IL-18 Antibody [D7E17] | Primary Antibodies

Application: Reactivity: Mouse

Usage Information

Dilution
WB1:1000 IHC1:5000 - 1:20000

Application
WB, IHC

Reactivity
Mouse

Source
Rabbit Monoclonal Antibody

Storage Buffer
PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage (from the date of receipt)
-20°C (avoid freeze-thaw cycles), 2 years

Predicted MW Observed MW
22 kDa 17 kDa, 22 kDa
^*Why do the predicted and actual molecular weights differ? The following reasons may explain differences between the predicted and actual protein molecular weight. Post-translational modifications(e.g., phosphorylation, glycosylation); Splice variants and isoforms; Relative charge; Multimerization.

Datasheet & SDS

Biological Description

Specificity
IL-18 Antibody [D7E17] detects endogenous levels of total IL-18 protein.

Clone
D7E17

Synonym(s)
IFN-gamma-inducing factor; Igif; IL 18; Il-; IL-1 gamma; IL-18; Il18; Interferon gamma-inducing factor; Interleukin-1 gamma; Interleukin-18

Background
Interleukin‑18 (IL‑18), originally identified as interferon‑gamma–inducing factor, is an IL‑1 family cytokine produced as an inactive cytosolic precursor by myeloid and non‑myeloid cells and converted to its mature, secreted form by inflammasome‑associated caspase‑1 or by alternative proteases such as neutrophil proteinase‑3, elastase, and cathepsin G, placing IL‑18 downstream of innate danger sensing and pyroptotic pathways. The mature cytokine engages a heterodimeric receptor composed of IL‑18Rα (IL‑1R7) and IL‑18Rβ (IL‑18RAP); IL‑18 first binds IL‑18Rα with low affinity, then recruits IL‑18Rβ to form a high‑affinity signaling complex whose intracellular Toll/IL‑1 receptor (TIR) domains assemble the MyD88–IRAK–TRAF6 adaptor and kinase platform that activates NF‑κB and AP‑1, as well as p38, JNK, and PI3K–Akt modules, leading to robust transcription of IFNG and a broad panel of pro‑inflammatory cytokines, chemokines, adhesion molecules, and Fas ligand. This signaling profile enables IL‑18 to act as a primary co‑stimulus for interferon‑gamma production by Th1 CD4⁺ T cells, CD8⁺ T cells, NK cells, and NKT cells, particularly in combination with IL‑12, IL‑15, IL‑2, or IL‑23, and to enhance NK and CD8⁺ cytotoxicity, macrophage activation, and expression of nitric oxide, matrix metalloproteinases, and inflammatory chemokines, positioning IL‑18 near the apex of the Th1‑skewing cytokine cascade. In the absence of IL‑12 or IL‑15, IL‑18 promotes Th2 and innate type‑2 responses by acting on mast cells and basophils to induce IL‑4 and IL‑13, and contributes to IL‑17‑producing γδ T‑cell and macrophage activation, illustrating its context‑dependent capacity to support Th1, Th2, or other effector programs depending on the surrounding cytokine milieu and receptor expression patterns. Biological activity of IL‑18 is tightly controlled by the secreted high‑affinity decoy IL‑18 binding protein (IL‑18BP), which sequesters mature IL‑18 and prevents engagement of IL‑18Rα, and by the related anti‑inflammatory cytokine IL‑37, which can bind IL‑18Rα in complex with IL‑1R8 to transmit inhibitory signals; only unbound “free” IL‑18 is bioactive, and extreme elevations of free IL‑18 in serum define a group of autoinflammatory conditions termed “IL‑18opathies” including NLRC4‑associated macrophage activation syndrome, systemic juvenile idiopathic arthritis, and adult‑onset Still’s disease, where IL‑18BP therapy shows clinical benefit. At the structural level, IL‑18 adopts a β‑trefoil fold closely related to IL‑1β, and crystallographic analysis of IL‑18 bound to IL‑18Rα and IL‑18Rβ reveals a three‑site binding interface that explains its receptor specificity and provides a framework for designing IL‑18 muteins and receptor‑targeted antagonists that selectively modulate signaling while preserving or enhancing antitumor functions. In host defense, IL‑18 contributes to clearance of intracellular pathogens including viruses and bacteria by reinforcing Th1 and cytotoxic responses, while dysregulated or chronically elevated IL‑18 drives tissue damage in diverse inflammatory and metabolic diseases, such as atherosclerosis, myocardial infarction, chronic obstructive pulmonary disease, Crohn’s disease, and hemophagocytic syndromes.

Background

Interleukin‑18 (IL‑18), originally identified as interferon‑gamma–inducing factor, is an IL‑1 family cytokine produced as an inactive cytosolic precursor by myeloid and non‑myeloid cells and converted to its mature, secreted form by inflammasome‑associated caspase‑1 or by alternative proteases such as neutrophil proteinase‑3, elastase, and cathepsin G, placing IL‑18 downstream of innate danger sensing and pyroptotic pathways. The mature cytokine engages a heterodimeric receptor composed of IL‑18Rα (IL‑1R7) and IL‑18Rβ (IL‑18RAP); IL‑18 first binds IL‑18Rα with low affinity, then recruits IL‑18Rβ to form a high‑affinity signaling complex whose intracellular Toll/IL‑1 receptor (TIR) domains assemble the MyD88–IRAK–TRAF6 adaptor and kinase platform that activates NF‑κB and AP‑1, as well as p38, JNK, and PI3K–Akt modules, leading to robust transcription of IFNG and a broad panel of pro‑inflammatory cytokines, chemokines, adhesion molecules, and Fas ligand. This signaling profile enables IL‑18 to act as a primary co‑stimulus for interferon‑gamma production by Th1 CD4⁺ T cells, CD8⁺ T cells, NK cells, and NKT cells, particularly in combination with IL‑12, IL‑15, IL‑2, or IL‑23, and to enhance NK and CD8⁺ cytotoxicity, macrophage activation, and expression of nitric oxide, matrix metalloproteinases, and inflammatory chemokines, positioning IL‑18 near the apex of the Th1‑skewing cytokine cascade. In the absence of IL‑12 or IL‑15, IL‑18 promotes Th2 and innate type‑2 responses by acting on mast cells and basophils to induce IL‑4 and IL‑13, and contributes to IL‑17‑producing γδ T‑cell and macrophage activation, illustrating its context‑dependent capacity to support Th1, Th2, or other effector programs depending on the surrounding cytokine milieu and receptor expression patterns. Biological activity of IL‑18 is tightly controlled by the secreted high‑affinity decoy IL‑18 binding protein (IL‑18BP), which sequesters mature IL‑18 and prevents engagement of IL‑18Rα, and by the related anti‑inflammatory cytokine IL‑37, which can bind IL‑18Rα in complex with IL‑1R8 to transmit inhibitory signals; only unbound “free” IL‑18 is bioactive, and extreme elevations of free IL‑18 in serum define a group of autoinflammatory conditions termed “IL‑18opathies” including NLRC4‑associated macrophage activation syndrome, systemic juvenile idiopathic arthritis, and adult‑onset Still’s disease, where IL‑18BP therapy shows clinical benefit. At the structural level, IL‑18 adopts a β‑trefoil fold closely related to IL‑1β, and crystallographic analysis of IL‑18 bound to IL‑18Rα and IL‑18Rβ reveals a three‑site binding interface that explains its receptor specificity and provides a framework for designing IL‑18 muteins and receptor‑targeted antagonists that selectively modulate signaling while preserving or enhancing antitumor functions. In host defense, IL‑18 contributes to clearance of intracellular pathogens including viruses and bacteria by reinforcing Th1 and cytotoxic responses, while dysregulated or chronically elevated IL‑18 drives tissue damage in diverse inflammatory and metabolic diseases, such as atherosclerosis, myocardial infarction, chronic obstructive pulmonary disease, Crohn’s disease, and hemophagocytic syndromes.

References
https://pubmed.ncbi.nlm.nih.gov/29247988/

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%