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| Product Name | Active Recombinant Human Follistatin |
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| Description | Human recombinant protein expressed in Nicotiana benthamiana. It is produced by transient expression in non-transgenic plants. This product contains no animal-derived components or impurities. Animal Free product. 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 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. Purity >97% by SDS-PAGE gel |
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| Size | 1 µg, 5 µg, 50 µg |
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| Concentration | n/a |
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| Applications | Functional studies, Cell culture, Western Blot |
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| Other Names | FS288; Activin-binding protein |
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| Gene, Accession, CAS # | UniProt: P19883 |
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| Catalog # | RF0043 |
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| Order / More Info | Active Recombinant Human Follistatin from AGRENVEC |
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| Product Specific References | - Gajos-Michniewicz, A., 2010. Follistatin as a potent regulator of bone metabolism. Biomarkers, 15(7):563-74. - Rodino-Klapac, L.R., 2009. Inhibition of myostatin with emphasis on follistatin as a therapy for muscle disease. Muscle Nerve, 39(3):283-96. - Shimasaki, S. et al., 1988. Primary structure of the human follistatin precursor and its genomic organization. Proc. Natl. Acad. Sci., 85:4218-4222. - Shimasaki, S. et al.,1988. Porcine follistatin gene structure supports two forms of mature follistatin produced by alternative splicing. Biochem. Biophys. Res. Commun., 152:717-723. - Phillips, D.J. and de Kretser, D.M., 1998. Follistatin: a multifunctional regulatory protein. Front Neuroendocrinol., 19:287-322. |
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