Recombinant Mouse IL-33 (carrier-free)

Pricing & Availability
Regulatory Status
RUO
Other Names
Il-1f11, Nuclear factor from high endothelial venules (NF-HEV)
a_IL-33_Mouse_Recombinant_Protein_BA_051818
Mouse IL-33 induces the proliferation of D10.G4.1 mouse T lymphocytes in a dose dependent manner.
  • a_IL-33_Mouse_Recombinant_Protein_BA_051818
    Mouse IL-33 induces the proliferation of D10.G4.1 mouse T lymphocytes in a dose dependent manner.
  • b_rm_IL-33_050109
    IL-5 induction by mouse IL-33 in splenocytes activated by anti-CD3 and anti-CD28. Data kindly provided Dr. Foo Y. Liew.
  • c_IL33_Mouse_Recombinant_Protein_BA_3_020923
    Recombinant mouse IL‐33 induces proliferation in murine helper T lymphocyte (Th‐2) D10.G4.1 cells in a dose dependent manner. BioLegend’s product was compared side‐by‐side to the leading competitor's equivalent product.
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580502 10 µg $206.00
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580504 25 µg $382.00
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580506 100 µg $938.00
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580508 500 µg $2578.00
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Description

IL-33 belongs to the IL-1 family and is closely related in structure to IL-18 and IL-1b. IL-33, IL-1b, and IL-18 are synthesized as biologically inactive precursor and are cleaved by the enzyme caspase-1 to be secreted as active mature forms. IL-33 stimulates target cells by binding to the IL-1R/TLR superfamily member ST2 and subsequently activates NF-κB and MAPK pathways via identical signalling events to those observed for IL-1b. In addition, IL-33 is a nuclear factor (NF-HEV) abundantly expressed in high endothelial venules from lymphoid organs that associates with chromatin and exhibits transcriptional regulatory properties.

Technical data sheet

Product Details

Source
Mouse IL-33, amino acids Ser109-Ile266 (Accession# AAH03847.1) was expressed in E. coli.
Molecular Mass
The 158 amino acid recombinant protein has a predicted molecular mass of approximately 17,554 Da. The DTT-reduced and non-reduced protein migrate at approximately 20 kDa by SDS-PAGE. The N-terminal amino acid is Serine.
Purity
Purity is > 98%, as determined by Coomassie stained SDS-PAGE.
Formulation
0.22 µm filtered protein solution is in 20 mM HEPES, 150 mM NaCl, pH 7.2, 10 mM TCEP.
Endotoxin Level
Endotoxin level is < 0.1 EU/µg (< 0.01ng/µg) protein as determined by the LAL method.
Concentration
10 and 25 µg sizes are bottled at 200 µg/mL. 100 µg size and larger sizes are lot-specific and bottled at the concentration indicated on the vial. To obtain lot-specific concentration and expiration, please enter the lot number in our Certificate of Analysis online tool.
Storage & Handling
Unopened vial can be stored between 2°C and 8°C for up to 2 weeks, at -20°C for up to six months, or at -70°C or colder until the expiration date. For maximum results, quick spin vial prior to opening. The protein can be aliquoted and stored at -20°C or colder. Stock solutions can also be prepared at 50 - 100 µg/mL in appropriate sterile buffer, carrier protein such as 0.2 - 1% BSA or HSA can be added when preparing the stock solution. Aliquots can be stored between 2°C and 8°C for up to one week and stored at -20°C or colder for up to 3 months. Avoid repeated freeze/thaw cycles.
Activity
ED50 = 0.0125 - 0.0625 ng/ml determined by the dose dependent stimulation of D10.G4.1 cell proliferation.
Application

Bioassay

Application Notes

BioLegend carrier-free recombinant proteins provided in liquid format are shipped on blue-ice. Our comparison testing data indicates that when handled and stored as recommended, the liquid format has equal or better stability and shelf-life compared to commercially available lyophilized proteins after reconstitution. Our liquid proteins are verified in-house to maintain activity after shipping on blue ice and are backed by our 100% satisfaction guarantee. If you have any concerns, contact us at tech@biolegend.com.

Application References

(PubMed link indicates BioLegend citation)
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  3. Barlow JL, et al. 2012. J Allergy Clin Immunol. 129:191. PubMed
  4. Rosen MJ, et al. 2013. J. Immunol. 190:1849. PubMed
Product Citations
  1. He D, et al. 2022. Immunity. 55:159. PubMed
  2. Slusarczyk P, et al. 2023. Elife. 12: . PubMed
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  5. Jowett GM, et al. 2022. Cell Rep. 40:111281. PubMed
  6. Dai C, et al. 2023. Clin Cosmet Investig Dermatol. 16:639. PubMed
  7. Burganova G, et al. 2023. Front Endocrinol (Lausanne). 14:1142988. PubMed
  8. Sun X, et al. 2023. Cell Death Dis. 14:242. PubMed
  9. Zheng P, et al. 2023. Stroke Vasc Neurol. . PubMed
  10. Frisbee AL, et al. 2019. Nat Commun. 10:2712. PubMed
  11. Bielecki P, et al. 2021. Nature. 592:128. PubMed
  12. Billroth-MacLurg, AC, et al. 2016. J Immunol. 197:2208-2218. PubMed
  13. Caslin H, et al. 2017. Cell Immunol. 10.1016/j.cellimm.2017.04.013. PubMed
  14. Boothby IC, et al. 2021. Nature. 599:667. PubMed
  15. Kenswil KJG, et al. 2018. Cell Rep. 22:666. PubMed
  16. Kienzl M, et al. 2020. Oncoimmunology. 9:1776059. PubMed
  17. Gao Y, et al. 2020. Front Neurosci. 1.206944444. PubMed
  18. Camacho DF, et al. 2022. JCI Insight. 7:. PubMed
  19. Dépis F, et al. 2016. Proc Natl Acad Sci U S A. 113: 1345 - 1350. PubMed
  20. Barlow J, et al. 2012. J Allergy Clin Immunol. 129:151. PubMed
  21. Hurrell BP, et al. 2019. Cell Rep. 29:4509. PubMed
  22. Nakajima T, et al. 2021. J Exp Med. 218:. PubMed
  23. Bremser A, et al. 2015. PLoS One. 10: 0137393. PubMed
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  25. Meiners J, et al. 2020. PLoS Pathog. 16:e1009121. PubMed
  26. Gomez-Rodriguez J, et al. 2016. Nat Commun. 7:10857. PubMed
  27. Miller A, et al. 2010. Circ Res. 107:650. PubMed
  28. Li C, et al. 2021. Cell Metabolism. 33(8):1610-1623.e5. PubMed
  29. Galle-Treger L, et al. 2016. Nat Commun. 7:13202. PubMed
  30. Li A, et al. 2019. Cell Rep. 29:2998. PubMed
  31. Miller JE, et al. 2021. JCI Insight. 6:. PubMed
  32. Zeis P, et al. 2020. Immunity. 53:775. PubMed
  33. Fu A, et al. 2016. Proc Natl Acad Sci U S A. 113: 2705 - 2713. PubMed
  34. Lu Y, et al. 2020. Immunity. 52:782. PubMed
  35. Mattei F, et al. 2022. iScience. 25:105110. PubMed
  36. Fujimoto M, et al. 2022. Nat Commun. 13:5408. PubMed
  37. Xu L, et al. 2022. Nat Commun. 13:6881. PubMed
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Antigen Details

Distribution

High levels of mouse IL-33 mRNA are detected in the stomach, lung, spinal cord, brain, and skin. Expression within these organs is restricted to a few cell types, such as epithelial cells, fibroblasts, and smooth muscle cells. In addition, mouse IL-33 mRNA is found in resting dendritic cells and activated macrophages. Endothelial cells constitute a major source of IL-33 mRNA in chronically inflamed tissues.

Function
IL-33 drives production of Th2-associated cytokines from in vitro polarized Th2 cells. In mice, IL-33 injection induced the expression of IL-4, IL-5, and IL-13 and led to severe pathological changes in the lung and the digestive tract. In addition, IL-33 acts as a chemoattractant for Th2 cells, both in vitro and in vivo. TNF-α and IL-1β are activators of IL-33 transcription in fibroblasts and keratinocytes.
Ligand/Receptor
IL-33 binds to the IL-1 family receptor T1/ST2 and IL-1RAcP (IL-1 receptor associated protein)
Biology Area
Cell Biology, Immunology, Stem Cells
Molecular Family
Cytokines/Chemokines
Antigen References

1. Schmitz J, et al. Immunity 2005 23:479-490.
2. Barksby HE, et al. C Exp Immunol 2007 149:217-225.
3. Arend WP, et al. ImmRev 2008 223:20-38.
4. Suzukawa M, et al. J. Immunol. 2008 181:5981-5989.
5. Moussio C, et al. PlosOne 2008 10:e3331.

Gene ID
77125 View all products for this Gene ID
UniProt
View information about IL-33 on UniProt.org
Go To Top Version: 9    Revision Date: 02/09/2023

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