The protein is produced in P. Pichia by recombinant DNA technology. The protein has a molecular mass of approximately 19,000 Daltons and is non-glycosylated. The protein is 177 amino acids in length and differs from the 178 amino acid length of native IL-11 only in lacking the amino-terminal praline residue.

IL-11 is a thrombopoietic growth factor that directly stimulates the proliferation of hematopoietic stem cells and megakaryocyte progenitor cells and induces megakaryocyte maturation resulting in increased platelet production. IL-11 is a member of a family of human growth factors which includes human growth hormone, granulocyte colony-stimulating factor and other growth factors.

The protein was lyophilized from a concentrated (1mg/ml) solution with no additives.

The ED50 as determined by the dose-dependant stimulation of the proliferation of murine 7TD1 was found to be less than 0.2ng/ml, corresponding to a Specific Activity of 1.0 x 10⁶ IU/ mg.

Less than 2ng/mg (2IEU/mg) determined by LAL test.

It is recommended to reconstitute the lyophilized rHuIL-11 in sterile 18MΩ-cm H₂O not less than 100ug/ml, which can then be further diluted to other aqueous solutions.

Lyophilized rHuIL-11 although stable at room temperature for 3 weeks, should be stored desiccated below -18^oC. Upon reconstitution rHuIL-11 should be stored at 4^oC between 2-7 days and for future use below -18^oC. For long-term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Aliquot to avoid repeated freeze-thaw cycles.

AGIF; IL-11; Adipogenesis inhibitory factor, Oprelvekin, Interleukin-11.

Cytokine-cytokine receptor interaction; Hematopoietic cell lineage; Jak-STAT signaling pathway

cytokine activity, interleukin-11 receptor binding activity