Follistatin is a monomeric glycoprotein that binds to ligands of the TGF-β superfamily and regulates their activity by inhibiting their access to signalling receptors. Follistatin received its name because it suppresses synthesis and secretion of follicle-stimulating hormone (FSH) from the pituitary gland. The follistatin gene is located at chromosome 5q11.2. It is composed of a relatively small 6-kb genomic DNA consisting of six exons. There is an alternative splice site that generates two major species, a full-length version that encodes a 344-amino acid preprotein differing by a 27-amino acid sequence from its carboxy-shortened version of the 317-amino acid form missing exon 6. Prior to activation, follistatin, like myostatin, undergoes further posttranslational modification to lose another 29 amino acids by removal of the signal peptide that results in polypeptides of 315 (FS315), often referred to as the long isoform and 288 (FS288), called the short isoform. Recombinant human Follistatin isoform 2 is a polypeptide chain containing 217 amino acids (30– 217 of P19883 FST_HUMAN). It has a predicted molecular mass of 32.3 kDa. Human recombinant FST expressed in Nicotiana benthamiana is produced by transient expression in non-transgenic plants and is purified by sequential chromatography (FPLC). This product does not contain any animal–derived components or impurities.
Human FST expressed in Nicotiana benthamiana
CAT# CSC-CTK0105-5 (5 μg); CAT# CSC-CTK0105-25 (25 μg)
Greater than 97% as determined by SDS-PAGE analysis.
rHu FST is fully biologically active when compared to a standard. The activity is determined by the ability to neutralize Activin A inhibitory effect of mouse MPC-11 cells. The ED50 is 0.1-0.3 μg/ml in the presence of 7.5 ng/ml Activin A.
Less than 0.04 EU/μg.
Lyophilized from a concentrated, sterile protein solution in 0.05 M Tris-HCl buffer (pH 7.4).
Please centrifuge product briefly before opening vial. The lyophilized protein should be reconstituted in sterile, ultra-pure water to a concentration of 50 μg/ml. This solution can then be diluted into other aqueous buffers and stored at -20°C for future use. At higher concentrations the solubility may be reduced and multimers generated. Optimal concentration should be determined for specific application and cell lines.
Storage & Stability
The lyophilized protein, though stable at room temperature for up to 3 weeks, is best stored desiccated at -20°C. Reconstituted protein 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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