Active Recombinant Human Follistatin

C1350H2153N405O433S39

1.28

Endotoxin Level : < 0.04 EU / ug protein (LAL method)

Follistatin is a monomeric glycoprotein that binds to ligands of the TGF-beta 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 localizes to 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 is lyophilized from a Tris HCl 0.05M buffer at pH 7.4.

Functional studies, Cell culture, Western Blot

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Centrifuge vial before opening. Lyophilized protein should be reconstituted in water to a concentration of 50 ng/ul. Optimal concentration should be determined for specific application and cell lines.

Room temperature