| Source | Human 293 Cells | M.W. | CAS No. | ||
|---|---|---|---|---|---|
| Structural Info | |||||
| Formulation | Lyophilized in sterile filtered solution of PBS. | ||||
| Reconstitution | Before reconstitution, a brief spin is recommend to drive down any material dislodged from the bottom of the tube. The lyophilized protein should be reconstituted in sterile H2O to a desired concentration. | ||||
| Stability | The lyophilized protein is stable for at least one year if stored at -80°C. Reconstituted protein is stable for at least four weeks at 4°C, but should be stored in aliquots at -80°C for longer term. Avoid repeated freeze and thaw. |
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| 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 | ||||
Follistatin is a secreted protein that binds to some members of the TGF-β family and blocks their access to corresponding receptors. In addition to being a natural antagonist of Activins, follistatin can inhibit the activity of other TGF-β ligands including BMPs, Myostatin, GDF-11, and TGF-β1.
StemRD’s Follistatin Fc fusion protein is full-length human Follistain-288 fused to the N-terminus of the Fc domain of human
IgG1. This fusion allows stabilization of the protein in vitro and in vivo and dimerization of the recombinant protein rendering high-affinity binding to Activins.
Expression is in human 293 cells cultured in serum-free and protein-free medium. Purification of the fusion protein from culture medium is achieved by using protein A chromatography.