Brief Summary

GDF-8, also known as myostatin, is a recombinant growth differentiation factor studied in laboratory settings for its role in muscle-cell regulation, myogenic signalling and tissue-development pathways. It belongs to the transforming growth factor beta superfamily and is investigated primarily as a regulatory protein associated with skeletal muscle growth and differentiation. Research has focused particularly on its interaction with activin type II receptors and the downstream SMAD-associated signalling pathways involved in myoblast activity, muscle-fibre development and protein regulation. Within scientific research catalogues, GDF-8 is valued for in vitro and preclinical investigation involving myogenic pathway activity, growth-factor signalling, cellular differentiation and comparative ligand-receptor analysis. Its defined mature protein sequence supports structured laboratory study, analytical characterisation and reproducible growth-factor research within professional scientific environments.

Product Overview

GDF-8 is a laboratory-grade recombinant protein developed for controlled research into myostatin signalling, muscle-cell differentiation and transforming growth factor beta pathway activity. The mature GDF-8 protein contains 109 amino acids and forms a disulphide-linked homodimer under biologically active conditions. This dimeric structure allows GDF-8 to interact with activin type II receptors, including ActRIIB, before recruiting associated type I receptors and initiating intracellular signalling. GDF-8 has been examined in myoblast cultures, muscle-cell development models and protein-expression assays involving myogenic regulatory factors. It is particularly relevant to comparative studies involving Follistatin, ACE-031 and other compounds associated with myostatin-pathway regulation. Its defined composition and reproducible molecular characteristics support controlled investigation into receptor binding, cellular differentiation, muscle-associated gene expression and growth-factor communication.

Scientific Background

From a molecular science perspective, GDF-8 is studied as a signalling protein that contributes to the regulation of skeletal muscle development. It is synthesised as a larger precursor protein before proteolytic processing releases the mature C-terminal growth-factor domain. Two mature GDF-8 chains form a disulphide-linked homodimer that can bind activin type II receptors on the cellular surface. This interaction supports the recruitment of type I receptors and the activation of SMAD2 and SMAD3-associated intracellular pathways. These signalling events are examined for their relationship with myoblast proliferation, cellular differentiation and muscle-associated protein expression. Laboratory studies also investigate the regulation of GDF-8 through extracellular binding proteins such as Follistatin and natural inhibitory propeptides. GDF-8 therefore provides a useful molecular tool for examining ligand-receptor communication, myogenic pathway regulation and the relationship between extracellular growth factors and muscle-cell responses.

Research Applications

GDF-8 is applied in laboratory research across protein science, molecular biology, myogenic pathway investigation and growth-factor regulation. Researchers use the protein to examine activin type II receptor binding, SMAD2 and SMAD3-associated signalling, myoblast differentiation and muscle-cell development under controlled experimental conditions. Additional research applications include analysis of myogenic regulatory proteins, muscle-fibre formation, cellular proliferation markers and comparative evaluation against Follistatin or other myostatin-binding compounds. GDF-8 may also be used to investigate extracellular ligand regulation, receptor activation and the influence of growth-factor concentration on cellular signalling responses. Its mature 109-amino-acid structure supports research into protein processing, homodimer formation, disulphide-bond stabilisation and structure-activity relationships. These applications contribute to a broader understanding of transforming growth factor beta superfamily signalling and the molecular regulation of myogenic cellular pathways. GDF-8 is supplied as a research compound for analytical, in vitro and controlled preclinical investigation only.

Technical Specifications

Contents: 1mg GDF-8
Form: Lyophilised powder
Purity: >99% (HPLC Verified)
Molecular Formula: C₅₅₀H₈₂₃N₁₄₇O₁₅₈S₁₂
Molecular Weight: Approximately 12,407 g/mol
Sequence: DFGLDCDEHSTESRCCRYPLTVDFEAFGWDWIIAPKRYKANYCSGECEFVFLQKYPHTHLVHQANPRGSAGPCCTPTKMSPINMLYFNGKEQIIYGKIPAMVVDRCGCS
Peptide Length: 109 amino acids
pH Range: 7.0-7.5
Storage: Store between 1°C and 5°C 

Note: Reconstitute with Bacteriostatic Water

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For research purposes only. Not for human consumption