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Recombinant Human ST2/IL-33R Fc Chimera Avi-tag Protein, CF

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When Recombinant Human IL-33 (3625-IL) is immobilized at 2 µg/mL (100 µL/well), Biotinylated Recombinant Human ST2/IL-33R Fc Chimera Avi-tag Protein (Catalog # AVI11066) binds with an ED50 of 90.0-720 ng/mL.
When Recombinant Human IL-33 (3625-IL) is immobilized at 2 µg/mL (100 µL/well), Biotinylated Recombinant Human ST2/IL-33R Fc Chimera Avi-tag Protein (Catalog # AVI11066) binds with an ED50 of 90.0-720 ng/mL.
2 μg/lane of Biotinylated Recombinant Human ST2/IL-33R Fc Chimera Avi-tag Protein (Catalog # AVI11066) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® ...read more

Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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Recombinant Human ST2/IL-33R Fc Chimera Avi-tag Protein, CF Summary

Additional Information
Biotinylated
Details of Functionality

When Recombinant Human IL-33  (Catalog # 3625-IL) is immobilized at 2 µg/mL (100 µL/well), Biotinylated Recombinant Human ST2/IL-33R Fc Chimera Avi-tag (Catalog # AVI11066) binds with an ED50 of 90.0-720 ng/mL.
Source
Chinese Hamster Ovary cell line, CHO-derived human ST2/IL-33R protein
Human ST-2
(Lys19-Ser328)
Accession # Q01638.4		IEGRMDHuman IgG1
(Pro100-Lys330)		Avi-tag
N-terminusC-terminus
Accession #
N-terminal Sequence
Lys19
Structure / Form
Covalent homo-dimer
Biotinylated via Avi-tag
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
63 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
90-105 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 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 ST2/IL-33R Fc Chimera Avi-tag Protein, CF

  • DER4
  • DER4ST2growth stimulation-expressed
  • Fit-1
  • IL-1 R4
  • IL1R4
  • IL-1R4
  • IL-1RL1
  • IL-33 R
  • IL33R
  • IL-33R
  • interleukin 1 receptor-like 1
  • interleukin 1 receptor-related protein
  • interleukin-1 receptor-like 1
  • Ly84
  • MGC32623
  • Protein ST2
  • ST2
  • ST2L
  • ST2V
  • T1
  • T1homolog of mouse growth stimulation-expressed

Background

Serum stimulation-2 (ST2), also known as Interleukin receptor like-1 (IL1RL1) and T1, is a member of the Interleukin-1 receptor superfamily family glycoprotein that contributes to Th2 immune responses (1, 2). Human ST2 consists of an extracellular domain (ECD) with three Ig-like domains, a transmembrane segment, and a cytoplasmic domain with an intracellular Toll/interleukin-1 receptor (TIR) domain (3, 4). Within the ECD, human ST2 shares 68% and 64% amino acid sequence identity with mouse and rat ST2, respectively. Alternate splicing of human ST2 generates a soluble isoform that lacks the transmembrane and cytoplasmic regions as well as an isoform that additionally lacks the third Ig‑like domain (4). ST2 is expressed on the surface of mast cells, activated Th2 cells, macrophages, and cardiac myocytes (5-8). It binds IL33, a cytokine that is upregulated by inflammation or mechanical strain in smooth muscle cells, airway epithelia, keratinocytes, and cardiac fibroblasts (5, 9). IL-33 binding induces the association of ST2 with IL1R AcP, a shared signaling subunit that also associates with IL1RI and IL1R rp2 (1, 10, 11). In macrophages, ST2 interferes with signaling from IL1RI and TLR4 by sequestering the adaptor proteins MyD88 and Mal (7). In addition to its role in promoting mast cell and Th2 dependent inflammation, ST2 activation enhances antigen induced hypernociception and protects from atherosclerosis and cardiac hypertrophy (5, 12-14). The soluble ST2 isoform is released by activated Th2 cells and strained cardiac myocytes and is elevated in the serum in allergic asthma (6, 8, 15). Soluble ST2 functions as a decoy receptor that blocks IL33 signaling by full-length ST2 (10, 13‑15). Our Avi-tag Biotinylated ST2 features biotinylation at a single site contained within the Avi-tag, a unique 15 amino acid peptide. Protein orientation will be uniform when bound to streptavidin-coated surface due to the precise control of biotinylation and the rest of the protein is unchanged so there is no interference in the protein's bioactivity.
  1. Barksby, H.E. et al. (2007) Clin. Exp. Immunol. 149:217.
  2. Gadina, M. and C.A. Jefferies (2007) Science STKE 2007:pe31.
  3. Tominaga, S. et al. (1992) Biochim. Biophys. Acta. 1171:215.
  4. Li, H. et al. (2000) Genomics 67:284.
  5. Schmitz, J. et al. (2005) Immunity 23:479.
  6. Lecart, S. et al. (2002) Eur. J. Immunol. 32:2979.
  7. Brint, E.K. et al. (2004) Nat. Immunol. 5:373.
  8. Weinberg, E.O. et al. (2002) Circulation 106:2961.
  9. Sanada S. et al. (2007) J. Clin. Invest. 117:1538.
  10. Palmer, G. et al. (2008) Cytokine 42:358.
  11. Chackerian, A.A. et al. (2007) J. Immunol. 179:2551.
  12. Allakhverdi, Z. et al. (2007) J. Immunol. 179:2051.
  13. Verri, Jr. W.A. et al. (2008) Proc. Natl. Acad. Sci. 105:2723.
  14. Miller, A.M. et al. (2008) J. Exp. Med. 205:339.
  15. Hayakawa, H. et al. (2007) J. Biol. Chem. 282:26369.

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Recombinant Human
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AVI11066
Recombinant Human ST2/IL-33R Fc Chimera Avi-tag Protein, CF
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