IL-33 Antibody (390412)

Over-expression and inhibition of miR-378a-3p modulate IL-33 expression. Stable expression of miR-378a-3p (Primir-378) or inhibition of miR-378a-3p (Inhibitor), and their respective controls (CTR PrimiR-378a, CTR Inhibitor) were obtained with Lentiviral vectors in HT-29 cells. (A) MiR-378a-3p Log2 fold change, and (B) IL-33 mRNA fold change relative to CTR cell lines by qPCR, (C) IL-33 protein and beta -actin by Western Blotting (WB) and bands quantification by densitometry analysis (Fiji Software) of Control Primir-378 and Primir-378 cell lines, and (D) Control Inhibitor and Inhibitor cell lines. Four experiments by duplicated were performed. Each cell line was compared with their respective control using Paired t-test. *P = < 0.05, **P = < 0.01, ***P = < 0.001. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/31824476), licensed under a CC-BY license. Not internally tested by R&D Systems.

Over-expression and inhibition of miR-378a-3p modulate IL-33 expression. Stable expression of miR-378a-3p (Primir-378) or inhibition of miR-378a-3p (Inhibitor), and their respective controls (CTR PrimiR-378a, CTR Inhibitor) were obtained with Lentiviral vectors in HT-29 cells. (A) MiR-378a-3p Log2 fold change, and (B) IL-33 mRNA fold change relative to CTR cell lines by qPCR, (C) IL-33 protein and beta -actin by Western Blotting (WB) and bands quantification by densitometry analysis (Fiji Software) of Control Primir-378 and Primir-378 cell lines, and (D) Control Inhibitor and Inhibitor cell lines. Four experiments by duplicated were performed. Each cell line was compared with their respective control using Paired t-test. *P = < 0.05, **P = < 0.01, ***P = < 0.001. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/31824476), licensed under a CC-BY license. Not internally tested by R&D Systems.

TNF alpha decreases miR-378a-3p and increases IL-33 expression in colonocytes. HT-29 cell line was stimulated with 10 ng/mL human recombinant TNF alpha (hr-TNF alpha ) for 3, 6, and 24 h. Fold change relative to non-stimulated control of (A) MiR-378a-3p and (B) IL-33 mRNA. (C) IL-33 protein was measured in HT-29 cells stimulated with hr-TNF alpha 10 ng/mL 12, 24, and 48 h by WB, (D) Band quantification of IL-33 protein normalized to beta -actin. (E) Fold change relative to non-stimulated control of PPARGC1B mRNA and (F) IL-8 mRNA levels (measured as control of TNF alpha stimulus). (G) AGO1 and (H) AGO2 mRNA levels were assessed as control of miRNA-biogenesis machinery. Four experiments by duplicated were analyzed using Two-way ANOVA with Bonferroni post-test. *P < 0.05, **P = < 0.01. Image collected and cropped by CiteAb from the following open publication (//pubmed.ncbi.nlm.nih.gov/31824476), licensed under a CC-BY license. Not internally tested by R&D Systems.

• Reactivity: Hu
• Applications: WB, ICC/IF
• Clone: 390412
• Clonality: Monoclonal
• Host: Rat
• Conjugate: Unconjugated
• Concentration: LYOPH

IL-33 Antibody (390412) Summary

• Immunogen: E. coli-derived recombinant human IL-33
  Ser112-Thr270
  Accession # O95760
• Specificity: Detects human IL-33 in direct ELISAs and Western blots. In direct ELISAs and Western blots, no cross-reactivity with recombinant mouse IL-33 is observed.
• Source: N/A
• Isotype: IgG2b
• Clonality: Monoclonal
• Host: Rat
• Gene: IL33
• Purity Statement: Protein A or G purified from hybridoma culture supernatant

Applications/Dilutions

• Dilutions:
  • Immunocytochemistry 8-25 ug/mL
  • Western Blot 1 ug/mL

Packaging, Storage & Formulations

• Storage: Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  12 months from date of receipt, -20 to -70 degreesC as supplied. 1 month, 2 to 8 degreesC under sterile conditions after reconstitution. 6 months, -20 to -70 degreesC under sterile conditions after reconstitution.
• Buffer: Lyophilized from a 0.2 μm filtered solution in PBS with Trehalose. *Small pack size (SP) is supplied either lyophilized or as a 0.2 µm filtered solution in PBS.
• Preservative: No Preservative
• Concentration: LYOPH
• Reconstitution Instructions: Reconstitute at 0.5 mg/mL in sterile PBS.

Notes

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

Alternate Names for IL-33 Antibody (390412)

• 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
• NFHEV
• NF-HEV
• NF-HEVNFEHEV
• Nuclear factor from high endothelial venules
• RP11-575C20.2

Background

IL-33, also known as NF-HEV and DVS 27, is a proinflammatory protein that may also regulate gene transcription (1-3). DVS 27 was identifed as a gene that is upregulated 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). IL-33 is constitutively expressed in smooth muscle and airway epithelia. It is upregulated 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 32 kDa 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 18 kDa fragment, corresponding to mature IL-33, binds and triggers signaling through mast cell IL-1 R4/ST2, a 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 ST2 with IL-1R AcP (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 human IL-33 share 52-58% aa sequence identity with mouse and rat IL-33. Human IL-33 shares less than 20% 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. USA 95:6930.
7. Dinarello, C.A. (2005) Immunity 23:461.
8. Chackerian, A.A. et al. (2007) J. Immunol. 179:2551.

Limitations

This product is for research use only and is not approved for use in humans or in clinical diagnosis. Primary Antibodies are guaranteed for 1 year from date of receipt.

Publications for IL-33 Antibody (MAB3625)(2)

Publications using MAB3625

• Leite-Silva, J;Oliveira-Ribeiro, C;Morgado, FN;Pimentel, MIF;Lyra, MR;Fagundes, A;Miranda, LFC;Valete-Rosalino, CM;Schubach, AO;Conceição-Silva, F; Is There Any Difference in the In Situ Immune Response in Active Localized Cutaneous Leishmaniasis That Respond Well or Poorly to Meglumine Antimoniate Treatment or Spontaneously Heal? Microorganisms 2023-06-22 [PMID: 37512804] (IHC, Human)
• Kurowska-Stolarska M, Kewin P, Murphy G, Russo RC, Stolarski B, Garcia CC, Komai-Koma M, Pitman N, Li Y, McKenzie AN, Teixeira MM, Liew FY, Xu D IL-33 induces antigen-specific IL-5+ T cells and promotes allergic-induced airway inflammation independent of IL-4. J. Immunol., 2008-10-01;181(7):4780-90. 2008-10-01 [PMID: 18802081] (Flow Cytometry, Human)

Bioinformatics

• Gene Symbol: IL33
• Uniprot:
  • O95760()