Recombinant Human Interleukin-1 receptor accessory protein (IL1RAP), partial (Active)

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Code CSB-MP878844HU
Abbreviation Recombinant Human IL1RAP protein, partial (Active)
MSDS
Size $186
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  • (Tris-Glycine gel) Discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
  • Activity
    Measured by its binding ability in a functional ELISA. Immobilized Human IL1RAP at 2 μg/ml can bind Anti-IL1RAP recombinant antibody (CSB-RA878844MA1HU). The EC50 is 0.9667-1.477 ng/mL. Biological Activity Assay
  • The purity of IL1RAP was greater than 95% as determined by SEC-HPLC
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Product Details

Purity
Greater than 95% as determined by SDS-PAGE.
Greater than 95% as determined by SEC-HPLC.
Endotoxin
Less than 1.0 EU/ug as determined by LAL method.
Activity
Measured by its binding ability in a functional ELISA. Immobilized Human IL1RAP at 2 μg/mL can bind Anti-IL1RAP recombinant antibody (CSB-RA878844MA1HU). The EC50 is 0.9667-1.477 ng/mL.
Target Names
Uniprot No.
Alternative Names
C3orf13, IL1R3
Species
Homo sapiens (Human)
Source
Mammalian cell
Expression Region
21-359aa
Target Protein Sequence
SERCDDWGLDTMRQIQVFEDEPARIKCPLFEHFLKFNYSTAHSAGLTLIWYWTRQDRDLEEPINFRLPENRISKEKDVLWFRPTLLNDTGNYTCMLRNTTYCSKVAFPLEVVQKDSCFNSPMKLPVHKLYIEYGIQRITCPNVDGYFPSSVKPTITWYMGCYKIQNFNNVIPEGMNLSFLIALISNNGNYTCVVTYPENGRTFHLTRTLTVKVVGSPKNAVPPVIHSPNDHVVYEKEPGEELLIPCTVYFSFLMDSRNEVWWTIDGKKPDDITIDVTINESISHSRTEDETRTQILSIKKVTSEDLKRSYVCHARSAKGEVAKAAKVKQKVPAPRYTVE
Mol. Weight
40.5 kDa
Protein Length
Partial
Tag Info
C-terminal 10xHis-tagged
Form
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.
Buffer
Lyophilized from a 0.2 μm filtered PBS, 6% Trehalose, pH 7.4
Reconstitution
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°C/-80°C. 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
3-7 business days
Notes
Repeated freezing and thawing is not recommended. Store working aliquots at 4°C for up to one week.
Datasheet & COA
Please contact us to get it.
Description

The recombinant human IL1RAP protein is a biologically active molecule produced in mammalian cells, ensuring correct folding and post-translational modifications essential for functionality. It includes the extracellular portion of the IL1RAP protein, covering amino acids 21 to 359, and features a C-terminal 10xHis tag to facilitate purification and analytical use. Supplied as a lyophilized powder, this recombinant IL1RAP protein achieves high purity—greater than 95%—as determined by both SDS-PAGE and SEC-HPLC analyses. Endotoxin levels are maintained below 1.0 EU/µg, verified through the LAL assay, making it suitable for sensitive biological assays. Functional activity is confirmed via ELISA, where the immobilized IL1RAP at 2 μg/mL specifically binds to the anti-IL1RAP recombinant antibody (CSB-RA878844MA1HU), with an EC50 in the range of 0.9667 to 1.477 ng/mL. These properties make it a reliable reagent for studies involving IL1RAP-mediated signaling or antibody interactions.

IL1RAP plays a crucial role in various biological processes, particularly in mediating the signaling pathways associated with interleukin-1 cytokines. IL1RAP is essential for the formation of receptor complexes necessary for the biological activity of the interleukin-1 family of cytokines, including IL-1α and IL-1β. Upon binding to its respective receptors, IL1RAP enhances the signaling cascade that initiates inflammatory responses and immune reactions [1][2].

One key function of IL1RAP is to act as a co-receptor that forms a heterotrimeric complex with the IL-1R and the cytokine itself. This complex is crucial for signal transduction through pathways such as NF-kB, which is pivotal in inflammatory responses and cellular activation [3][4]. For instance, the interaction of IL1RAP with IL-1R leads to the activation of downstream signaling molecules, including MyD88, which is integral to the innate immunity signaling axis [5][6].

Moreover, IL1RAP has a demonstrated role in hematopoiesis and the regulation of specific blood cell populations. Research indicates that IL1RAP upregulation in acute myeloid leukemia (AML) is associated with an increased proliferation of myeloid cells, suggesting it may serve as a biomarker or target for immunotherapy in hematological malignancies [7][8]. Furthermore, it has been implicated in the differentiation and activation of various immune cells, such as T lymphocytes and mast cells, emphasizing its significance in adaptive immunity as well [5][9].

Additionally, IL1RAP exists in various isoforms that have differential expression patterns across tissues, indicating specialized functions depending on the cellular context. For example, the soluble form of IL1RAP has been linked to anti-inflammatory responses, enhancing its complexity beyond merely inflammatory roles [10]. The interplay between different isoforms highlights the nuanced regulation of immune responses and the potential for therapeutic strategies targeting IL1RAP, especially in the context of inflammatory diseases [9].

Lastly, the involvement of IL1RAP in synaptogenesis and neuronal function has been noted, indicating its broader relevance beyond the immune system. In this context, IL1RAP is linked to the organization of synapses and signaling in the central nervous system, contributing to cognitive and emotional processes [4][11].

References:
[1] C. Kim, S. Sohn, S. Jeon, K. Ki-Nam, J. Ryu, & M. Kim. Effect of various implant coatings on biological responses in mg63 using cdna microarray. Journal of Oral Rehabilitation, vol. 33, no. 5, p. 368-379, 2006. https://doi.org/10.1111/j.1365-2842.2005.01553.x
[2] H. Wesche, D. Neumann, K. Resch, & M. Martin. Co‐expression of mrna for type i and type ii interleukin‐1 receptors and the il‐1 receptor accessory protein correlates to il‐1 responsiveness. Febs Letters, vol. 391, no. 1-2, p. 104-108, 1996. https://doi.org/10.1016/0014-5793(96)00713-2
[3] J. Wu, Z. Liu, et al. The long noncoding rna differential expression in peripheral blood leukocyte from schizophrenia patients by rna sequencing. 2020. https://doi.org/10.21203/rs.3.rs-113426/v1
[4] T. Yoshida, T. Shiroshima, et al. Interleukin-1 receptor accessory protein organizes neuronal synaptogenesis as a cell adhesion molecule. Journal of Neuroscience, vol. 32, no. 8, p. 2588-2600, 2012. https://doi.org/10.1523/jneurosci.4637-11.2012
[5] A. Mehrabadi, N. Aghamohamadi, et al. The roles of interleukin‐1 receptor accessory protein in certain inflammatory conditions. Immunology, vol. 166, no. 1, p. 38-46, 2022. https://doi.org/10.1111/imm.13462
[6] K. Mitchell, L. Barreyro, et al. Il1rap potentiates multiple oncogenic signaling pathways in aml. The Journal of Experimental Medicine, vol. 215, no. 6, p. 1709-1727, 2018. https://doi.org/10.1084/jem.20180147
[7] L. Barreyro, B. Will, et al. Overexpression of il-1 receptor accessory protein in stem and progenitor cells and outcome correlation in aml and mds. Blood, vol. 120, no. 6, p. 1290-1298, 2012. https://doi.org/10.1182/blood-2012-01-404699
[8] M. Askmyr, H. Ågerstam, et al. Selective killing of candidate aml stem cells by antibody targeting of il1rap. Blood, vol. 121, no. 18, p. 3709-3713, 2013. https://doi.org/10.1182/blood-2012-09-458935
[9] W. Warda, F. Larosa, et al. Cml hematopoietic stem cells expressing il1rap can be targeted by chimeric antigen receptor–engineered t cells. Cancer Research, vol. 79, no. 3, p. 663-675, 2019. https://doi.org/10.1158/0008-5472.can-18-1078
[10] H. Chung, L. Middleton, et al. Longitudinal clinical and proteomic diabetes signatures in women with a history of postgestational diabetes. Jci Insight, vol. 10, no. 2, 2024. https://doi.org/10.1172/jci.insight.183213
[11] T. Yoshida, M. Yasumura, et al. Il-1 receptor accessory protein-like 1 associated with mental retardation and autism mediates synapse formation bytrans-synaptic interaction with protein tyrosine phosphatase δ. Journal of Neuroscience, vol. 31, no. 38, p. 13485-13499, 2011. https://doi.org/10.1523/jneurosci.2136-11.2011

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Target Background

Function
Coreceptor for IL1RL2 in the IL-36 signaling system. Coreceptor with IL1R1 in the IL-1 signaling system. Associates with IL1R1 bound to IL1B to form the high affinity interleukin-1 receptor complex which mediates interleukin-1-dependent activation of NF-kappa-B and other pathways. Signaling involves the recruitment of adapter molecules such as TOLLIP, MYD88, and IRAK1 or IRAK2 via the respective TIR domains of the receptor/coreceptor subunits. Recruits TOLLIP to the signaling complex. Does not bind to interleukin-1 alone; binding of IL1RN to IL1R1, prevents its association with IL1R1 to form a signaling complex. The cellular response is modulated through a non-signaling association with the membrane IL1R2 decoy receptor. Coreceptor for IL1RL1 in the IL-33 signaling system. Can bidirectionally induce pre- and postsynaptic differentiation of neurons by trans-synaptically binding to PTPRD. May play a role in IL1B-mediated costimulation of IFNG production from T-helper 1 (Th1) cells (Probable).; Associates with secreted ligand-bound IL1R2 and increases the affinity of secreted IL1R2 for IL1B; this complex formation may be the dominant mechanism for neutralization of IL1B by secreted/soluble receptors. Enhances the ability of secreted IL1R1 to inhibit IL-33 signaling.; Unable to mediate canonical IL-1 signaling. Required for Src phosphorylation by IL1B. May be involved in IL1B-potentiated NMDA-induced calcium influx in neurons.
Gene References into Functions
  1. Expression level of sIL1RAP may become one of the potential indexes for determining the prognosis of low-grade gliomas PMID: 29238884
  2. These results provide novel insights into the role of IL1RAP in CML and a strong rationale for the development of an IL1RAP antibody therapy to target residual CML stem cells. PMID: 27621309
  3. single nucleotide polymorphism A471T in the Toll-interleukin 1 receptor domain (TIR) of the IL-1Rrp2 that is present in approximately 2% of the human population, down-regulated IL-36R signaling by a decrease of interaction with IL-1RAcP. PMID: 27307043
  4. The findings of this study support IL1RAP as a novel potential Alzheimer's disease target and highlight the use of amyloid PET as a valuable Alzheimer's disease endophenotype, particularly in a longitudinal framework. PMID: 26268530
  5. The SNP rs4624606 in IL-1RAcP was nominally associated with CAD risk. PMID: 25517029
  6. Data suggest serum levels of soluble IL1RAP (from alternative splicing) are down-regulated in endometriosis throughout menstrual cycle; IL1RAP levels (which peak in proliferative phase in fertile women) exhibit minor variations in endometriosis. PMID: 24935223
  7. Plasma sIL1RAP levels are reduced in obesity and can potentially act as biomarkers of obesity. PMID: 24915116
  8. Combined crystallography and small-angle X-ray-scattering studies reveal that ST2 possesses hinge flexibility between the D3 domain and D1D2 module, whereas IL-1RAcP exhibits a rigid conformation in the unbound state in solution. PMID: 23980170
  9. Knockdown of IL1RAP decreased clonogenicity and increased cell death of AML cells. PMID: 22723552
  10. Interleukin-1R3 mediates interleukin-1-induced potassium current increase through fast activation of Akt kinase. PMID: 22778412
  11. decreased protein levels in the peritoneal fluid of women with endometriosis PMID: 21958553
  12. Studies indicate that new targets have recently been investigated as potential modulators in myeloid leukemia pathogenesis, including miR-328, BMI1, FOXOs and IL1RAP. PMID: 21373837
  13. This study showed a significant downregulation of soluble interleukin-1 receptor accessory protein expression in the endometrium of women with endometriosis. PMID: 21272866
  14. identifies IL1RAP as a unique cell surface biomarker distinguishing Ph(+) from Ph(-) candidate chronic myeloid leukemia (CML) stem cells and opens up a previously unexplored avenue for therapy of CML PMID: 20805474
  15. Identification of essential regions in the cytoplasmic tail of interleukin-1 receptor accessory protein critical for interleukin-1 signaling PMID: 11880380
  16. soluble form of IL-1R AcP contributes to the antagonism of IL-1 action by the type II decoy receptor PMID: 12530978
  17. The dramatic changes in levels of IL-1RAcP mRNAs suggest important functions in regulating sensitivity to IL-1 during stress and may play a role in oncogenic processes that are engaged during chronic inflammation. PMID: 12781872
  18. IL-1F6, IL-1F8, and IL-1F9 signal through IL-1Rrp2 and IL-1RAcP in Jurkat cells PMID: 14734551
  19. Specific destabilization of membrane-bound IL-1 receptor accessory protein mRNA in HepG2 hepatoma cells is mediated by its 2.8-kilobase 3'-untranslated region. PMID: 15528363
  20. Analysis of a three-dimensional docking model of the TIR-TIR interaction between MyD88 and IL1RAcP PMID: 15849357
  21. IL-1ra is associated with preserved beta-cell capacity in type 1 diabetes. PMID: 18299313
  22. an isoform of the IL-1 receptor accessory protein (termed AcPb) was identified that is expressed exclusively in the CNS. PMID: 19481478

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Subcellular Location
[Isoform 1]: Cell membrane; Single-pass type I membrane protein.; [Isoform 2]: Secreted.; [Isoform 3]: Secreted.
Protein Families
Interleukin-1 receptor family
Tissue Specificity
Detected in liver, skin, placenta, thymus and lung. Isoform 4 is predominantly expressed in brain. Overexpressed on candidate chronic myeloid leukemia (CML) stem cells, hematopoietic stem cells and mononuclear cells of patients with acute myeloid leukemia
Database Links

HGNC: 5995

OMIM: 602626

KEGG: hsa:3556

UniGene: Hs.478673

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