||Recombinant Human IL-10 produced in E. coli is a single, non-glycosylated polypeptide chain containing 160 amino acids and having a molecular mass of 18648 Dalton.
||In humans IL-10 is produced by activated CD8 (+) peripheral blood T-cells, by T-helper CD4 (+) T-cell clones (resembling Th0, Th1, and Th2) after both antigen-specific and polyclonal activation, by B-cell lymphomas, and by monocytes following cell activation by bacterial lipopolysaccharides and mast cells. B-cell lines derived from patients with acquired immunodeficiency syndrome and Burkitt"s lymphoma constitutively secrete large quantities of IL-10 into the conditioned medium. The synthesis of IL-10 by monocytes is inhibited by IL-4 and IL-10.
||>98% as determined by SDS-PAGE , RP-HPLC and FPLC.
||The protein was lyophilized from a concentrated (1mg/ml) solution containing 60mM PBS pH-6.5 and 100mM NaCl.
||The ED50 as determined by the dose-dependant co-stimulation with murine IL-4 of MC-9 cells was found to be < 2ng/ml, corresponding to a Specific Activity of 1.5 x 106IU/mg.
||Less than 0.1 ng/µg (IEU/µg) of rHuIL-10.
||It is recommended to reconstitute the lyophilized rHuIL-10 in sterile 18MΩ-cm H2O not less than 100µg/ml, which can then be further diluted to other aqueous solutions.
||Lyophilized rHuIL-10 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution rHuIL-10 should be stored at 4°C between 2-7 days and for future use below -18°C. For long-term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Aliquot to avoid repeated freeze-thaw cycles.