Recombinant Human IL-18 Protein, >95% (SDS-PAGE), high purity
ActiBioPure™
Azide Free
Bioactive
Carrier Free
≥95%(SDS-PAGE)
Features and benefits
Expression System: E. coli
Protein Tag: N-His
Bioactivity: 1. Immobilized Recombinant Human IL-18 Bpa Protein (rp169678) at 2.0 μg/mL can bind Recombinant Human IL-18 Protein (rp156177) with the EC50 of 24.67 ng/mL. 2. Measured by its binding ability in a functional ELISA. Immobilized human IL-18 (rp156177) at 2
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10μg
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$99.90
rp156177-50μg
50μg
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$299.90
rp156177-100μg
100μg
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$479.90
rp156177-1mg
1mg
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Recombinant Human IL-18 Protein, >95% (SDS-PAGE), high purity
Grade
ActiBioPure™, Azide Free, Bioactive, Carrier Free
Product Description
Purity: >95%, by SDS-PAGE visualized with Coomassie® Blue Staining 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 expressed IL-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.
1. Immobilized Recombinant Human IL-18 Bpa Protein (rp169678) at 2.0 μg/mL can bind Recombinant Human IL-18 Protein (rp156177) with the EC50 of 24.67 ng/mL. 2. Measured by its binding ability in a functional ELISA. Immobilized human IL-18 (rp156177) at 2
17.8 kDa, under reducing condition; 17.8 kDa, under non-reducing condition
Images
Recombinant Human IL-18 protein (rp156177) - ELISA Immobilized Recombinant Human IL-18 protein (rp156177) at 2.0 μg/mL can bind GSK 1070806 (anti-IL-18) (Ab177855) with the EC50 of 481.8 ng/mL.
Recombinant Human IL-18 Protein (rp156177) - SDS-PAGE 3 μg/lane of Recombinant Human IL-18 Protein was resolved with SDS-PAGE under reducing (R) and non-reducing (N) conditions and visualized by Coomassie® Blue staining, showing a band at 17.8 kDa.
Recombinant Human IL-18 Protein (rp156177) - Binding Activity Immobilized Recombinant Human IL-18 Bpa Protein (rp169678) at 2.0 μg/mL can bind Recombinant Human IL-18 Protein (rp156177) with the EC50 of 24.67 ng/mL.
Product Specifications
Form
Lyophilized
Reconstitution
We recommend that this vial be briefly centrifuged prior to opening to bring the contents to the bottom. Reconstitute at 1.0 mg/mL in sterile distilled water. Stock solutions should be apportioned into working aliquots and stored at ≤ -20 °C. Further dilu
Storage Temp
Store at -20°C,Avoid repeated freezing and thawing
Shipped In
Ice chest + Ice pads
Stability And Storage
Store at -20°C stable up to 1 year. Avoid freeze / thaw cycle.
Certificates
Certificate of Analysis(COA)
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