IL11 Human Recombinant produced in Pichia Pastoris is a single, non-glycosylated, Polypeptide chain containing 177 amino acids (it differs from the 178 amino acid length of the native IL11 only in lack of the N-terminal praline residue) and having a molecular mass of 19kDa.The IL11 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.
Sterile Filtered White lyophilized (freeze-dried) powder.
IL11 was lyophilized after extensive dialysis against 20mM PB, pH7.0 and 2% Glycine buffer.
It is recommended to reconstitute the lyophilized Interleukin -11 in sterile 18M?-cm H2O not less than 100
Lyophilized IL11 althoµgh 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.Please prevent freeze-thaw cycles.
Amino Acid Sequence
The sequence of the first five N-terminal amino acids was determined and was found to be Gly-Pro-Pro-Pro-Gly.
Greater than 95.0% as determined by:(a) Analysis by RP-HPLC.(b) Analysis by SDS-PAGE.
The ED50 as determined by the dose-dependent stimulation of the proliferation of murine 7TD1 was found to be less then 0.2ng/ml, corresponding to a Specific Activity of 8,000,000 IU/ mg.
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