Mouse Recombinant IL1RAP protein, ECD, hFc Tag (V2LY-0526-LY8509)

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Basic Information

Expressed Host
HEK293 Cells
Protein Species
Mouse
Tag
hFc Tag
Protein Construction
This product is Mouse Recombinant IL1RAP protein, ECD, hFc Tag consist of Amino Acid: 1-350 and predicts a molecular mass of 65 kDa.
Molecule Mass
65 kDa
Protein Domain
ECD
Verified
HPLC
Sequence
Amino Acid: 1-350
Species
Mouse

Formulations & Storage [For reference only, actual COA shall prevail!]

Purity
≥95% as determined by SDS-PAGE. ≥95% as determined by SEC-HPLC.
Endotoxin
Please contact us for more information.
Format
Lyophilized
Reconstitution
Allow the vial and reconstitution buffer to equilibrate to room temperature. Briefly centrifuge or tap down the vial to ensure that all lyophilized powder is collected at the bottom of the vial. For the reconstitution of this product, we recommend adding PBS or sterile water to achieve a final antibody concentration of 1 mg/mL. Allow the vial to reconstitute for 10-15 minutes at room temperature with gentle agitation. Avoid vigorous shaking that can cause foaming and antibody denaturation. Aliquot into volumes based on your experiment and store liquid protein at -20°C or -80°C for long time.
Buffer
Lyophilized from sterile Tris, NaCl
Preservative
None
Storage
Samples are stable for up to twelve months from date of receipt at -20°C to -80°C. Store it under sterile conditions at -20°C to -80°C. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
More Infomation

Target

Full Name
Interleukin 1 Receptor Accessory Protein
Function
Coreceptor for IL1RL2 in the IL-36 signaling system (By similarity).

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 (By similarity).

May play a role in IL1B-mediated costimulation of IFNG production from T-helper 1 (Th1) cells (Probable).

Isoform 2:
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 (PubMed:12530978).

Enhances the ability of secreted IL1R1 to inhibit IL-33 signaling (By similarity).

Isoform 4:
Unable to mediate canonical IL-1 signaling (PubMed:19481478).

Required for Src phosphorylation by IL1B. May be involved in IL1B-potentiated NMDA-induced calcium influx in neurons (By similarity).
Biological Process
Immune response Source: ProtInc
Inflammatory response Source: ProtInc
Innate immune response Source: UniProtKB-KW
Positive regulation of interleukin-13 production Source: Ensembl
Positive regulation of interleukin-4 production Source: Ensembl
Positive regulation of interleukin-5 production Source: Ensembl
Positive regulation of interleukin-6 production Source: Ensembl
Positive regulation of NF-kappaB transcription factor activity Source: GO_Central
Positive regulation of synapse assembly Source: UniProtKB
Protein-containing complex assembly Source: ProtInc
Regulation of postsynaptic density assembly Source: Ensembl
Regulation of presynapse assembly Source: Ensembl
Synaptic membrane adhesion Source: Ensembl
Trans-synaptic signaling by trans-synaptic complex Source: Ensembl
Cellular Location
Isoform 1: Cell membrane
Isoform 2&3: Secreted
Topology
Extracellular: 21-367
Helical: 368-388
Cytoplasmic: 389-570

Badi, Y. E., Salcman, B., Taylor, A., Rana, B., Kermani, N. Z., Riley, J. H., ... & Adcock, I. M. (2023). IL1RAP expression and the enrichment of IL‐33 activation signatures in severe neutrophilic asthma. Allergy, 78(1), 156-167.

Zou, H., & Mao, Q. (2022). Circ_0037078 promotes trophoblast cell proliferation, migration, invasion and angiogenesis by miR‐576‐5p/IL1RAP axis. American Journal of Reproductive Immunology, 87(1), e13507.

Zhang, H. F., Hughes, C. S., Li, W., He, J. Z., Surdez, D., El-Naggar, A. M., ... & Sorensen, P. H. (2021). Proteomic screens for suppressors of anoikis identify IL1RAP as a promising surface target in Ewing sarcoma. Cancer discovery, 11(11), 2884-2903.

Lv, Q., Xia, Q., Li, A., & Wang, Z. (2021). The potential role of IL1RAP on tumor microenvironment-related inflammatory factors in stomach adenocarcinoma. Technology in Cancer Research & Treatment, 20, 1533033821995282.

De Boer, B., Sheveleva, S., Apelt, K., Vellenga, E., Mulder, A. B., Huls, G., & Schuringa, J. J. (2021). The IL1-IL1RAP axis plays an important role in the inflammatory leukemic niche that favors acute myeloid leukemia proliferation over normal hematopoiesis. haematologica, 106(12), 3067.

Wang, N., Li, R., & Xue, M. (2019). Potential regulatory network in the PSG10P/miR‐19a‐3p/IL1RAP pathway is possibly involved in preeclampsia pathogenesis. Journal of cellular and molecular medicine, 23(2), 852-864.

Warda, W., Larosa, F., Neto Da Rocha, M., Trad, R., Deconinck, E., Fajloun, Z., ... & Ferrand, C. (2019). CML hematopoietic stem cells expressing IL1RAP can be targeted by chimeric antigen receptor–engineered T cells. Cancer Research, 79(3), 663-675.

Mitchell, K., Barreyro, L., Todorova, T. I., Taylor, S. J., Antony-Debré, I., Narayanagari, S. R., ... & Steidl, U. (2018). IL1RAP potentiates multiple oncogenic signaling pathways in AML. Journal of Experimental Medicine, 215(6), 1709-1727.

Zhao, X., Bai, X., Guan, L., Li, J., Song, X., Ma, X., ... & Tong, D. (2018). microRNA-4331 promotes transmissible gastroenteritis virus (TGEV)-induced mitochondrial damage via targeting RB1, upregulating interleukin-1 receptor accessory protein (IL1RAP), and activating p38 MAPK pathway in vitro. Molecular & Cellular Proteomics, 17(2), 190-204.

Liu, F., Dai, M., Xu, Q., Zhu, X., Zhou, Y., Jiang, S., ... & Teng, Y. (2018). SRSF10-mediated IL1RAP alternative splicing regulates cervical cancer oncogenesis via mIL1RAP-NF-κB-CD47 axis. Oncogene, 37(18), 2394-2409.

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For research use only. Not intended for any clinical use.

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