Human IL-12/IL-23 p40 (Research Grade Ustekinumab Biosimilar) Antibody
Human IL-12/IL-23 p40 (Research Grade Ustekinumab Biosimilar) Antibody Summary
Ile23-Ser328
Accession # P29460
*Small pack size (-SP) is supplied either lyophilized or as a 0.2 µm filtered solution in PBS.
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Applications
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.
Scientific Data
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Human IL‑12/IL‑23 p40 ELISA Standard Curve Direct ELISA binding curve demonstrating the recognition of Human Anti-Human IL‑12/IL‑23 p40 (Research Grade Ustekinumab Biosimilar) Monoclonal Antibody (Catalog # MAB11483) to IL‑12/IL‑23 p40. The target protein was coated onto the microplate well surface, followed by binding of the antibody. A goat anti-human HRP conjugate was used for detection.
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.
Product Datasheets
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