Follistatin

Description

Overview of Follistatin

Follistatin is encoded by the FST gene. It is associated with regulatory systems within the transforming growth factor-beta (TGF-β) superfamily. It contains cysteine-rich domains that facilitate high-affinity binding to specific ligands. This is particularly important for binding to ligands such as activin and myostatin.

In research settings, these interactions are examined at the molecular level. This helps researchers understand how ligand sequestration influences receptor accessibility and downstream signaling pathways.

Note: Follistatin is not approved for human or veterinary use and is intended strictly for laboratory research purposes.

Chemical and Molecular Properties 

Follistatin
Molecular Formula	Not a single fixed formula (protein composed of ~344 amino acids)
Molar Mass	~37–40 kDa (≈ 37,000–40,000 g/mol depending on isoform)
Synonyms	Activin-binding protein; FST (gene product)
IUPAC	Not commonly assigned due to peptide complexity; defined by full amino acid sequence
Labeling	Research Use Only (RUO). Not for human or veterinary use.
Chemical Structure Depiction
Purity	≥98%
Classification	Research Use Only (RUO)
Safety	Handle with gloves, a lab coat, and eye protection; use a fume hood if dust/aerosol is possible

Working Mechanism of Follistatin

Follistatin’s activity is primarily defined through ligand-binding interactions. These interactions influence downstream signaling pathways. The following mechanisms describe its molecular behavior:

• Follistatin forms high-affinity complexes with activin and myostatin, preventing their interaction with activin receptors (ActRIIA/IIB).
• This ligand sequestration alters downstream signaling cascades. Follistatin indirectly inhibits SMAD signaling by blocking ligand binding upstream.
• The binding interaction is mediated through follistatin’s cysteine-rich domains. These interactions stabilize ligands–protein complexes. 
• Follistatin indirectly influences transcriptional signaling pathways. This occurs through modulation of ligand–receptor interactions. These pathways are regulated by SMAD complexes.
• The protein’s activity is also associated with extracellular regulation, affecting the distribution and bioavailability of signaling molecules in the cellular microenvironment.

Why Choose Purerawz for Follistatin?

Buy Follistatin for laboratory research use from our online shop. At Purerawz, we provide high-quality reference materials. Each research compound comes with a Certificate of Analysis for verification of purity and concentration.

Note:

Recombinant follistatin and related therapies are under investigation.It has not been evaluated or approved for therapeutic use.

Disclaimer

This information is for educational purposes only and not medical advice. Products are for research use only. Research must follow IRB or IACUC guidelines. Verify information independently before purchasing. By ordering, you agree to our Terms and Conditions. If you are not 100% satisfied with the product you received, please contact us at support@purerawz.co

ATTENTION: All our products are for LABORATORY AND RESEARCH PURPOSES ONLY, not for veterinary or human use

Reference Links

• PubMed. (2011). Follistatin-related study. PubMed; National Library of Medicine. https://pubmed.ncbi.nlm.nih.gov/21353885/ 
• PubMed. (2006). Follistatin-related study. PubMed; National Library of Medicine. https://pubmed.ncbi.nlm.nih.gov/16482217/ 
• National Library of Medicine (NLM). (2003). Follistatin. MeSH Browser. https://meshb.nlm.nih.gov/record/ui?name=Follistatin 
• PubMed. (2023). Follistatin-related study. PubMed; National Library of Medicine. https://pubmed.ncbi.nlm.nih.gov/36718082/ 
• PubMed. (2017). Follistatin-related study. PubMed; National Library of Medicine. https://pubmed.ncbi.nlm.nih.gov/29020616/