Weight | 1 lbs |
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Dimensions | 9 × 5 × 2 in |
express system | E.coli |
product tag | No Tag |
purity | > 95% as determined by Tris-Bis PAGE;> 90% as determined by HPLC |
background | Interleukin (IL)-18 was originally discovered as a factor that enhanced IFN-γ production from anti-CD3-stimulated Th1 cells, especially in the presence of IL-12. Upon stimulation with Ag plus IL-12, naïve T cells develop into IL-18 receptor (IL-18R) expressing Th1 cells, which increase IFN-γ production in response to IL-18 stimulation. |
molecular weight | The protein has a predicted MW of 18.2 kDa same as Tris-Bis PAGE result. |
available size | 100 µg, 500 µg |
endotoxin | Less than 1EU per μg by the LAL method. |
Biotinylated Human IL-18 Protein (Primary Amine Labeling) 3392
$525.00 – $1,750.00
Summary
- Expression: E.coli
- Functional: Yes (ELISA)
- Amino Acid Range: Tyr37-Asp193
Biotinylated Human IL-18 Protein (Primary Amine Labeling) 3392
protein |
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Size and concentration 100, 500µg and liquid |
Form Liquid |
Storage Instructions Valid for 12 months from date of receipt when stored at -80°C. Recommend to aliquot the protein into smaller quantities for optimal storage. Please minimize freeze-thaw cycles. |
Storage buffer Shipped with dry ice. |
Purity > 95% as determined by Tris-Bis PAGE |
target relevance |
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Interleukin (IL)-18 was originally discovered as a factor that enhanced IFN-γ production from anti-CD3-stimulated Th1 cells, especially in the presence of IL-12. Upon stimulation with Ag plus IL-12, naïve T cells develop into IL-18 receptor (IL-18R) expressing Th1 cells, which increase IFN-γ production in response to IL-18 stimulation. |
Protein names Interleukin-18 (IL-18) (Iboctadekin) (Interferon gamma-inducing factor) (IFN-gamma-inducing factor) (Interleukin-1 gamma) (IL-1 gamma) |
Gene names IL18,IL18 IGIF IL1F4 |
Protein family IL-1 family |
Mass 9606Da |
Function Pro-inflammatory cytokine primarily involved in epithelial barrier repair, polarized T-helper 1 (Th1) cell and natural killer (NK) cell immune responses (PubMed:10653850). Upon binding to IL18R1 and IL18RAP, forms a signaling ternary complex which activates NF-kappa-B, triggering synthesis of inflammatory mediators (PubMed:14528293, PubMed:25500532, PubMed:37993714). Synergizes with IL12/interleukin-12 to induce IFNG synthesis from T-helper 1 (Th1) cells and natural killer (NK) cells (PubMed:10653850). Involved in transduction of inflammation downstream of pyroptosis: its mature form is specifically released in the extracellular milieu by passing through the gasdermin-D (GSDMD) pore (PubMed:33883744). |
Subellular location Cytoplasm, cytosol. Secreted. Note=The precursor is cytosolic (PubMed:33883744). In response to inflammasome-activating signals, cleaved and secreted (PubMed:33883744, PubMed:37993712, PubMed:37993714). Mature form is secreted and released in the extracellular milieu by passing through the gasdermin-D (GSDMD) pore (PubMed:33883744, PubMed:37993714). In contrast, the precursor form is not released, due to the presence of an acidic region that is proteolytically removed by CASP1, CASP4 or CASP5 during maturation (PubMed:33883744, PubMed:37993714). The secretion is dependent on protein unfolding and facilitated by the cargo receptor TMED10 (PubMed:32272059). |
Tissues [Isoform 2]: Expressed in ovarian carcinoma but undetectable in normal ovarian epithelial cells. Resistant to proteolytic activation by caspase-1 and -4. |
Structure Forms a ternary complex with ligand-binding receptor subunit IL18R1 and signaling receptor subunit IL18RAP at the plasma membrane (PubMed:14528293, PubMed:25261253, PubMed:25500532, PubMed:37993714). Mature IL18 first binds to IL18R1 forming a low affinity binary complex, which then interacts with IL18RAP to form a high affinity ternary complex that signals inside the cell (PubMed:14528293, PubMed:25261253, PubMed:25500532). Interacts with cargo receptor TMED10; the interaction mediates the translocation from the cytoplasm into the ERGIC (endoplasmic reticulum-Golgi intermediate compartment) and thereby secretion (PubMed:32272059). |
Post-translational modification The pro-IL-18 precursor is processed by CASP1, CASP4 or CASP5 to yield its mature, active form (PubMed:15326478, PubMed:25261253, PubMed:37993712, PubMed:37993714, PubMed:9334240). The pro-IL-18 precursor features autoinhibitory interactions between the propeptide and the post-cleavage-site region, preventing recognition by the IL18R1 receptor (PubMed:37993714). Processing by CASP1, CASP4 or CASP5 induces conformational changes to generate critical receptor-binding sites (PubMed:37993714). The mature form is then secreted and released in the extracellular milieu by passing through the gasdermin-D (GSDMD) pore (PubMed:33883744, PubMed:37993714). In contrast, cleavage by CASP3 inactivates IL18 (PubMed:37993714, PubMed:9334240). |
Target Relevance information above includes information from UniProt accession: Q14116 |
The UniProt Consortium |
Publications
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