For research use only — not for human or veterinary use.
Analytical Verification (COA)
Each batch of Follistatin-344 supplied by Grail Formula undergoes independent third-party laboratory verification to confirm compound identity, assay content, purity and microbiological safety. Analytical testing for this batch was performed by Liquilabs s.r.o. (Czechia) using validated chromatographic and spectrometric techniques. Batch: GF122025092 Key analytical results include:
Assay Content: 1.075 mg Identification – Retention Time: 1.000 Identification – Spectrum: 983 Purity: greater than 99.8 percent Bacterial Endotoxins: below 0.001 EU per mg Total Aerobic Microbial Count: not detected Total Yeast and Mold Count: not detected
Independent heavy metal screening confirmed no detectable levels of arsenic, cadmium, cobalt, lead, nickel, mercury or vanadium. These analytical procedures ensure traceability, purity verification and laboratory-grade compound consistency.
Product Overview
Follistatin-344 is a recombinant peptide frequently studied in laboratory environments investigating regulatory protein signalling and cellular growth factor pathways. The compound belongs to a class of regulatory glycoproteins involved in biological signalling systems that interact with members of the transforming growth factor-beta (TGF-β) family. This preparation contains 1 mg of high purity lyophilized peptide supplied in a sealed research vial. The lyophilization process preserves peptide stability and allows researchers to reconstitute the compound for controlled in vitro experimentation. Because of its well-characterized molecular structure and stable analytical profile, Follistatin-344 has become a frequently referenced molecule in experimental protein signalling and regulatory pathway research.
Compound Overview
Follistatin-344 is a recombinant form of follistatin, a naturally occurring regulatory protein that binds and neutralizes specific members of the transforming growth factor-beta (TGF-β) superfamily. The protein is particularly studied for its interactions with activin proteins, which are signalling molecules involved in cellular growth regulation, tissue development and various intracellular regulatory pathways. Within experimental biochemical models, follistatin molecules are investigated for their ability to bind and modulate signalling molecules that influence cellular regulatory networks. The 344-amino-acid variant represents one of the naturally occurring isoforms derived from the follistatin precursor protein.
Historical Background and Scientific Context
Follistatin was first identified during the late twentieth century while researchers were investigating proteins capable of regulating follicle-stimulating hormone activity. Subsequent molecular biology research revealed that follistatin functions as a binding protein for activins, thereby influencing several biological signalling systems. As understanding of growth factor signalling pathways expanded, follistatin variants such as Follistatin-344 began to be studied in experimental cellular models investigating regulatory protein interactions. Today the molecule remains an important research tool in laboratory studies exploring protein-mediated signalling networks and cellular regulatory mechanisms.
Mechanistic Focus in Research
Within experimental laboratory environments, Follistatin-344 is frequently examined in relation to protein signalling systems and growth factor regulatory pathways. Research investigations commonly explore the compound in experimental models examining:
Activin binding and signalling modulation Transforming growth factor-beta pathway interactions Protein-mediated cellular regulatory networks Growth factor signalling research Comparative regulatory protein interaction studies Intracellular signalling network modelling Molecular protein-binding mechanisms
These experimental models help researchers better understand molecular communication systems that regulate cellular signalling and protein interactions.
Research Applications
In controlled research environments, Follistatin-344 may be utilized in experimental models designed to explore protein signalling systems and regulatory molecular pathways. Examples of research applications include:
Growth factor signalling investigation Protein interaction research Cellular signalling pathway modelling Molecular regulatory network studies Comparative protein binding analysis Biochemical pathway research Controlled in vitro regulatory protein studies
Grail Formula Quality
Every Grail Formula research compound is produced under strict quality control procedures designed to support reliable laboratory experimentation. Each batch undergoes independent analytical testing to verify:
Compound identity Assay accuracy Purity confirmation Microbial safety Endotoxin levels Heavy metal screening Full batch traceability
All testing is performed by independent laboratories to ensure transparent verification and reproducible research material.
Research Use Limitation
Used solely for in vitro experiments Not permitted for clinical trials involving humans Not permitted for human or veterinary administration Not permitted for investigational human use