| Source | Human 293 Cells | M.W. | CAS No. | ||
|---|---|---|---|---|---|
| Structural Info | |||||
| Formulation | Lyophilized in sterile filtered solution of PBS. | ||||
| Reconstitution | Before reconstitution, abrief spin is recommend to drive down any material dislodged from the bottom ofthe tube. The lyophilized protein shouldbe reconstituted in sterile H2O to a desired concentration. | ||||
| Stability | The lyophilized protein isstable for at least one year if stored at -80°C. Reconstituted protein is stable for at least fourweeks at 4°C, but should be stored in aliquots at -80°C forlonger term. Avoidrepeated freeze and thaw. | ||||
| Purity | Greater than 95% as determined by SDS-PAGE analysis | ||||
| Biological Activity | The activity was determined by using a SMAD reporter gene assay in cultured human cells. The IC50 ranges from 20 - 100 ng/ml in the inhibition of 2 ng/mL Activin A activity. | ||||
| Country of Origin | USA | ||||
Follistatinis a secreted protein that binds to some members of the TGF-β family and blockstheir access to corresponding receptors. In addition to being a natural antagonist ofActivins, follistatin can inhibit the activity of other TGF-β ligands includingBMPs, Myostatin, GDF-11, and TGF-β1. StemRD’s Follistatin Fc fusion protein is full-lengthhuman Follistain-288 fused to the N-terminus of the Fc domain of humanIgG1. This fusion allows stabilization of the protein in vitro and invivo and dimerization of the recombinant protein rendering high-affinity bindingto Activins.Expression is in human 293 cells cultured inserum-free and protein-free medium.Purification of the fusion protein from culture medium is achieved byusing protein A chromatography.
