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Human IL-18 Protein 4839

$300.00$1,000.00

Summary

  • Expression: E.coli
  • Active: Yes (cell based assay)
  • Amino Acid Range: Tyr37-Asp193
SKU: 4839parent Categories: , Tag:
Weight1 lbs
Dimensions9 × 5 × 2 in
accession

Q14116

express system

E.coli

product tag

No Tag

purity

> 95% as determined by Tris-Bis PAGE;> 95% 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 0.02 EU per μg by the LAL method.

Human IL-18 Protein 4839

protein
Size and concentration
100, 500µg and lyophilized
Form
Lyophilized
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 at ambient temperature.
Purity
> 95% as determined by Tris-Bis PAGE
target relevance
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

Data

Cell based assay with Human IL-18 Protein
Measured by its ability to induce Interferon gamma secretion by human natural killer lymphoma NK-92 cells. The ED50 for this effect is 1-5 ng/mL (QC Test).
SPR with Human IL-18 Protein
Human IL-18 R1, His Tag captured on CM5 Chip via anti-his antibody can bind Human IL-18, No Tag with an affinity constant of 2.38 nM as determined in SPR assay (Biacore T200).
ELISA with Human IL-18 Protein
Immobilized Human IL-18 at 5µg/ml (100µl/Well) on the plate. Dose response curve for Human IL-18BP, hFc Tag with the EC50 of 16.9ng/ml determined by ELISA (QC Test).
Cell based assay with Human IL-18 Protein
Measured by its ability to induce Interferon gamma secretion by human natural killer lymphoma NK-92 cells. The ED50 for this effect is 1-5 ng/mL (QC Test).
HPLC of Human IL-18 Protein
The purity of Human IL-18 is greater than 95% as determined by SEC-HPLC.
SDS-PAGE gel of Human IL-18 Protein
Human IL-18 on Tris-Bis PAGE under reduced condition. The purity is greater than 95%.

Publications

Published literature highly relevant to the biological target of this product and referencing this antibody or clone are retrieved from PubMed database provided by The United States National Library of Medicine at the National Institutes of Health.




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Protocols

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Documents

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