Optimized DNA sequence encoding Human Interleukin-20 mature chain was expressed in Escherichia Coli.
Nativehuman Interleukin-20 generated by the proteolytic removal of the signal peptide and propeptide, the molecule has a calculated molecular mass of approximately16kDa. Recombinant IL-20 is a monomeric protein consisting of 135 amino acid residue subunits,and migrates as an approximately 18kDa protein under non-reducing conditions and reducing conditions in SDS-PAGE.
>95%, as determined by SDS-PAGE and HPLC
The ED(50) was determined by by a cell proliferation assay using human IL-20Rα and human IL-20Rβ co-transfected murine BaF3 pro-B cells , and was found to be less than 0.6 ng/ml, corresponding to a specific activity of 1.7 × 10 6 IU/mg.
(*)Complete precursor sequence shown, expressed chain highlighted
Endotoxin content was assayed using a LAL gel clot method. Endotoxin level was found to be less than 0.1 ng/µg(1EU/µg).
Recombinant Human Interleukin-17 was lyophilized from a 0.2 μm filtered PBS solution pH 7.5.
A quick spin of the vial followed by reconstitution in distilled water to a concentration not less than 0.1 mg/mL. This solution can then be diluted into other buffers.
The lyophilized protein is stable for at least 2 years from date of receipt at -20° C. Upon reconstitution, this cytokine can be stored in working aliquots at 2° - 8° C for one month, or at -20° C for six months, with a carrier protein without detectable loss of activity. Avoid repeated freeze/thaw cycles.
This cytokine product is for research purposes only.It may not be used for therapeutics or diagnostic purposes.