| Product | CAT. No. | Volumn | Shelf life | Price |
|---|---|---|---|---|
rhIL18 | GE11.1 | 50μg | 24 months | 1800 |
GE11.2 | 100μg | 2800 |
| Product | Catalog No. | Specification | Shelf life | Price |
|---|---|---|---|---|
BETAGENE rhIL-18 | GE11.1 | 50μg | 24 months | 1800 |
GE11.2 | 100μg | 2800 |
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.
Storage Class Code | WGK | Flash Point（F） |
13 - Non Combustible Solids | WGK 3 | Not Applicable |
Flash Point（C) | Personal Protection | |
Not Applicable | Dust mask type N95, Eyeshields, Gloves | |
Specs
Data
Appearence | Sterile Filtered White lyophilized (freeze-dried) powder. |
Gene ID | 3606 |
AA Sequence | YFGKLESKLSVIRNLNDQVLFIDQGNRPLFEDMTDSDCRDNAPRTIFIISMYKDSQPRGMAVTISVKCEKISTLSCENKIISFKEMNPPDNIKDTKSDIIFFQRSVPGHDNKMQFESSSYEGYFLACEKERDLFKLILKKEDELGDRSIMFTVQNED |
| Host | E.Coli |
Molecule Weight | Approximately 18.2 kDa, a single non-glycosylated polypeptide chain containing 157 amino acids. |
Biological Activity | 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, corresponding to a specific activity of ≥ 3.0 × 106 IU/mg, which is calibrated against the human IL-18 reference standard (NIBSC code: 03/200). |
| Purity | ＞95% by SDS-PAGE or HPLC |
| Formulation | Lyophilized from a 0.2 μm filtered solution in PBS, 0.02 % Tween-20, pH 7.0. |
| Host Cell DNA | < 0.02 ng/μg of protein |
| Host Cell Protein | < 0.05% when tested by ELISA |
| Mycoplasma | Negative |
Endotoxin (LAL) | < 0.01 EU/μg |
| Sterility | Negative |
Reconstitution | Before use this product, please read the direction below carefully. 1. This vial must be briefly centrifuged prior to opening to bring the contents to the bottom. 2. Reconstitute in a sterile aqueous buffer to an appropriate concentration. 3. Stock solutions should be apportioned into working aliquots and stored at ≤ -20 °C. Further dilutions should be made in appropriate buffered solutions. |
| Stability&Storage | For long term storage, the product should be stored ≤-20°C. Please avoid repeated freeze-thaw cycles after reconstitution. 1. At least 24 months from date of receipt, ≤-20℃ as supplied; 2. 1 month, 2 to 8 °C under sterile conditions after reconstitution; 3. 3 months, -20 to -70 °C under sterile conditions after reconstitution. |
Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended. |
| Description |
| 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-1β 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. |
| Data |
| |