Specifications
- SPECIES: Human, Mouse
- SOURCE SPECIES: E. coli
- RECOMBINANT PROTEIN SEQUENCE: Human IL-33 (aa 112-270) is fused at the C-terminus to a His-tag. Amino acids C208, C227, C232 and C259 have been mutated to serine to protect IL-33 from oxidation.
- FUSION TAG: C-His-tag
- APPLICATION NOTE: This recombinant proteins is for research use only.
- PREDICTED MOLECULAR WEIGHT: ~17kDa
- BIOLOGICAL ACTIVITY: Activates human and mouse ST2-dependent NF-kappaB pathway.
Properties
- PURITY: ≥95% (SDS-PAGE).
Endotoxin level is less than <0.01EU/μg purified protein (LAL test). - PHYSICAL STATE: Lyophilized
- BUFFER: Lyophilized. Contains PBS.
- CONCENTRATION: 0.1mg/ml
- STORAGE CONDITIONS: After reconstitution, prepare aliquots and store at -20°C. Avoid freeze/thaw cycles. PBS containing at least 0.1% BSA should be used for further dilutions
Additional Info
- ADDITIONAL NAMES: IL-33 (human) (C208S / C227S / C232S / C259S Mutant); Interleukin-33 (human) (C208S / C227S / C232S / C259S Mutant); IL-1F11; NF-HEV
- Protein Accession Number: Q2YEJ5
Background
- Interleukin-33 (IL-33; HF-NEV; IL-1F11), a member of the IL-1 family of cytokines, is expressed by many cell types following pro-inflammatory stimulation and is thought to be released upon cell lysis. IL-33 binds to and signals through ST2 (IL-1R1) and its stimulation recruits MYD88, IRAK, IRAK4 and TRAF6, followed by phosphorylation of ERK1 (MAPK3) / ERK2 (MAPK1), p38 (MAPK14) and JNK. The ability of IL-33 to target numerous immune cell types, like Th2-like cells, mast cells and B1 cells, and to induce cytokine and chemokine production underlines its potential in influencing the outcome of a wide range of diseases, such as arthritis, asthma, atopic allergy & anaphylaxis, cardiovascular disease/atherosclerosis, nervous system diseases and sepsis. IL-33 facilitates Treg expansion in vitro and in vivo. Recently, IL-33 has been involved in adipocyte differentiation. The biological activity of IL-33 at its receptor ST2 is rapidly terminated in the extracellular environment by its oxidation (formation of two disulfide bridges), resulting in an extensive conformational change that disrupts the ST2 binding site. Cysteines at amino acids C208, C227, C232 and C259 control IL-33 oxidation and mutations of two or more of these four cysteines protect IL-33 from oxidation and increase its activity.
Disclaimer
- FOR RESEARCH USE ONLY
For additional information, visit ProSci's Terms & Conditions Page. - Disclaimer: Products are intended for laboratory research purposes only and should be used by qualified personnel only. They are not intended for use in humans. ProSci is not liable for damages or injuries resulting from receipt and/or use of ProSci materials. Please refer to the Material Safety Data Sheet (MSDS) for safe storage, handling, and use procedures.
Shipping Info
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