rHuIL-18 GMP

Escherichia coli

> 95% by SDS-PAGE analyses.
> 98% by HPLC analyses.

Approximately 18.2 kDa, a single non-glycosylated polypeptide chain containing 157 amino acids.

YFGKLESKLS VIRNLNDQVL FIDQGNRPLF EDMTDSDCRD NAPRTIFIIS MYKDSQPRGM AVTISVKCEK ISTLSCENKI ISFKEMNPPD NIKDTKSDII FFQRSVPGHD NKMQFESSSY EGYFLACEKE RDLFKLILKK EDELGDRSIM FTVQNED

Measured by its ability to induce IFN-gamma secretion by KG‑1 human acute myelogenous leukemia cells. The ED50 for this effect is 1.5-15 ng/mL. The specific activity of recombinant human IL-18 is > 3.0 × 106 Units/mg, which is calibrated against rHuIL-18 WHO reference reagent (NIBSC code: 03/200).

Sterile filtered white lyophilized (freeze-dried) powder.

Lyophilized from a 0.2 μm filtered solution in PBS, 0.05% Tween-20, pH 7.0.

Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
- A minimum of 12 months from date of receipt, when stored at ≤ -20 °C as supplied.
- 1 month, 2 to 8 °C under sterile conditions after reconstitution.
- 3 months, -20 to -70 °C under sterile conditions after reconstitution.
- Refer to lot-specific CoA for the Expiry Date.

The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.

Less than 0.01 EU/μg of rHuIL-18 GMP as determined by LAL method.

Less than 0.05% when tested by ELISA.

Less than 20 ng/mg when tested by qPCR.

Prior to opening, it is recommended to centrifuge the vial briefly to bring the contents down the bottom. Reconstitute in sterile distilled water or aqueous buffer containing 0.1% BSA to a concentration of 0.1-0.3 mg/mL. If animal-origin-free condition is expected in your product, then sterile distilled water is recommended. Stock solutions should be apportioned into working aliquots and stored at ≤ -20 °C. Further dilutions should be made in appropriate buffered solutions.

This material is offered by Shanghai PrimeGene Bio-Tech for research, laboratory, or further evaluation purposes. NOT FOR HUMAN USE.

The manufacturing and testing of these products comply with ICH Q7 guidelines.

Negative

Negative

Negative

5μg, 100μg

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. IL-18 binds to the widely expressedIL-18 R alpha which recruits IL-18 R beta to form the signaling receptor complex. Its bioactivity is negatively regulated by interactions with IL-18 binding proteins and virally encoded IL-18BP homologs. 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. 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. 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. IL-18 also promotes myeloid dendritic cell maturation and triggers neutrophil respiratory burst. In cancer, IL-18 exhibits diverse activities including enhancing anti-tumor immunity, inhibiting or promoting angiogenesis, and promoting tumor cell metastasis. Mature human IL-18 shares approximately 63% amino acid sequence identity with mouse and rat IL-18. Alternative splicing in human ovarian cancer generates an isoform that is resistant to Caspase-1 activation. A cell surface form can be expressed on M-CSF induced macrophages and released in response to bacterial endotoxin.