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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-gamma. Mouse IL-23 does induce strong proliferation of memory T cells (but not naive 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-gamma production by naive 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: Recombinant human IL-23 is biologically active.
Applications Tested: The ED50 of this protein, as measured by induction of IL-17A in mouse splenocytes, is less than or equal to 3.5 ng/mL. This corresponds to a specific activity of greater than or equal to 2.9 x 10e5 Units/mg.
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.
Bioactivity: The ED50 of this protein, as measured by induction of IL-17A in mouse splenocytes, is less than or equal to 3.5 ng/mL. This corresponds to a specific activity of greater than or equal to 2.9 x 10e5 Units/mg.
Endotoxin: Less than 0.01 ng/ug cytokine as determined by the LAL assay. Purity: >98% as determined by SDS-PAGE.
Molecular Weight: 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.
Storage and handling: For best recovery, quick-spin vial prior to opening. Use in a sterile environment.
Purity: Greater than 90%, as determined by SDS-PAGE.
Aggregation: Less than 10%, as determined by HPLC.
Filtration: 0.2 µm post-manufacturing filtered.
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 naive 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 naive and memory T cells, as compared to IL-12.
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