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Recombinant Feline IL-18/IL-1F4 Protein, CF

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Product Details

Summary
Reactivity FeSpecies Glossary
Applications Bioactivity
Format
Carrier-Free

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Recombinant Feline IL-18/IL-1F4 Protein, CF Summary

Details of Functionality
Measured by its ability to induce IFN-gamma secretion by KG‑1 human acute myelogenous leukemia cells in the presence of TNF-alpha . The ED50 for this effect is 0.200-5.00 μg/mL in the presence of 20 ng/mL recombinant human TNF-alpha .
Source
E. coli-derived feline IL-18/IL-1F4 protein
Tyr36-Asn192, with an N-terminal Met
Accession #
N-terminal Sequence
Met
Protein/Peptide Type
Recombinant Proteins
Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Endotoxin Note
<0.01 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Bioactivity
Theoretical MW
18.3 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
19 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 MOPS, Na2SO4, EDTA and DTT.
Purity
>90%, by SDS-PAGE under reducing conditions and visualized by silver stain.
Reconstitution Instructions
Reconstitute at 100 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 Feline IL-18/IL-1F4 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 feline IL-18 shares 87% - 89% aa sequence identity with canine and porcine IL-18 and 62% - 77% with human, mouse, rat, and rhesus IL-18 (15).
  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. Ishizaka, T. et al. (2001) Vet. Immunol. Immunopathol. 79:209.

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