The proliferation of MC/9 cells treated with increasing concentrations of hIL-10 in the presence of 1 pg/ml mouse IL-4 #5208 was assessed. After 72 hours treatment with hIL-10, cells were incubated with a tetrazolium salt and the OD450-OD650 was determined.
The purity of recombinant hIL-10 was determined by SDS-PAGE of 6 µg reduced (+) and non-reduced (-) recombinant hIL-10 and staining overnight with Coomassie Blue.
Western blot analysis of extracts from MC/9 cells, untreated or treated with hIL-10 for 10 minutes, using Phospho-Stat3 (Tyr705) (D3A7) Rabbit mAb #9145 (upper) or Stat3 Antibody #9132 (lower).
With carrier: Lyophilized from a 0.22 μm filtered solution of PBS, pH 7.2 containing 20 μg BSA per 1 μg hIL-10. 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. Avoid repeated freeze-thaw cycles.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-10. All lots are greater than 98% pure.
Recombinant hIL-10 contains no "tags" and has a calculated MW of 18,647. DTT-reduced protein migrates as an 18 kDa polypeptide and non-reduced protein migrates as a 16 kDa polypeptide due to intramolecular cystines. The expected amino-terminal SPGQG of recombinant hIL-10 was verified by amino acid sequencing.
The bioactivity of recombinant hIL-10 was determined in a MC/9 cell proliferation assay. The ED50 of each lot is between 0.3-1.4 ng/ml.
Less than 0.01 ng endotoxin/1μg hIL-10.
Recombinant human IL-10 (hIL-10) Ser19 - Asn178 (Accession # NP_000563) was expressed in human 293 cells at Cell Signaling Technology.
IL-10 is an anti-inflammatory cytokine that is produced by T cells, NK cells and macrophages (1,2). IL-10 initiates signal transduction by binding to a cell surface receptor complex consisting of IL-10 RI and IL-10 RII (1). Binding of IL-10 leads to the activation of Jak1 and Tyk2, which phosphorylates Stat3 (1,3). The anti-inflammatory activity of IL-10 is due to its ability to block signaling through other cytokine receptors, notably IFNγ receptor, by upregulating expression of SOCS1 (1,3). In addition, IL-10 promotes T cell tolerance by inhibiting tyrosine phosphorylation of CD28 (4,5). IL-10 is an important negative regulator of the immune response, which allows for maintenance of pregnancy (1). In contrast, increased IL-10 levels contribute to persistent Leishmania major infections (6).
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