Recombinant Human IL-18/IL-1F4 Protein, Animal-Free Summary
Learn more about Animal-Free Recombinant ProteinsProduct Specifications
Tyr37-Asp193
Produced using non-animal reagents in an animal-free laboratory.
Analysis
Product Datasheets
Carrier Free
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
BT-018-AFL
| Formulation | Lyophilized from a 0.2 μm filtered solution in PBS and TCEP with Trehalose. |
| Reconstitution | Reconstitute at 500 μg/mL in water. |
| Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. |
| Stability & Storage: | Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
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Scientific Data
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Equivalent bioactivity of GMP (BT-018-GMP) Animal-Free (Catalog # BT-018-AFL) and RUO (BT-018) grades of Recombinant Human IL‑18/IL‑1F4 as measured in a IFN-gamma secretion assay using KG‑1 human acute myelogenous leukemia cells (orange, green, red, respectively).
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Animal-FreeTM Recombinant Human IL‑18/IL‑1F (Catalog # BT-018-AFL) as measured in a IFN-gamma secretion assay using KG‑1 human acute myelogenous leukemia cells. The ED50 for this effect is 1.25-15.0 ng/mL.
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2 μg/lane of Animal-Free™ Recombinant Human IL‑18/IL‑1F4 Protein (Catalog # BT-018-AFL) was resolved with SDS-PAGE under reducing (R) and non-reducing (NR) conditions and visualized by Coomassie® Blue staining, showing a band at 18kDa under reducing conditions.
Reconstitution Calculator
Background: IL-18/IL-1F4
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 (1‑3). IL-18 binds to the widely expressed IL-18 R alpha which recruits IL-18 R beta to form the signaling receptor complex (4, 5). Its bioactivity is negatively regulated by interactions with IL-18 binding proteins and virally encoded IL-18BP homologs (6). 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 (7, 8). 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 (9, 10). 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 (11). IL-18 also promotes myeloid dendritic cell maturation and triggers neutrophil respiratory burst (12, 13). In cancer, IL-18 exhibits diverse activities including enhancing anti-tumor immunity, inhibiting or promoting angiogenesis, and promoting tumor cell metastasis (14). Mature human IL‑18 shares approximately 63% amino acid sequence identity with mouse and rat IL-18 (15). Alternative splicing in human ovarian cancer generates an isoform that is resistant to Caspase-1 activation (16). A cell surface form can be expressed on M-CSF induced macrophages and released in response to bacterial endotoxin (17).
- Dinarello, C.A. et al. (2013) Front. Immunol. 4:289.
- Smith, D.E. (2011) J. Leukoc. Biol. 89:383.
- Gu, Y. et al. (1997) Science 275:206.
- Torigoe, K. et al. (1997) J. Biol. Chem. 272:25737.
- Cheung, H. et al. (2005) J. Immunol. 174:5351.
- Novick, D. et al. (1999) Immunity 10:127.
- Fehniger, T.A. et al. (1999) J. Immunol. 162:4511.
- Yoshimoto, T. et al. (1998) J. Immunol. 161:3400.
- Yoshimoto, T. et al. (2000) Nat. Immunol. 1:132.
- Kroeger, K.M. et al. (2009) J. Leukoc. Biol. 86:769.
- Lalor, S.J. et al. (2011) J. Immunol. 186:5738.
- Li, J. et al. (2004) Cell. Immunol. 227:103.
- Elbim, C. et al. (2005) Clin. Diagn. Lab. Immunol. 12:436.
- Fabbi, M. et al. (2015) J. Leukoc. Biol. 97:665.
- Ushio, S. et al. (1996) J. Immunol. 156:4274.
- Gaggero, A. et al. (2004) Oncogene 23:7552.
- Bellora, F. et al. (2012) Eur. J. Immunol. 42:1618.
Manufacturing Specifications
Animal-Free Manufacturing ConditionsOur dedicated controlled-access animal-free laboratories ensure that at no point in production are the products exposed to potential contamination by animal components or byproducts. Every stage of manufacturing is conducted in compliance with R&D Systems' stringent Standard Operating Procedures (SOPs). Production and purification procedures use equipment and media that are confirmed animal-free.
Production
- All molecular biology procedures use animal-free media and dedicated labware.
- Dedicated fermentors are utilized in committed animal-free areas.
Purification
- Protein purification columns are animal-free.
- Bulk proteins are filtered using animal-free filters.
- Purified proteins are stored in animal-free containers in a dedicated cold storage room.
Quality Assurance
- Low Endotoxin Level.
- No impairment of biological activity.
- High quality product obtained under stringent conditions.
- For ex vivo research or bioproduction, additional documentation can be provided.
FAQs
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