Recombinant Human IL-33 Biotinylated Protein, CF

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.

• Reactivity: Hu
• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Human IL-33 Biotinylated Protein, CF Summary

• Additional Information: Biotinylated
• Details of Functionality: Measured by its binding ability in a functional ELISA. When Recombinant Human ST2/IL-33R Fc Chimera (Catalog # 523-ST) is immobilized at 0.5 µg/mL (100 µL/well), Biotinylated Recombinant Human IL-33 (Catalog # BT3625) binds with an ED₅₀ of 0.900-9.00 ng/mL.
• Source: E. coli-derived human IL-33 protein
  Ser112-Thr270
• Accession #: O95760.1
• N-terminal Sequence: Ser112
• Structure / Form: Biotinylated via amines
• Protein/Peptide Type: Recombinant Proteins
• Purity: >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Endotoxin Note: <0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

• Dilutions:
  • Bioactivity
• 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.
• SDS-PAGE: 18-22 kDa, under reducing conditions.

Packaging, Storage & Formulations

• Storage: 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.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
• Buffer: Lyophilized from a 0.2 μm filtered solution in PBS, EDTA and DTT with Trehalose.
• Purity: >95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
• Reconstitution Instructions: Reconstitute at 500 μg/mL in PBS.

Notes

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

Alternate Names for Recombinant Human IL-33 Biotinylated 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
• 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 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.

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.

Bioinformatics

• Uniprot:
  • O95760.1()