Brief Summary

Follistatin is a recombinant single-chain glycoprotein studied in laboratory settings for its interaction with activin-family proteins, myostatin and related transforming growth factor beta signalling pathways. The Follistatin 344 form contains 344 amino acids and acts as a high-affinity binding protein rather than directly activating a cell-surface receptor. Research has focused particularly on its ability to bind selected extracellular ligands and restrict their interaction with activin type II receptors. This molecular behaviour makes Follistatin relevant to controlled studies examining myogenic signalling, muscle-cell differentiation, protein regulation and tissue-development pathways. Within scientific research catalogues, Follistatin is valued for in vitro and preclinical investigation involving myostatin activity, activin signalling, cellular growth regulation and comparative ligand-binding analysis. Its defined protein structure supports structured laboratory study, analytical characterisation and reproducible research within professional scientific environments.

Product Overview

Follistatin is a laboratory-grade recombinant glycoprotein developed for controlled research into myostatin regulation, activin signalling and myogenic pathway activity. Follistatin 344 represents the full-length 344-amino-acid precursor form associated with the production of the soluble Follistatin 315 isoform following signal-peptide processing. Its molecular structure contains an N-terminal region and three cysteine-rich follistatin domains stabilised by multiple intramolecular disulphide bonds. These specialised domains allow Follistatin to bind selected members of the transforming growth factor beta superfamily, including activin A, activin B, myostatin and growth differentiation factor 11. By binding these extracellular proteins, Follistatin can limit their availability for receptor interaction in experimental systems. Its defined composition and reproducible molecular characteristics support controlled investigation into ligand sequestration, myogenic signalling, cell differentiation and growth-factor regulation.

Scientific Background

From a molecular science perspective, Follistatin is studied as an extracellular binding protein that regulates selected transforming growth factor beta superfamily pathways. Myostatin, also known as growth differentiation factor 8, acts through activin type II receptors and downstream SMAD-associated signalling. Follistatin can bind myostatin before receptor interaction, allowing researchers to examine how extracellular ligand availability influences intracellular pathway activity. Follistatin also binds activins, which are involved in cellular differentiation, proliferation and broader tissue-associated signalling. Its three follistatin domains form specialised binding surfaces that create stable complexes with these target proteins. Laboratory studies have examined Follistatin in myoblast cultures, muscle-fibre development models, protein-expression assays and comparative ligand-binding experiments. Follistatin therefore provides a useful molecular tool for investigating ligand neutralisation, receptor-pathway regulation and the relationship between extracellular growth factors and myogenic cellular responses.

Research Applications

Follistatin is applied in laboratory research across protein science, molecular biology, myogenic pathway investigation and growth-factor regulation. Researchers use the protein to examine myostatin binding, activin sequestration, activin type II receptor signalling and downstream SMAD-associated responses under controlled experimental conditions. Additional research applications include myoblast differentiation studies, muscle-cell development models, protein-synthesis markers, tissue-growth signalling and comparative evaluation against other myostatin-pathway compounds. Follistatin may also be used to investigate extracellular ligand regulation, cell-culture responses and the influence of glycoprotein structure on molecular binding affinity. Its 344-amino-acid structure supports research into protein-domain organisation, disulphide-bond stabilisation, ligand recognition and structure-activity relationships. These applications contribute to a broader understanding of transforming growth factor beta superfamily signalling and the molecular control of myogenic cellular pathways. Follistatin is supplied as a research compound for analytical, in vitro and controlled preclinical investigation only.

Technical Specifications

Contents: 1mg Follistatin
Form: Lyophilised powder
Purity: >99% (HPLC Verified)
Molecular Formula: C₁₆₀₆H₂₅₃₇N₄₃₇O₅₁₀S₃₃
Molecular Weight: Approximately 38,007 g/mol
Sequence: Follistatin 344
Peptide Length: 344 amino acids
pH Range: 6.5-7.5
Storage: Store between 1°C and 5°C 

Note: Reconstitute with Bacteriostatic Water

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For research purposes only. Not for human consumption