Recombinant Human IL-33 Biotinylated Protein, CF Summary
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CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
|Formulation||Lyophilized from a 0.2 μm filtered solution in PBS, EDTA and DTT with Trehalose.|
|Reconstitution||Reconstitute at 500 μg/mL in PBS.|
|Shipping||The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
When Recombinant Human ST2/IL-33R Fc Chimera Protein (523-ST) is immobilized at 0.5 µg/mL (100 µL/well), Biotinylated Recombinant Human IL‑33 Protein (Catalog # BT3625) binds with an ED50 of 0.900-9.00 ng/mL.
2 μg/lane of Recombinant Human IL-33 Biotinylated Protein (Catalog # BT3625) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 18-22 kDa.
IL-33, also known as NF-HEV and DVS 27, is a 30-kDa proinflammatory protein that was identified based on sequence and structural homology with IL‑1 family cytokines (1-3). IL‑33 is constitutively expressed in smooth muscle and airway epithelia and 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). Mature human IL‑33 shares 52‑58% aa sequence identity with mouse and rat IL‑33 and 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. 95:6930.
- Dinarello, C.A. (2005) Immunity 23:461.
- Chackerian, A.A. et al. (2007) J. Immunol. 179:2551.
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