Serial dilutions of Human IL-10 Recombinant Protein were added to MC/9 cells. Cell proliferation was measured and the linear portion of the curve was used to calculate the ED50.
The purity of Human IL-10 Recombinant Protein was determined by SDS-PAGE of 1 µg reduced (+) and non-reduced (-) recombinant hIL-10 and staining with Coomassie Blue.
Human IL-10 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 hIL-10.
The bioactivity of recombinant hIL-10 was determined in an MC/9 cell proliferation assay. The ED50 of each lot is less than or equal to 5 ng/ml.
Recombinant human IL-10 was expressed in E. coli and is supplied in a lyophilized form. Endotoxin levels are less than or equal to 1 EU / 1 μg hIL-10.
Interleukin-10 (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), leading to the activation of Jak1 and Tyk2 and phosphorylation of Stat3 (1,3). The anti-inflammatory activity of IL-10 is due to its ability to block signaling through other cytokine receptors, notably IFN-γ 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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