Recombinant Human IL-1 RAcP/IL-1R3 ST2/IL-33R Fc Protein, CF

When Recombinant Human IL-1 RAcP/IL-1R3 ST2/IL-33R Fc Chimera Protein (Catalog # 11268-CP) is immobilized at 1 µg/mL (100 µL/well), Recombinant Human IL‑33 (3625-IL) binds with an ED50 of 2.50-25.0 ng/mL.

2 μg/lane of Recombinant Human IL-1 RAcP/IL-1 R3 ST2/IL-33R Fc Chimera Protein (Catalog # 11268-CP) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing bands at 130-144 kDa.

• Applications: Bioactivity
• Format: Carrier-Free

Recombinant Human IL-1 RAcP/IL-1R3 ST2/IL-33R Fc Protein, CF Summary

• Details of Functionality: Measured by its binding ability in a functional ELISA. When Recombinant Human IL-1 RAcP/IL-1 R3 ST2/IL-33R Fc Chimera (Catalog # 11268-CP) is immobilized at 1 µg/mL (100 µL/well), Recombinant Human IL-33 (Catalog # 3625-IL) binds with an ED₅₀ of 2.50-25.0 ng/mL.
• Source: Chinese Hamster Ovary cell line, CHO-derived human IL-1 RAcP/IL-1 R3 protein
  

  Human IL-1 RAcP/IL-1 R3 (Ser21-Glu359) Accession # Q9NPH3.2	Human ST2/IL-33R (Lys19-Ser328) Accession # Q01638.4	IEGRMD	Human IgG1 (Pro100-Lys330)
  N-terminus			C-terminus

• Accession #: Q9NPH3.2 & Q01638.4
• N-terminal Sequence: Ser21
• 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: 102 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: 130-144 kDa, under reducing conditons.

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 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-1 RAcP/IL-1R3 ST2/IL-33R Fc Protein, CF

• C3orf13IL-1RAcPIL1R3Interleukin-1 receptor 3
• FLJ37788
• IL-1 R3
• IL-1 RAcP
• IL-1 receptor accessory protein
• IL-1R3
• IL-1R-3
• IL1RAcP
• IL-1RAcP
• IL1RAP
• interleukin 1 receptor accessory protein
• interleukin-1 receptor accessory protein beta
• interleukin-1 receptor accessory protein

Background

Serum stimulation-2 (ST2), also known as IL-1RL1, heterodimerizes with IL1-R3, also referred to as IL-1RAP, IL-1R3, or C3orf13, after binding IL-33 (1). The 556 aa human ST2 contains an 18 aa signal peptide sequence, 310 amino acid (aa) extracellular domain, 21 aa transmembrane region, and 207 cytoplasmic domain. ST2 contains three extracellular IgG domains and an intracellular TIR domain. The 570 aa human 1L-1R3 contains a 20 aa signal peptide sequence, 347 aa extracellular domain, 21 aa transmembrane region, and 182 cytoplasmic domain. Differential promoter binding of ST2 generates two main splice variants, a membrane-bound receptor (ST2) expressed on cardiomyocytes and a variety of immune cells that promotes NF-kappa B signaling and a soluble form (sST2) that prevents its signaling, which can be produced spontaneously by lung, kidney, heart, and small intestine cells or by activated mast cells and TH2 cells (2). Two less well understood ST2 splice variants include ST2V, expressed highly in gastrointestinal organs (3), and ST2LV, secreted by eye, heart, lung, and liver tissues (4). Within the ECD, human ST2 shares 68% and 64% aa sequence identity with mouse and rat ST2, and human 1L-1R3 has 86% and 94% aa sequence identity with mouse and rat IL-1R3. After ST2 binds to IL-33 and heterodimerization with IL-1R3, the TIR domain can be activated by MyD88 and IL-1R-associated kinase activation to activate MAPK or NF-kappa B pathways (1). While the mechanisms/signals are unclear, TRAF6 is required for NF-kappa B but not for MAPK activation (5). ST2 participates in a variety of disease implications, especially with its association with immune cells. For example, IL-33 signaling through ST2 is involved with lung diseases in allergic asthma (6), both participating in inflammation but also in its maintenance (7). With skin diseases, upregulation of ST2 and IL-33 has been observed with atopic dermatitis (8), psoriasis (9), and vitiligo (10).

1. Chackerian, A.A. et al. (2007) J. Immunol. 179:2551.
2. Bergers, G. et al. (1994) EMBO. J. 13:1176.
3. Tago, K. et al. (2001) 285:1377.
4. Hiroyuki, I. et al. (2004) Biochim. Biophys. Acta. 24:1.
5. Funakoshi-Tago, M. et al. (2008) Cell. Signal. 20:1679.
6. Kearley, J. et al. (2009) Am. J. Respir. Crit. Care. Med. 179:772.
7. Coyle, A.J. et al. (1990) J. Exp. Med. 190:895.
8. Imai, Y. et al. (2013) PNANS. 110:13921.
9. Hueber, A.J. et al. (2011) Eur. J. Immunol. 41:2229.
10. Li, P. et al. (2015) Clin. Exp. Dermatol. 40:163.

Bioinformatics

• Uniprot:
  • Q9NPH3.2 & Q01638.4()