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Follistatin, human recombinant

based on 3 citations in multiple journalsFollistatin, human recombinant34.1 4
An autocrine glycoprotein involved in binding and bioneutralization of members of the TGF-β superfamily
Catalog #: 4708
SKU-Size Size Price Qty
4708-10 10 μg
4708-50 50 μg
4708-100 100 μg
4708-1000 1 mg
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Product Details

Alternate Name FST, FS, Activin-binding protein
Gene Symbol FST
Gene ID 10468
Accession # P19883
Source E. coli
Appearance Lyophilized protein
Physical Form Description Sterile filtered and lyophilized from 10 mM Sodium Phosphate, pH 7.5 + 75 mM NaCl
Molecular Weight 31.5 kDa
Purity by SDS-PAGE ≥95%
Endotoxin Level <0.1 ng/μg
Biological Activity Determined by its ability to neutralize Activin A inhibitory effect of murine MPC-11 cells. The expected ED₅₀ is 0.1-0.4 µg/ml in the presence of 7.5 ng/ml Activin A.
Reconstitution Instructions Reconstitute in H₂O to a concentration of 0.1-1.0 µg/µl. The solution can then be diluted into other aqueous buffers and stored at 4°C for 1 week or –20°C for future use.
Handling Centrifuge the vial prior to opening.
Storage Conditions -20°C
Shipping Conditions Gel Pack
USAGE For Research Use Only! Not to be used in humans


Follistatin belongs to a group of structurally-diverse diffusible proteins that binds to TGF-β ligands and inhibit their activity by hindering access to signaling receptors. This naturally occurring antagonist binds to Activin, BMP-2,-4,-6,-7, Myostatin, GDF-11, and TGF-β1. Follistatin is expressed in the pituitary, ovaries, decidual cells of the endometrium, and in some other tissues. Recombinant human Follistatin is a 31.5 kDa protein containing 288 amino acids including 36 cysteine residues.

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Li, S. et. al. Activin A Binds to Perlecan through Its Pro-region That Has Heparin/Heparan Sulfate Binding Activity J. Biol. Chem., Nov 2010; 285: 36645 - 36655.
Umezu, T. et al. Follistatin-like-1, a Diffusible Mesenchymal Factor Determines the Fate of Epithelium. PNAS 2010 107: 4601-460
Rose, Jr. FF et al (2009) Hum. Mol. Genet.; 18: 997 - 1005.
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