Human IL-33 PE-conjugated Antibody Summary
Ser112-Thr270
Accession # O95760
Applications
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Scientific Data
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Detection of IL-33 in Human Peripheral Blood Lymphocytes by Flow Cytometry. Human peripheral blood lymphocytes were stained with (A) Goat Anti-Human IL-33 PE-conjugated Monoclonal Antibody (Catalog # IC36253P) or (B) Goat IgG PE-conjugated control antibody (Catalog # IC108P) and Mouse anti-Human CD19 APC-conjugated Monoclonal Antibody (Catalog # FAB4867A). To facilitate intracellular staining, cells were fixed with Flow Cytometry Fixation Buffer (Catalog # FC004) and permeabilized with methanol.
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Detection of IL-33 in HUVECs by Flow Cytometry. HUVECs were stained with Goat Anti-Human IL-33 PE-conjugated Monoclonal Antibody (Catalog # IC36253P, filled histogram) or Goat IgG PE-conjugated control antibody (IC108P, open histogram). To facilitate intracellular staining, cells were fixed with Flow Cytometry Fixation Buffer (FC004) and permeabilized with methanol.
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Preparation and Storage
- 12 months from date of receipt, 2 to 8 °C as supplied.
Background: IL-33
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-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.
- Onda, H. et al. (1999) J. Cereb. Blood Flow Metab. 19:1279.
- Baekkevold, E.S. et al. (2003) Am. J. Pathol. 163:69.
- Schmitz, J. et al. (2005) Immunity 23:479.
- Black, R.A. et al. (1989) J. Biol. Chem. 264:5323.
- Xu, D. et al. (1998) J. Exp. Med. 187:787.
- Lohning, M. et al. (1998) Proc. Natl. Acad. Sci. USA 95:6930.
- Dinarello, C.A. (2005) Immunity 23:461.
- Chackerian, A.A. et al. (2007) J. Immunol. 179:2551.
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