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Recombinant Human IL-18/IL-1F4 Biotinylated Protein, CF

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Measured by its binding ability in a functional ELISA. When Recombinant Human IL-18 BPa His-tag Protein (11236-BP) is immobilized at 0.25 μg/mL (100 μL/well), the concentration of Biotinylated Recombinant Human IL-18/IL-1F4 (Catalog # BT9124) that produces 50% of the binding response is 1.50-12.0 ng/mL.
Measured by its binding ability in a functional ELISA. When Recombinant Human IL-18 BPa His-tag Protein (11236-BP) is immobilized at 0.25 μg/mL (100 μL/well), the concentration of Biotinylated Recombinant Human ...read more
2 μg/lane of Biotinylated Recombinant Human IL-18/IL-1F4 Protein (Catalog # BT9124) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, ...read more

Product Details

Summary
Reactivity HuSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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Recombinant Human IL-18/IL-1F4 Biotinylated Protein, CF Summary

Additional Information
Biotinylated
Details of Functionality
Measured by its binding ability in a functional ELISA. When Recombinant Human IL-18 BPa His-tag Protein (Catalog # 11236-BP) is immobilized at 0.25 μg/mL (100 μL/well), the concentration of Biotinylated Recombinant Human IL‑18/IL‑1F4 (Catalog # BT9124) that produces 50% of the binding response is 1.50-12.0 ng/mL.
Source
E. coli-derived human IL-18/IL-1F4 protein
Tyr37-Asp193
Accession #
N-terminal Sequence
Tyr37
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
15-21 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 and DTT with Trehalose.
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 250 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-18/IL-1F4 Biotinylated Protein, CF

  • Iboctadekin
  • IFN-gamma-inducing factor
  • IGIF
  • IGIFIL-1 gamma
  • IL18
  • IL-18
  • IL-18MGC12320
  • IL-1F4
  • IL1F4iboctadekin
  • IL-1g
  • Interferon gamma-inducing factor
  • interleukin 18 (interferon-gamma-inducing factor)
  • Interleukin-1 gamma
  • interleukin-18

Background

Interleukin-18 (IL-18) is a proinflammatory cytokine in the IL-1 family that exerts distinct immune effects depending on the local cytokine environment. It is expressed as a 24 kDa precursor by endothelial and epithelial cells, keratinocytes, gamma δ T cells, and phagocytes. The precursor is activated intracellularly by Caspase-1 mediated proteolysis to release the 17 kDa mature cytokine. The precursor can also be released by necrotic cells for extracellular cleavage by multiple proteases. IL‑18 activation is induced by infection or tissue damage and contributes to disease pathology in chronic inflammation (1-3). IL-18 binds to the widely expressed IL-18 R alpha which recruits IL-18 R beta to form the signaling receptor complex (4, 5). Its bioactivity is negatively regulated by interactions with IL-18 binding proteins and virally encoded IL-18BP homologs (6). In the presence of IL-12 or IL-15, IL-18 enhances anti-viral Th1 immune responses by inducing IFN-gamma production and the cytolytic activity of CD8+ T cells and NK cells (7, 8). In the absence of IL-12 or IL-15, however, IL-18 promotes production of the Th2 cytokines IL-4 and IL-13 by CD4+ T cells and basophils (9, 10). In the presence of IL-1 beta or IL-23, IL-18 induces the antigen-independent production of IL-17 by gamma δ T cells and CD4+ T cells (11). IL-18 also promotes myeloid dendritic cell maturation and triggers neutrophil respiratory burst (12, 13). In cancer, IL-18 exhibits diverse activities including enhancing anti-tumor immunity, inhibiting or promoting angiogenesis, and promoting tumor cell metastasis (14). Mature human IL-18 shares approximately 63% amino acid sequence identity with mouse and rat IL-18 (15). Alternative splicing in human ovarian cancer generates an isoform that is resistant to Caspase-1 activation (16). A cell surface form can be expressed on M-CSF induced macrophages and released in response to bacterial endotoxin (17).
  1. Dinarello, C.A. et al. (2013) Front. Immunol. 4:289.
  2. Smith, D.E. (2011) J. Leukoc. Biol. 89:383.
  3. Gu, Y. et al. (1997) Science 275:206.
  4. Torigoe, K. et al. (1997) J. Biol. Chem. 272:25737.
  5. Cheung, H. et al. (2005) J. Immunol. 174:5351.
  6. Novick, D. et al. (1999) Immunity 10:127.
  7. Fehniger, T.A. et al. (1999) J. Immunol. 162:4511.
  8. Yoshimoto, T. et al. (1998) J. Immunol. 161:3400.
  9. Yoshimoto, T. et al. (2000) Nat. Immunol. 1:132.
  10. Kroeger, K.M. et al. (2009) J. Leukoc. Biol. 86:769.
  11. Lalor, S.J. et al. (2011) J. Immunol. 186:5738.
  12. Li, J. et al. (2004) Cell. Immunol. 227:103.
  13. Elbim, C. et al. (2005) Clin. Diagn. Lab. Immunol. 12:436.
  14. Fabbi, M. et al. (2015) J. Leukoc. Biol. 97:665.
  15. Ushio, S. et al. (1996) J. Immunol. 156:4274.
  16. Gaggero, A. et al. (2004) Oncogene 23:7552.
  17. Bellora, F. et al. (2012) Eur. J. Immunol. 42:1618.

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