IL 11 Recombinant eiwit

Source : Escherichia Coli. Interleukin-11 Human Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 179 amino acids and having a molecular mass of 19256.29 Dalton. The IL-11 is purified by proprietary chromatographic techniques. IL11 is a member of the gp130 family of cytokines. These cytokines drive the assembly of multisubunit receptor complexes, all of which contain at least one molecule of the transmembrane signaling receptor IL6ST (gp130) . IL-11 is shown to stimulate the T-cell-dependent development of immunoglobulin-producing B cells. It is also found to support the proliferation of hematopoietic stem cells and megakaryocyte progenitor cells.

AGIF||Adipogenesis inhibitory factor||Oprelvekin||IL-11.

Greater than 98.0% as determined by: (a) Analysis by RP-HPLC. (b) Analysis by SDS-PAGE.

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

Lyophilized Interleukin-11 although stable at room temperature for 3 weeks, should be stored desiccated below -18°C. Upon reconstitution IL11 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) .Please prevent freeze-thaw cycles.

It is recommended to reconstitute the lyophilized Interleukin 11 in sterile 18MΩ-cm H2O not less than 100μg/ml, which can then be further diluted to other aqueous solutions. The ED50 as determined by the dose-dependant stimulation of the proliferation of murine 7TD1 was found to be < 10ng/ml, corresponding to a Specific Activity of 100,000 IU/mg.

The sequence of the first five N-terminal amino acids was determined and was found to be Gly-Pro-Pro-Pro-Gly. N-terminal methionine has been completely removed enzymatically.