Product Information

Contents: Recombinant Human Interleukin-23 (IL-23)
Catalog Number: 14-8239
Sizes: 2 ug, 10 ug
Formulation: Sterile liquid; phosphate buffered saline, pH 7.2, 150 mM NaCl, with 0.5% BSA, 0.22 µM filtered.
Storage Conditions: For greatest stability, keep concentration of primary stock at or above 10 µg/ml. For long term storage, aliquot into polypropylene vials (volumes of 20 µl or greater) and store at or below -80°C. Avoid repeated freeze/thaw cycles.
Handling Conditions: For best recovery, always quick-spin vial prior to opening. For dilution of current stock, always include carrier protein (1% BSA or 10% FBS) in the buffered saline diluent.
Source: Insect cells infected with baculovirus: human p40, amino acids met 1-ser 328, (accession # NM_002187) was co-expressed with human p19, amino acids met 1-pro 189, (accession # NM_016584).
Molecular Mass: The heterodimer of p40, amino acids ile 23-ser 328, cystine linked to p19, amino acids arg 20-pro 189, has a predicted molecular mass of 53,356. On non-reducing SDS-PAGE the heterodimeric cystine-linked protein migrates as a 55 kDa protein. The DTT reduced protein migrates as 43 kDa and 18 kDa polypeptides.
Purity: Greater than 98% as determined by SDS-PAGE
Endotoxin Level: Less than 0.01 ng/ug cytokine as determined by the LAL assay.
Bioactivity: Measured by induction of IL-17 secretion by mouse splenocytes. The ED₅₀ for this effect is typically 4.0 ng/ml.

Available Formats of This Product
Cat. No.	Format	Excite (nm)	Emit (nm)	Reported Applications
14-8239	Recombinant Human IL-23 (Interleukin-23, IL23)	N/A	N/A	BA ELISA std
34-8239	Carrier-Free Recombinant Human IL-23 (Interleukin-23, IL23)	N/A	N/A	BA ELISA std
39-8239	Single-Use ELISA RSG Standard Recombinant Human IL-23 (Interleukin-23, IL23)	N/A	N/A	ELISA

Questions? Please consult our answers to frequently asked questions at http://www.ebioscience.com/faq.

Description

IL-23 is a heterodimeric cytokine composed of the p40 subunit of IL-12 disulfide-linked with a protein p19. p19, like p35 of IL-12, is biologically inactive by itself. IL-23 interacts with IL-12Rbeta1 and an additional, novel beta2-like receptor subunit with STAT4 binding domain, termed IL-23R. IL-23 is secreted by activated mouse and human dendritic cells. Biological activities of mouse IL-23 are distinct from those of mouse IL-12. Mouse IL-23 was found not to induce significant amounts of IFN-γ. Mouse IL-23 does induce strong proliferation of memory T cells (but not naïve T cells), whereas IL-12 has no effect on memory cells. Additionally, mouse IL-23 (but not IL-12) can activate mouse memory T cells to produce the proinflammatory cytokine IL-17. Human IL-23 has biological properties which are less distinct from human IL-12; human IL-23 induces proliferation of memory T cells and induces moderate levels of IFN-γ production by naïve and memory T cells, as compared to IL-12.

eBioscience’s recombinant IL-23 is produced in baculovirus-infected insect cells as an authentic heterodimer of precursor p19 and p40 subunits using a dual promoter expression system. It is distinct from other available forms of the protein in that it is expressed as a true heterodimer, as opposed to a single-chain, pseudo-heterodimer in which the subunits are joined by an artificial linker.

Applications Reported

For research use only, not for diagnostic or therapeutic use. Recombinant human IL-23 is biologically active.

Applications Tested

This recombinant human IL-23 has been tested in bioassay for induction of IL-17 secretion by mouse splenocytes. The ED₅₀ for this effect is typically 4.0 ng/ml.

References

Brombacher, F., et al. 2003. Novel IL-12 family members shed light on the orchestration of Th1 responses. Trends Immunol. 24: 207-212.
Oppmann, B., et al. 2000. Novel p19 protein engages IL-12p40 to form a cytokine, IL-23, with biological activities similar as well as distinct from IL-12. Immunity. 13: 715-725.
Aggarwal, S., et al. 2003. IL-23 promotes a distinct CD4 T cell activation state characterized by the production of IL-17. J. Biol. Chem. 278: 1910-1914.

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