Follistatin (human, recombinant)

Activin-binding Protein|FS|FSH-suppressing Protein|FST

Follistatin is a glycoprotein with roles in the reproductive system, as well as during development and in cell growth and differentiation.{61343,61344} It is composed of an N-terminal region, three 10-cysteine follistatin domains (FSDs), and a C-terminal segment.{61345} Alternative splicing of FST, the gene encoding follistatin, generates two isoforms: FS-288 and FS-315, which differ in the length of the C-terminal region, and a third isoform, FS-303, is formed through proteolytic cleavage of FS-315.{61345,61343,61346} Follistatin is ubiquitously expressed and primarily secreted but is found in the cytosol of certain cells.{61344,61346} It binds to proteins in the TGF-β superfamily, including activin, inhibin, and myostatin, and prevents them from interacting with their respective receptors. This inhibition of TGF-β family proteins leads to a wide variety of effects on inflammation, immunity, muscle formation, and cancer, among others.{61343,61364,61365} Overexpression of FST in breast cancer cells in vitro reduces cell growth rate, and FST expression in breast cancer is associated with increased relapse-free survival.{61365} FST gene therapy increases muscle mass and reduces knee inflammation in a mouse model of high-fat diet-induced obesity and surgically induced osteoarthritis.{61366} Cayman’s Follistatin (human, recombinant) protein can be used for ELISA and binding assay applications. This protein is a disulfide-linked homodimer. The reduced monomer, composed of follistatin (amino acids 30-344) fused to human IgG1 Fc at its C-terminus, consists of 556 amino acids and has a calculated molecular weight of 61.7 kDa. As a result of glycosylation, the monomer migrates at approximately 70 kDa by SDS-PAGE under reducing conditions.

-80

-80

Lyophilized from sterile PBS, pH 7.4

365

≥85% estimated by SDS-PAGE