The purity of Mouse IL-5 Recombinant Protein was determined by SDS-PAGE of 1 µg reduced (+) and non-reduced (-) recombinant mIL-5 and staining with Coomassie Blue. mIL-5 is a homodimer with a predicted total molecular weight (MW) of 26.3 kDa with each subunit equaling 13.15 kDa.
Mouse IL-5 Recombinant Protein is supplied as lyophilized material that is very stable at -20°C. It is recommended to reconstitute with sterile water at a concentration of 0.1 mg/ml which can be further diluted in aqueous solutions as needed. Addition of a carrier protein (0.1% HSA or BSA) is recommended for long-term storage.
A greater than or equal to 95% purity was determined by SDS-PAGE.
Endotoxin levels are less than or equal to 1 EU / 1 μg mIL-5.
The bioactivity of recombinant mIL-5 was determined in a TF-1 cell proliferation assay. The ED50 of each lot is less than or equal to 2 ng/ml.
Recombinant mouse IL-5 was expressed in E. coli and is supplied in a lyophilized form. Endotoxin levels are less than or equal to 1 EU / 1 μg mIL-5.
IL-5 is a pleiotropic cytokine that is predominantly produced by Th2 T cells but can also be expressed by activated eosinophils, mast cells, NK cells, and iNKT cells (1-4). Both human and mouse IL-5 are glycosylated disulfide-linked homodimers (1). The IL-5 receptor is a heterodimer that consists of a high affinity IL-5 binding α chain and the common β chain, which is shared by GM-CSF and IL-3 receptors, for signal transduction (1,2). Soluble IL-5Rα binds with high affinity to IL-5, thereby inhibiting IL-5 activity (1). IL-5-mediated signaling can activate the Erk1/2, Jak2, and Stat5 signaling pathways (1,2). In mice, IL-5 is important for the differentiation of antibody-secreting cells from activated B cells (2). IL-5 induces eosinophil activation, proliferation, and differentiation in both mice and humans (2,3).
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