The proliferation of TF-1 cells treated with increasing concentrations of hIL-13 was assessed. After 48 hour treatment with hIL-13, cells were incubated with a tetrazolium salt and the OD450 - OD650 was determined.
The purity of recombinant hIL-13 was determined by SDS-PAGE of 6 µg reduced (+) and non-reduced (-) recombinant hIL-13 and staining overnight with Coomassie Blue.
Western blot analysis of extracts from TF-1 cells, untreated or treated with hIL-13 for 20 minutes, using Phospho-Stat6 (Tyr641) Antibody #9361 (upper) and Stat6 Antibody #9362 (lower).
With carrier: Lyophilized from a 0.22 μm filtered solution of PBS, pH 7.2 containing 20 μg BSA per 1 μg hIL-13. Carrier free: Lyophilized from a 0.22 μm filtered solution of PBS, pH 7.2.
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.Maintain sterility. Storage at -20°C should be in a manual defrost freezer.
>98% as determined by SDS-PAGE of 6 μg reduced (+) and non-reduced (-) recombinant hIL-13. All lots are greater than 98% pure.
Recombinant hIL-13 does not have a Met on the amino terminus and has a calculated MW of 12,344. DTT-reduced and non-reduced protein migrate as 12 kDa polypeptides with non-reduced protein having slightly greater mobility due to intramolecular cystines. The expected amino-terminal GPVPP of recombinant hIL-13 was verified by amino acid sequencing.
The bioactivity of recombinant hIL-13 was determined in a TF-1 cell proliferation assay. The ED50 of each lot is between 0.6-1.2 ng/ml.
Less than 0.01 ng endotoxin/1μg hIL-13.
Recombinant human IL-13 (hIL-13) Gly21-Asn132 (Accession #AAK53823) was produced in E. coli at Cell Signaling Technology.
IL-13 is produced by T cells and is important in the TH2 response. IL-13 targets include B cells, eosinophils, fibroblasts, mast cells and macrophages (1-3). IL-13 binds specifically to IL-13Rα1 that complexes with IL-4Rα to form the Type II IL-4R. Jak1 and Tyk2 are activated and signal through Stat3 and Stat6 (6). IL-13Rα2 is a different gene product, lacks the intracellular domain, does not complex with IL-4Rα and does not signal (1,6,7). The extracellular domain of IL-13Rα2 is often elevated in diseased states. IL-13 plays key roles in airway hyperresponsiveness (AHR) of allergic asthma (1,4,5) and modulates resistance to parasitic organisms (1).
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