Follistatin-344
Myostatin Inhibitor- Molecular Formula
- Large glycoprotein
- Molar Mass
- ~38,000 g/mol
- CAS Number
- 80449-31-6
- Purity Standard
- 98%+ (SDS-PAGE Verified)
- Amino Acid Sequence
- 344-amino acid activin-binding protein with three follistatin domains and heparin-binding site
Overview
Follistatin-344 (FST-344) is a naturally occurring glycoprotein that functions as a potent inhibitor of several TGF-beta superfamily members, most notably myostatin (GDF-8) and activins A and B. By binding and neutralizing these growth factors, follistatin promotes muscle growth and prevents muscle wasting.
The protein contains three characteristic follistatin domains that mediate binding to target ligands, plus a heparin-binding sequence that influences tissue distribution. FST-344 is the full-length isoform that circulates systemically, while the FST-317 variant lacks the heparin-binding domain and acts more locally.
Research has demonstrated dramatic muscle hypertrophy in animal models when follistatin is overexpressed or administered exogenously. The mechanism involves both direct myostatin inhibition, which removes the brake on muscle growth, and activin inhibition, which influences muscle stem cell function and differentiation.
Beyond muscle research, follistatin plays important roles in reproductive biology (follicular development, FSH regulation), inflammation, fibrosis, and cancer. Its ability to modulate multiple TGF-beta family members makes it a broad-spectrum tool for studying this signaling pathway, though this also complicates interpretation of results.
Synthesis Overview
Follistatin-344 is produced via recombinant DNA technology, typically in Chinese hamster ovary (CHO) cells or HEK293 cells that provide appropriate post-translational modifications including glycosylation. The expression construct includes a signal peptide for secretion. Purification involves multiple chromatographic steps including heparin affinity, ion exchange, and size exclusion chromatography. Product characterization includes SDS-PAGE, Western blot, mass spectrometry, and functional binding assays for activin and myostatin.
Research Applications
- Myostatin inhibition and muscle growth mechanism studies
- Activin A and B sequestration research
- Duchenne muscular dystrophy and sarcopenia investigation
- Reproductive biology and folliculogenesis studies
- Cancer cachexia muscle wasting prevention research
- Bone morphogenetic protein pathway modulation
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