Product Usage: This PRODUCT IS INTENDED AS A RESEARCH CHEMICAL ONLY. This designation allows the use of research chemicals strictly for in vitro testing and laboratory experimentation only.All product information available on this website is for educational purposes only. Bodily introduction of any kind into humans or animals is strictly forbidden by law. This product should only be handled by licensed, qualified professionals. This product is not a drug, food, or cosmetic and may not be misbranded, misused or mislabeled as a drug, food or cosmetic.

Follistatin_1MG

Follistatin

Follistatin-344 is a recombinant protein corresponding to the 344–amino acid isoform of human follistatin, a glycoprotein originally identified for its high-affinity binding to members of the transforming growth factor-β (TGF-β) superfamily, including activins and related ligands. In laboratory settings, follistatin-344 is widely utilized as a research reagent for studying growth factor regulation, ligand sequestration, and signaling pathway modulation in controlled experimental systems.*

Due to its defined amino acid sequence and reproducible recombinant production, follistatin-344 is commonly incorporated into in vitro and preclinical research models focused on cell signaling, differentiation, and protein–protein interaction studies.*

  • Protein Name: Follistatin-344
  • Protein Class: TGF-β superfamily binding protein
  • Expression Type: Recombinant protein
  • Form: Lyophilized powder
  • Purity: ≥99% (analytical verification)
  • Quantity: 1 mg per vial
  • Analytical Methods: HPLC and Mass Spectrometry (MS)
  • Manufacturing: Produced and quality-controlled under controlled laboratory conditions
  • Designation: For Research Use Only (RUO)

$155.00

$147.25 each
$139.50 each

Products will arrive in a lyophilized (powder) form for maximum stability.

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Follistatin

Scientific & Research Context

Follistatin-344 has been extensively studied in basic science and translational research for its role in binding and neutralizing specific growth factors, thereby modulating downstream signaling cascades in experimental models.* Published research has examined follistatin’s involvement in developmental biology, tissue regulation, and cellular differentiation through its interactions with activin-related pathways.*

In research environments, follistatin-344 is frequently studied in relation to:*

  • Growth factor binding and sequestration models*
  • TGF-β / activin signaling pathway research*
  • Cell differentiation and lineage commitment studies*
  • Protein–protein interaction and ligand affinity assays*
  • Molecular regulation of cellular signaling networks*

Its well-characterized binding properties make follistatin-344 a valuable tool for mechanistic studies investigating growth factor regulation at the molecular level.*

Quality & Analytical Assurance

Each batch of follistatin-344 undergoes rigorous quality control testing to confirm molecular identity, structural integrity, and purity. Verification using validated HPLC and MS methodologies ensures batch-to-batch consistency and reliability for reproducible research outcomes.

Storage & Handling

Follistatin-344 is supplied in lyophilized form to enhance stability during storage and transport. Store unopened vials in a cool, dry environment protected from light. Reconstitution and subsequent handling should follow established protein handling and laboratory best practices to maintain molecular integrity.

For further information on proper storage techniques, click the button…

Storage Instructions

Referenced Scientific Literature
Provided for informational and educational purposes only

  • Ueno N, Ling N, Ying SY, Esch F, Shimasaki S, Guillemin R. Isolation and partial characterization of follistatin: a single-chain protein that inhibits the release of follicle-stimulating hormone. Proceedings of the National Academy of Sciences USA, 1987; 84(23): 8282–8286.
  • Shimasaki S, et al. Primary structure of the human follistatin precursor and its genomic organization. Proceedings of the National Academy of Sciences USA, 1988; 85(12): 4218–4222.
  • Nakamura T, Sugino K, Titani K, Sugino H. Follistatin, an activin-binding protein, as an auto-regulatory factor in activin signal transduction. Journal of Biological Chemistry, 1991; 266(29): 19432–19437.
  • Phillips DJ, de Kretser DM. Follistatin: a multifunctional regulatory protein. Frontiers in Neuroendocrinology, 1998; 19(4): 287–322.
  • Thompson TB, et al. Structure of the follistatin–activin complex reveals antagonism of receptor binding. Developmental Cell, 2005; 9(4): 535–543.
  • Sidis Y, et al. Biological activity of follistatin isoforms and follistatin-like proteins. Endocrinology, 2006; 147(8): 3586–3597.
  • Cash JN, et al. Characterization of follistatin-type domains and their role in ligand binding. Journal of Biological Chemistry, 2012; 287(13): 10430–10441.
  • Haidet AM, et al. Long-term enhancement of skeletal muscle mass and strength by single gene administration of myostatin inhibitors. Proceedings of the National Academy of Sciences USA, 2008; 105(11): 4318–4322.
  • Rodino-Klapac LR, et al. Inhibition of myostatin with emphasis on follistatin as a therapy for muscle disease. Muscle & Nerve, 2009; 39(3): 283–296.
  • Barbé C, et al. Role of IGF-I in follistatin-induced skeletal muscle hypertrophy. American Journal of Physiology – Endocrinology and Metabolism, 2015; 309(6): E557–E567.
  • Iskenderian A, et al. Myostatin and activin blockade by engineered follistatin results in hypertrophy in mdx mice. Skeletal Muscle, 2018; 8.
  • Schumann C, et al. Increasing lean muscle mass in mice via nanoparticle-mediated hepatic delivery of follistatin mRNA. Theranostics, 2018; 8(19): 5276–5288.
  • Bloise E, et al. Differential expression of follistatin and FLRG in human breast proliferative disorders. BMC Cancer, 2009; 9: 320.
  • Zabkiewicz C, et al. Increased expression of follistatin in breast cancer reduces invasiveness and correlates with better survival. Cancer Genomics & Proteomics, 2017; 14(4): 241–251.
  • Seachrist DD, et al. Follistatin is a metastasis suppressor in a mouse model of HER2-positive breast cancer. Breast Cancer Research, 2017; 19(1): 66.
  • Shi L, et al. Clinical and therapeutic implications of follistatin in solid tumours. Cancer Genomics & Proteomics, 2016; 13(6): 425–436.
  • Grusch M, et al. Deregulation of the activin/follistatin system in hepatocarcinogenesis. Journal of Hepatology, 2006; 45(5): 673–680.
  • Ooe H, et al. Proliferation of rat small hepatocytes requires follistatin expression. Journal of Cellular Physiology, 2012; 227(6): 2363–2370.
  • Patella S, et al. Follistatin attenuates early liver fibrosis. American Journal of Physiology – Gastrointestinal and Liver Physiology, 2006; 290(1): G137–G144.
  • Zhao C, et al. Overcoming insulin insufficiency by forced follistatin expression in β-cells of db/db mice. Molecular Therapy, 2015; 23(5): 866–874.
  • Knickmeyer MD, et al. TGF-β-facilitated optic fissure fusion and BMP antagonism. Open Biology, 2018; 8(3).
  • Zimber MP, et al. Hair regrowth following a Wnt- and follistatin-containing treatment: phase 1 clinical trial. Journal of Drugs in Dermatology, 2011; 10(11): 1308–1312.

ALL ARTICLES AND PRODUCT INFORMATION PROVIDED ON THIS WEBSITE ARE FOR INFORMATIONAL AND EDUCATIONAL PURPOSES ONLY. The products offered on this website are furnished for in-vitro studies only. In-vitro studies (Latin: in glass) are performed outside of the body. These products are not medicines or drugs and have not been approved by the FDA to prevent, treat or cure any medical condition, ailment or disease. Bodily introduction of any kind into humans or animals is strictly forbidden by law.