The purity of recombinant mHis6IL-33 was determined by SDS-PAGE of 6 µg reduced (+) and non-reduced (-) recombinant mHis6IL-33 and staining overnight with Coomassie Blue.Learn more about how we get our images
The production of IL-13 by MC/9 cells cultured with increasing concentrations of mHis6IL-33 was assessed. Media from cells incubated with mHis6IL-33 for 24 hours was collected and assayed for IL-13 production by ELISA and the OD450 was determined.Learn more about how we get our images
Recombinant mouse His6IL-33 (mHis6IL-33) Ser109-Ile266 (Accession #NP_598536) was produced in E.coli at Cell Signaling Technology.
>98% as determined by SDS-PAGE of 6 μg reduced (+) and non-reduced (-) recombinant mHis6IL-33. All lots are greater than 98% pure.
Recombinant N-terminally His6-tagged mIL-33 has a calculated MW of 19,439. DTT-reduced and non-reduced protein migrate as 22 kDa polypeptides.
The bioactivity of recombinant mHis6IL-33 was determined by its ability to induce IL-13 production by MC/9 cells. The ED50 of each lot is between 1-6 ng/ml.
Less than 0.01 ng endotoxin/1 μg mHis6IL-33.
With carrier: Lyophilized from a 0.22 μm filtered solution of PBS, pH 7.2 containing 1 mM EDTA, 3 mM DTT and 20 μg BSA per 1 μg mHis6IL-33. Carrier free: Lyophilized from a 0.22 μm filtered solution of PBS, pH 7.2 containing 1 mM EDTA and 3 mM DTT.
Stable in lyophilized state at 4°C for 1 year after receipt. Sterile stock solutions reconstituted with carrier protein are stable at 4°C for 2 months and at -20°C for 6 months. Avoid repeated freeze-thaw cycles. Maintain sterility. Storage at -20°C should be in a manual defrost freezer.
IL-33 is a novel member of the IL-1 family of proteins that was discovered in a computational search to identify unknown family members (1). IL-33 is expressed by fibroblasts and endothelial cells, and is upregulated in response to inflammatory stimuli (1). IL-33 plays a key role in Th2 type inflammatory responses, including atopic allergic responses and asthma (1,2). The IL-33 receptor consists of the ST2 and IL-1 accessory protein (IL-1-Acp) (1,3). ST2 is expressed on mast cells, basophils and Th2 cells (1). In addition to its putative role as a Th2 cytokine, IL-33 also contains a nuclear localization domain and may function as a nuclear factor (4,5). The nuclear function of IL-33 remains unclear. IL-33 is released by cellular necrosis, similar to other “alarmins”, thereby signaling tissue injury (5,6). However, more recent data suggests that IL-33 may also be actively secreted from live cells via a non-classical mechanism (7).
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