Mouse IL-12/IL-23 p40 Antibody
Mouse IL-12/IL-23 p40 Antibody Summary
Accession # P43432
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Detection of IL‑12/IL‑23 p40 in Mouse Spleen. IL‑12/IL‑23 p40 was detected in immersion fixed paraffin-embedded sections of Mouse Spleen using Rat Anti-MouseIL‑12/IL‑23 p40 Monoclonal Antibody (Catalog # MAB6092) at 5 µg/mL for 1 hour at room temperature followed by incubation with the Anti-Rat IgG VisUCyte™ HRP Polymer Antibody (Catalog # VC005). Before incubation with the primary antibody, tissue was subjected to heat-induced epitope retrieval using VisUCyte Antigen Retrieval Reagent-Basic (Catalog # VCTS021). Tissue was stained using DAB (brown) and counterstained with hematoxylin (blue). Specific staining was localized to cytoplasm in lymphocytes. View our protocol for IHC Staining with VisUCyte HRP Polymer Detection Reagents.
Preparation and Storage
- 12 months from date of receipt, -20 to -70 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 6 months, -20 to -70 °C under sterile conditions after reconstitution.
Background: IL-12/IL-23 p40
Interleukin 12, also known as natural killer cell stimulatory factor (NKSF) or cytotoxic lymphocyte maturation factor (CLMF), is a pleiotropic cytokine originally identified in the medium of activated human B lymphoblastoid cell lines. IL-12 is produced by macrophages and B lymphocytes and has multiple effects on T-cells and NK cells, including stimulation of cytotoxic activity, proliferation, and promotion of Th1 development as well as IFN-gamma and TNF production. IL-12 is a
disulfide-linked, 70 kDa (p70) heterodimeric glycoprotein composed of a 40 kDA (p40) subunit and a 35 kDa (p35) subunit. The p40 and p35 subunits by themselves have no IL‑12 activity, the p40 dimer has been shown to bind the IL-12 receptor and to be an IL-12 antagonist. Free p35 has not been detected in supernatant solutions of cultured cells expressing only p35 or both p35 and p40 mRNAs. In contrast, p40 is secreted in excess of IL-12 in cells expressing both p35 and p40 mRNAs. The p40 subunit of IL-12 has been shown to have extensive amino acid sequence homology to the extracellular domain of the human IL-6 receptor while the p35 subunit shows distant but significant sequence similarity to IL-6, G-CSF, and chicken MGF. These observations have led to the suggestion that IL-12 might have evolved from a cytokine/soluble receptor complex. Human and mouse IL-12 share 70% and 60% amino acid sequence homology in their p40 and p35 subunits, respectively. IL-12 apparently shows species specificity with human IL-12 reportedly showing minimal activity in the murine system.
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