Recombinant Macaca fascicularis Interleukin 1 receptor accessory protein(IL1RAP), partial (Active)

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Code CSB-MP5268MOV
Abbreviation Recombinant Cynomolgus monkey IL1RAP protein, partial (Active)
MSDS
Size $90
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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 Macaca fascicularis IL1RAP at 2 μg/ml can bind Anti-IL1RAP recombinant antibody (CSB-RA878844MA1HU). The EC50 is 0.9099-1.181 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 Macaca fascicularis IL1RAP at 2 μg/mL can bind Anti-IL1RAP recombinant antibody (CSB-RA878844MA1HU). The EC50 is 0.9099-1.181 ng/mL.
Target Names
Uniprot No.
Species
Macaca fascicularis (Crab-eating macaque) (Cynomolgus monkey)
Source
Mammalian cell
Expression Region
21-359aa
Target Protein Sequence
SERCDDWGLDTMRQIQVFEDEPARIKCPLFEHFLKFNYSTAHSAGLTLIWYWTRQDRDLEEPINFRLPENRISKEKDVLWFRPTLLNDTGNYTCMLRNTTYCSKVAFPLEVVQKDSCFNSPMKLPVHKLYIEYGIQRITCPNVDGYFPSSVKPTITWYMGCYKIQNFNNVIPEGMNLSFLIAFISNNGNYTCVVTYPENGRTFHLTRTLTVKVVGSPKNAVPPVIHSPNDHVVYEKEPGEELLIPCTVYFSFLMDSRNEVWWTIDGKKPDDIPIDVTINESISHSRTEDETRTQILSIKKVTSEDLKRSYVCHARSAKGEVAKAATVKQKVPAPRYTVE
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 Macaca fascicularis IL1RAP protein is a functionally active construct produced in mammalian cells, ensuring accurate protein folding and post-translational modifications. It includes amino acids 21 to 359 of the native IL1RAP sequence and is fused with a C-terminal 10xHis tag to facilitate purification and downstream applications. Supplied as a lyophilized powder, the recombinant IL1RAP protein meets high purity standards, exceeding 95% as determined by both SDS-PAGE and SEC-HPLC. Endotoxin levels are maintained below 1.0 EU/µg, confirmed by LAL testing, making it suitable for use in sensitive biological assays. Functional validation was performed via ELISA, where the immobilized protein at 2 μg/mL binds specifically to the anti-IL1RAP recombinant antibody (CSB-RA878844MA1HU), with an EC50 ranging from 0.9099 to 1.181 ng/mL. This confirms its strong bioactivity and utility in immunological or receptor-binding research contexts.

The IL1RAP is a crucial component in the signaling pathways mediated by the IL-1 family of cytokines. In Macaca fascicularis, as well as other mammals, IL1RAP is essential for the formation of functional IL-1 receptor complexes that initiate pro-inflammatory signaling cascades critical for various physiological and pathological processes.

IL-1, particularly IL-1β, exerts its effects by binding to IL-1R1, which subsequently recruits IL1RAP to form a heterodimeric receptor complex. This assembly activates intracellular signaling pathways, including those involving NF-κB and MAPK (Mitogen-Activated Protein Kinase) pathways, necessary for the expression of inflammatory molecules and the modulation of immune responses [1][2]. Research indicates that IL1RAP is indispensable for the effective transduction of IL-1 signaling, as it aids in receptor dimerization and the recruitment of downstream signaling proteins like MyD88 and IL-1 receptor-associated kinases [1][3].

Moreover, studies have highlighted IL1RAP's role in macrophage activation and inflammation, where it influences cytokine production in response to infections. For instance, IL1RAP is involved in the inflammatory response to pathogens such as Burkholderia mallei, as observed in profiling studies using serum from infected Macaca fascicularis [4]. Furthermore, there is evidence suggesting that manipulation of IL1RAP expression can significantly alter immune responses, indicating its potential as a therapeutic target for inflammatory diseases [5][6].

In addition, its evolutionary conservation across different primate species points to its fundamental biological importance, particularly in the context of immune responses and disease models. The interaction between IL-1β and its receptor complex, including IL1RAP, has implications for various health conditions, including periodontal disease, where the upregulation of IL-1 signaling is associated with tissue inflammation and degradation [7][8].

References:
[1] J. Markovics, J. Araya, et al. Interleukin-1β induces increased transcriptional activation of the transforming growth factor-β-activating integrin subunit β8 through altering chromatin architecture. Journal of Biological Chemistry, vol. 286, no. 42, p. 36864-36874, 2011. https://doi.org/10.1074/jbc.m111.276790
[2] S. Lavalette, W. Raoul, et al. Interleukin-1β inhibition prevents choroidal neovascularization and does not exacerbate photoreceptor degeneration. American Journal of Pathology, vol. 178, no. 5, p. 2416-2423, 2011. https://doi.org/10.1016/j.ajpath.2011.01.013
[3] И. Кутырев, B. Cleveland, T. Leeds, & G. Wiens. Proinflammatory cytokine and cytokine receptor gene expression kinetics following challenge with flavobacterium psychrophilum in resistant and susceptible lines of rainbow trout (oncorhynchus mykiss). Fish & Shellfish Immunology, vol. 58, p. 542-553, 2016. https://doi.org/10.1016/j.fsi.2016.09.053
[4] T. Glaros, C. Blancett, T. Bell, M. Natesan, & R. Ulrich. Serum biomarkers of burkholderia mallei infection elucidated by proteomic imaging of skin and lung abscesses. Clinical Proteomics, vol. 12, no. 1, 2015. https://doi.org/10.1186/s12014-015-9079-4
[5] M. Heuvel, L. Scholtens, E. Turk, D. Mantini, W. Vanduffel, & L. Barrett. Multimodal analysis of cortical chemoarchitecture and macroscale fmri resting‐state functional connectivity. Human Brain Mapping, vol. 37, no. 9, p. 3103-3113, 2016. https://doi.org/10.1002/hbm.23229
[6] S. Sugawara, R. Reeves, & S. Jost. Learning to be elite: lessons from hiv-1 controllers and animal models on trained innate immunity and virus suppression. Frontiers in Immunology, vol. 13, 2022. https://doi.org/10.3389/fimmu.2022.858383
[7] Y. Shimazaki, Y. Egami, et al. Relationship between obesity and physical fitness and periodontitis. Journal of Periodontology, vol. 81, no. 8, p. 1124-1131, 2010. https://doi.org/10.1902/jop.2010.100017
[8] N. Hengartner, J. Fiedler, A. Ignatius, & R. Brenner. Il-1β inhibits human osteoblast migration. Molecular Medicine, vol. 19, no. 1, p. 36-42, 2013. https://doi.org/10.2119/molmed.2012.00058

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