Product Details: Follistatin 315 Follistatin 315 is an investigational recombinant glycoprotein composed of 315 amino acids. It is produced through recombinant expression systems and supplied as a high-purity (98%) lyophilized powder for laboratory and research applications. [1][3] Follistatin belongs to a class of secreted proteins that interact with members of the transforming growth factor-beta (TGF-β) superfamily. In experimental models, it is primarily studied for its high-affinity binding to activin ligands, forming inactive complexes that regulate ligand availability in extracellular environments. [2][4] The 315-amino acid isoform differs structurally from shorter variants due to an extended C-terminal domain. This structural feature is associated with reduced affinity for cell-surface heparan sulfate proteoglycans, allowing increased extracellular diffusion in research models. [1] Mechanism of Action In experimental systems, follistatin 315 functions through direct binding to activin dimers. Structural studies demonstrate that follistatin molecules envelop the activin ligand, masking receptor-binding sites and preventing interaction with activin type II receptors. [4] This inhibition blocks downstream signaling through the SMAD2/3 pathway, which is involved in transcriptional regulation in TGF-β-related signaling cascades. These pathways are widely examined in research models for their role in cellular communication and gene expression regulation. [4]Follistatin 315 may also interact with other members of the TGF-β superfamily, contributing to broader regulatory effects on ligand availability in extracellular environments. These interactions are examined in experimental systems to better understand signaling modulation and ligand sequestration. [2] The extended C-terminal region of the FS-315 isoform contributes to altered binding dynamics compared to shorter isoforms. This structural variation is associated with reduced interaction with heparan sulfate proteoglycans, influencing extracellular mobility in research models. [1] Properties of Follistatin 315: Molecular Formula: Not defined (protein; glycosylation-dependent) Molecular Weight: ~35 kDa (approximate, isoform-dependent) CAS Number: NA PubChem CID: NA Synonyms: FST315, Follistatin Isoform 315, FS-315 Research Applications/Benefits of Follistatin 315 : Activin Binding and Neutralization Studies Follistatin 315 is used in experimental models to study activin binding and inhibition. Structural analyses confirm that follistatin forms complexes with activin, preventing receptor activation and downstream signaling. [4] TGF-β Signaling Pathway Research In vitro and preclinical models utilize follistatin 315 to investigate signaling through the TGF-β pathway. By modulating activin availability, researchers examine effects on SMAD-dependent transcriptional regulation. [4] Protein–Protein Interaction Analysis Follistatin 315 is used as a model protein to study ligand–protein interactions. Its well-characterized binding to activin allows detailed analysis of molecular binding mechanisms and complex formation. [2][4] Isoform and Structural Studies Research comparing FS-315 and other isoforms has demonstrated differences in extracellular binding and distribution. FS-315 is associated with reduced affinity for heparan sulfate proteoglycans, which influences its localization in experimental systems. [1] Why Choose BehemothLabz for Follistatin 315? Choose BehemothLabz, choose quality! We are among the few online sellers that believe in the integrity and purity of products. Our Follistatin 315 is designed to meet the industrial criteria and the needs of researchers.Before launching our products, we test them through an independent laboratory to check their purity and ingredients. This procedure maximizes the accuracy and findings of your research experiments. Additionally, we deliver nationwide and internationally. We use a secure payment system that safeguards your personal information and prevents unauthorized third-party access. So, purchase Follistatin 315 now and experience quality and purity for your research. Disclaimer: This information is for educational purposes. We do not allow the human consumption of our products. All our products are sold for laboratory and research experiments. References Hashimoto, O., Nakamura, T., Shoji, H., & Sugino, H. (1997). Differential effects of follistatin isoforms on binding to heparan sulfate proteoglycans and activin. Journal of Biological Chemistry. Shi, Y., et al. (2016). The structure of follistatin and its role in regulating TGF-β family signaling. Molecular and Cellular Endocrinology. Sugino, K., et al. (1993). Molecular heterogeneity of follistatin, an activin-binding protein. Journal of Biological Chemistry, 268(21), 15579–15587. Thompson, T. B., Woodruff, T. K., & Jardetzky, T. S. (2005). Structures of an ActRIIB:activin A:follistatin ternary complex reveal specific binding interfaces. Journal of Biological Chemistry, 280(20), 17848–17855.
