Recombinant Mouse IL-33 Protein, CF


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Recombinant Mouse IL-33 Protein, CF Summary

Details of Functionality
Measured in a cell proliferation assay using D10.G4.1 mouse helper T cells. The ED50 for this effect is 0.0125-0.05 ng/mL.
E. coli-derived mouse IL-33 protein
Accession #
N-terminal Sequence
Protein/Peptide Type
Recombinant Proteins
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.01 EU per 1 μg of the protein by the LAL method.


Theoretical MW
18 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
20 kDa, reducing conditions
Read Publications using
3626-ML/CF in the following applications:

Packaging, Storage & Formulations

Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
Lyophilized from a 0.2 μm filtered solution in PBS, EDTA and DTT.
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS.


This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Mouse IL-33 Protein, CF

  • C9orf26
  • C9orf26chromosome 9 open reading frame 26 (NF-HEV)
  • DKFZp586H0523
  • DVS27
  • DVS27-related protein
  • IL1F11
  • IL-1F11
  • IL33
  • IL-33
  • interleukin 33
  • Interleukin-1 family member 11
  • interleukin-33
  • NF-HEV
  • Nuclear factor from high endothelial venules
  • RP11-575C20.2


IL-33, also known as NF-HEV and DVS 27, is a 30 kDa proinflammatory protein that may also regulate gene transcription (1‑3). DVS 27 was identifed as a gene that is up‑regulated in vasospastic cerebral arteries (1). NF-HEV was described as a nuclear factor that is preferentially expressed in the endothelial cells of high endothelial venules relative to endothelial cells from other tissues (2). IL-33 was identified based on sequence and structural homology with IL-1 family cytokines (3). DVS 27, NF-HEV, and IL-33 share 100% amino acid sequence identity. IL-33 is constitutively expressed in smooth muscle and airway epithelia. It is up‑regulated in arterial smooth muscle, dermal fibroblasts, and keratinocytes following IL-1 alpha or IL‑1 beta stimulation (1, 3). Similar to IL-1, IL-33 can be cleaved in vitro by caspase‑1, generating an N‑terminal fragment that is slightly shorter than the C‑terminal fragment (3, 4). The N‑terminal portion of full length IL-33 contains a predicted bipartite nuclear localization sequence and a homeodomain-like helix-turn-helix DNA binding domain. By immunofluorescence, full length IL-33 localizes to the nucleus in HUVECs and transfectants (2). The C‑terminal fragment, corresponding to mature IL-33, binds and triggers signaling through mast cell IL‑1 R4/ST2L, a longtime orphan receptor involved in the augmentation of Th2 cell responses (3, 5‑7). A ternary signaling complex is formed by the subsequent association of IL-33 and ST2L with IL‑1 RAcP (8). Stimulation of Th2 polarized lymphocytes with mature IL-33 in vitro induces IL-5 and IL-13 secretion (3). In vivo administration of mature IL-33 promotes increased production of IL-5, IL-13, IgE, and IgA, as well as splenomegaly and inflammatory infiltration of mucosal tissues (3). Full length and mature mouse IL-33 share approximately 55% and 90% aa sequence identity with human and rat IL-33, respectively. Mouse IL-33 shares less than 25% aa sequence identity with other IL-1 family proteins.

  1. Onda, H. et al. (1999) J. Cereb. Blood Flow Metab. 19:1279.
  2. Baekkevold, E.S. et al. (2003) Am. J. Pathol. 163:69.
  3. Schmitz, J. et al. (2005) Immunity 23:479.
  4. Black, R.A. et al. (1989) J. Biol. Chem. 264:5323.
  5. Xu, D. et al. (1998) J. Exp. Med. 187:787.
  6. Lohning, M. et al. (1998) Proc. Natl. Acad. Sci. 95:6930.
  7. Dinarello, C.A. (2005) Immunity 23:461.
  8. Chackerian, A.A. et al. (2007) J. Immunol. 179:2551.

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Publications for IL-33 (3626-ML/CF)(78)

We have publications tested in 1 confirmed species: Mouse.

We have publications tested in 5 applications: Bioassay, Cell Culture, Flow Cytometry, In Vivo, Neutralization.

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Showing Publications 1 - 10 of 78. Show All 78 Publications.
Publications using 3626-ML/CF Applications Species
Bosteels C, Neyt K, Vanheerswynghels M, van Helden M, Sichien D, Debeuf N, De Prijck S, Bosteels V, Vandamme N, Martens L, Saeys Y, Louagie E, Lesage M, Williams D, Tang S, Mayer J, Ronchese F, Scott C, Hammad H, Guilliams M, Lambrecht B Inflammatory Type 2 cDCs Acquire Features of cDC1s and Macrophages to Orchestrate Immunity to Respiratory Virus Infection. Immunity, 0;0(0):. 0 [PMID: 32392463] (Mouse) Mouse
CL Hsu, KD Chhiba, R Krier-Burr, S Hosakoppal, S Berdnikovs, ML Miller, PJ Bryce Allergic inflammation is initiated by IL-33-dependent crosstalk between mast cells and basophils PLoS ONE, 2020;15(1):e0226701. 2020 [PMID: 31940364] (Bioassay, Mouse) Bioassay Mouse
K Ishimaru, S Nakajima, G Yu, Y Nakamura, A Nakao The Putatively Specific Synthetic REV-ERB Agonist SR9009 Inhibits IgE- and IL-33-Mediated Mast Cell Activation Independently of the Circadian Clock Int J Mol Sci, 2019;20(24):. 2019 [PMID: 31847374] (Bioassay, Mouse) Bioassay Mouse
PT Mantani, P Dunér, I Ljungcrant, J Nilsson, H Björkbacka, GN Fredrikson ILC2 transfers to apolipoprotein E deficient mice reduce the lipid content of atherosclerotic lesions BMC Immunol., 2019;20(1):47. 2019 [PMID: 31823769] (Bioassay, Mouse) Bioassay Mouse
Y Mishima, H Sonoyama, S Ishihara, N Oshima, I Moriyama, K Kawashima, Y Kinoshita Interleukin-33 delays recovery of mucosal inflammation via downregulation of homeostatic ABCG5/8 in the colon Lab. Invest., 2019;0(0):. 2019 [PMID: 31641224] (In Vivo, Mouse) In Vivo Mouse
C Morales De, JR Maxwell, MM Xu, A Menoret, P Mittal, N Tsurutani, AJ Adler, AT Vella Costimulation Induces CD4�T Cell Antitumor Immunity via an Innate-like Mechanism Cell Rep, 2019;27(5):1434-1445.e3. 2019 [PMID: 31042471] (Bioassay, Mouse) Bioassay Mouse
H Katsura, Y Kobayashi, PR Tata, BLM Hogan IL-1 and TNF? Contribute to the Inflammatory Niche to Enhance Alveolar Regeneration Stem Cell Reports, 2019;0(0):. 2019 [PMID: 30930244] (Bioassay, Mouse) Bioassay Mouse
HS Cho, A Reboldi, JA Hall, LJ Berg The Tec kinase ITK is essential for ILC2 survival and epithelial integrity in the intestine Nat Commun, 2019;10(1):784. 2019 [PMID: 30770814] (Bioassay, Mouse) Bioassay Mouse
EO Weinberg, B Ferran, Y Tsukahara, MMS Hatch, J Han, CE Murdoch, R Matsui IL-33 induction and signaling are controlled by glutaredoxin-1 in mouse macrophages PLoS ONE, 2019;14(1):e0210827. 2019 [PMID: 30682073] (Bioassay, Mouse) Bioassay Mouse
V Koliaraki, N Chalkidi, A Henriques, C Tzaferis, A Polykratis, A Waisman, W Muller, DJ Hackam, M Pasparakis, G Kollias Innate Sensing through Mesenchymal TLR4/MyD88 Signals Promotes Spontaneous Intestinal Tumorigenesis Cell Rep, 2019;26(3):536-545.e4. 2019 [PMID: 30650348] (Bioassay, Mouse) Bioassay Mouse
Show All 78 Publications.

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Interleukin 33 (IL-33) - A dual function cytokine
IL-33 is a member of the interleukin family of cytokines that regulates a wide variety of cellular functions. Its receptor is ST2, an IL-1 receptor family member that also acts as a negative regulator of TLR-IL-1R signaling and the IL-1R accessory...  Read full blog post.

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Gene Symbol Il33