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Recombinant Human IL-1 RAcP/IL-1 R3 Protein, CF

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Recombinant Human IL-1 RAcP/IL-1 R3 (Catalog # 9176-CP) inhibits IL-1 alpha -induced IL-8 secretion in HepG2 human hepatocellular carcinoma cells. The ED50 for this effect is 0.8-4 μg/mL.
Recombinant Human IL-1 RAcP/IL-1 R3 (Catalog # 9176-CP) inhibits IL-1 alpha -induced IL-8 secretion in HepG2 human hepatocellular carcinoma cells. The ED50 for this effect is 0.8-4 μg/mL.

Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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Recombinant Human IL-1 RAcP/IL-1 R3 Protein, CF Summary

Details of Functionality
Measured by its ability to inhibit IL-1 alpha -induced IL-8 secretion in HepG2 human hepatocellular carcinoma cells. The ED50 for this effect is 0.8‑4 µg/mL in the presence of 1 μg/mL of recombinant human (rh) IL-1 R2 Fc Chimera and 50 pg/mL rhIL-1 alpha .
Source
Human embryonic kidney cell, HEK293-derived human IL-1 RAcP/IL-1 R3 protein
Ser21-Glu359, with a C-terminal 6-His tag
Accession #
N-terminal Sequence
Ser21
Protein/Peptide Type
Recombinant Proteins
Purity
>90%, 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
40 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
55-65 kDa, 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.
Purity
>90%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 200 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-1 R3 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

IL-1 Receptor Accessory Protein (IL-1 RAcP), also known as IL-1 R3, is a ubiquitously expressed 70-90 kDa member of the Interleukin-1 receptor family of proteins (1). It serves as a non-ligand-binding component of the receptors for IL-1 alpha , IL-1 beta , IL-33, and IL-36 (2-4). It is a subunit of the functional signaling complex with IL-1 RI and associates with IL-1 RII in a non-signaling receptor complex (2, 5). In addition, it interacts with ST2/IL-1 R4 on mast cells and Th2 cells to create a functional IL-33 receptor complex (3). IL-1 RAcP also functions as a co-receptor for IL-36 alpha /IL-1F6, IL-36 beta /IL-1F8, and IL-36 gamma /IL-1F9 (4). Mature human IL-1 RAcP consists of a 347 amino acid (aa) extracellular domain (ECD) with three Ig-like domains, a 21 aa transmembrane segment, and a 182 aa cytoplasmic domain (2). Within the ECD, human IL-1 RAcP shares 86% aa sequence identity with mouse and rat IL-1 RAcP. Alternative splicing generates two secreted decoy receptor isoforms and an isoform with a substituted cytoplasmic domain (6-8). When present with soluble IL-1 RII, soluble IL-1 RAcP increases the IL-1 binding affinity of IL-1 RII more than 100-fold, thus neutralizing the effects of IL-1 (9). Neuronal IL-1 RAcP interacts trans-synaptically with PTP sigma and can induce excitatory pre- and post-synaptic development (10).
  1. Boraschi, D. and A. Tagliabue (2013) Semin. Immunol. 25:394.
  2. Greenfeder, S.A. et al. (1995) J. Biol. Chem. 270:13757.
  3. Chackerian, A.A. et al. (2007) J. Immunol. 179:2551.
  4. Towne, J.E. et al. (2004) J. Biol. Chem. 279:13677.
  5. Lang, D. et al. (1998) J. Immunol. 161:6871.
  6. Lu, H.-L. et al. (2008) Mol. Immunol. 45:1374.
  7. Jensen, L.E. et al. (2000) J. Immunol. 164:5277.
  8. Jensen, L.E. and A.S. Whitehead (2003) Cell. Signal. 15:793.
  9. Smith, D.E. et al. (2003) Immunity 18:87.
  10. Yoshida, T. et al. (2012) J. Neurosci. 32:2588.

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