Human IL-18/IL-1F4 Antibody
Human IL-18/IL-1F4 Antibody Summary
Accession # Q14116
This antibody functions as an ELISA capture antibody when paired with Goat Anti-Human IL‑18 BPa Antigen Affinity-purified Polyclonal Antibody (Catalog # AF119). This antibody pair detects the human IL-18/IL-18 BPa complex.
This product is intended for assay development on various assay platforms requiring antibody pairs. We recommend the Human IL-18/IL-18 BPa Complex DuoSet ELISA Kit (Catalog # DY8936-05) for convenient development of a sandwich ELISA or the Human IL-18 BPa Quantikine ELISA Kit (Catalog # DBP180) for a complete optimized ELISA.
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.
Human IL‑18/IL-18 BPa Complex ELISA Standard Curve. Recombinant Human IL-18/IL-18 BPa complex protein was serially diluted 2-fold and captured by Rabbit Anti-Human IL-18/IL-1F4 Monoclonal Antibody (Catalog # MAB91244) coated on a Clear Polystyrene Microplate (Catalog # DY990). Goat Anti-Human IL-18 BPa Antigen Affinity-purified Polyclonal Antibody (Catalog # AF119) was biotinylated and incubated with the protein captured on the plate. Detection of the standard curve was achieved by incubating Streptavidin-HRP (Catalog # DY998) followed by Substrate Solution (Catalog # DY999) and stopping the enzymatic reaction with Stop Solution (Catalog # DY994).
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.
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 human IL-18 shares approximately 63% amino acid sequence identity with mouse and rat IL-18 (15). Alternative splicing in human ovarian cancer generates an isoform that is resistant to Caspase-1 activation (16). A cell surface form can be expressed on M-CSF induced macrophages and released in response to bacterial endotoxin (17).
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