on TLR-mediated signaling. PMID: 26634342
  6. Levels of SIGIRR are lower in human colorectal tumors, compared with nontumor tissues; tumors contain the dominant-negative isoform SIGIRR(DeltaE8). PMID: 26344057
  7. SIGIRR predicts biochemical recurrence in patients with low Gleason score and low pathological stage prostate cancer. PMID: 26344417
  8. decreased numbers of SIGIRR-positive CD4+ T cells in SLE patients and its correlation with SLEDAI score as well as the clinical data suggest that SIGIRR may be involved in the pathogenesis of SLE. PMID: 25287661
  9. To the best of our knowledge, this is one of the first reports of a phenotype associated with SIGIRR in humans. Our data provide novel mechanistic insight into the probable causation of necrotizing enterocolitis PMID: 25963006
  10. An association was found in the SIGIRR rs7396562 polymorphism and systemic lupus erythematosus susceptibility in a Chinese population. PMID: 24826913
  11. IL-37 requires the receptors IL-18Ralpha and IL-1R8 to carry out its multifaceted anti-inflammatory program upon innate signal transduction. PMID: 25729923
  12. 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
  13. Lipopolysaccharide decreases SIGIRR expression by suppressing specificity protein 1 Sp1 via the TLR4-p38 pathway in monocytes and neutrophils. PMID: 24821721
  14. the tested variations of IRAK-M and SIGIRR genes do not confer a relevant role in the susceptibility to systemic lupus erythematosus in European-descent populations PMID: 22634523
  15. These results demonstrate a strong association of single-nucleotide polymorphisms in the PKP3-SIGIRR-TMEM16J gene region and tuberculosis in discovery and validation cohorts. PMID: 22223854
  16. These results suggest that PALM3 may function as an adaptor in the LPS- Toll-like receptor 4 signaling and the interaction of SIGIRR with PALM3 may partly account for the mechanism of the negatively regulatory effect of SIGIRR. PMID: 21187075
  17. 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
  18. SIGIRR/TIR-8 is an inhibitor of Toll-like receptor signaling in primary human cells and regulates inflammation in models of rheumatoid arthritis PMID: 20506350
  19. regulatory functions in inflammation and Th1/Th2 cell polarization (Review) PMID: 19699681
  20. SIGIRR inhibits IL-1R and TLR4-mediated signaling through different mechanisms PMID: 15866876

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Subcellular Location
Membrane; Single-pass type III membrane protein.
Protein Families
Interleukin-1 receptor family
Tissue Specificity
Mainly expressed in epithelial tissues such as kidney, lung and gut.
Database Links

HGNC: 30575

OMIM: 605478

KEGG: hsa:59307

STRING: 9606.ENSP00000333656

UniGene: Hs.501624

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