IL-11 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 IL-6ST (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. Recombinant human IL-11 produced in Pichia pastoris is a single, non-glycosylated, Polypeptide chain of 177 amino acids (it differs from the 178 amino acid length of the native IL-11 only in lack of the N-terminal praline residue) and a molecular mass of 19 kDa. It has been purified by proprietary chromatographic techniques.
Human IL11 expressed in Pichia pastoris
CAT# CSC-CTK0246-10 (10 μg); CAT# CSC-CTK0246-50 (50 μg)
Greater than 98% as determined by SDS-PAGE and RP-HPLC analysis.
rHu IL-11 is fully biologically active when compared to a standard. The ED50, as determined by the dose-dependent stimulation of the proliferation of murine 7TD1, was found to be less then 0.2 ng/ml, corresponding to a Specific Activity of 8,000,000 units/mg.
Less than 1 EU/μg.
Sterile-filtered protein solution was lyophilized after extensive dialysis against 20 mM PBS (pH 7.0) and 2% glycine buffer.
Please centrifuge product briefly before opening vial. The lyophilized protein should be reconstituted in sterile, ultra-pure water to a concentration of 0.1 - 1.0 mg/ml. This solution can then be diluted into other aqueous buffers and stored at -20°C for future use.
Storage & Stability
The lyophilized protein, though stable at room temperature for up to 3 weeks, is best stored desiccated at -20°C. Reconstituted rHu IL-11 should be used immediately or stored long-term in undiluted working aliquots at -20°C. For long-term storage it is recommended to add a carrier protein (0.1% HSA or BSA). Avoid repeated freeze-thaw cycles.
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