Product Details: GDF-8 Peptide

GDF-8, also known as myostatin, is a member of the transforming growth factor-beta (TGF-β) superfamily and is investigated extensively in research models for its role in regulating cellular growth and differentiation pathways. It is typically supplied as a recombinant protein or lyophilized powder to ensure stability and reproducibility in controlled laboratory environments. [1]

This protein is synthesized as a precursor molecule that undergoes proteolytic processing to produce a biologically active mature domain. The mature form is responsible for receptor binding and downstream signaling in experimental systems. Its well-characterized structure makes it suitable for studies involving ligand–receptor interactions and signal transduction pathways. [2]

Mechanism of Action

In experimental models, GDF-8 binds to activin type II receptors (ActRIIA and ActRIIB) on the surface of target cells. This interaction initiates recruitment of type I receptors, leading to phosphorylation and activation of intracellular SMAD2/3 signaling proteins. These activated SMAD complexes translocate to the nucleus, where they regulate transcription of genes associated with cellular differentiation and regulatory processes. [2][3]

GDF-8 signaling is also associated with modulation of pathways involved in cellular proliferation and differentiation. This signaling framework provides a controlled system for studying receptor-mediated transcriptional regulation and intracellular signaling cascades in vitro. [3][4]

Properties of GDF-8 Peptide: 

• Molecular Type: Recombinant Protein (TGF-β family)
• Molecular Weight: NA
• CAS Number: NA
• PubChem CID: NA
• Synonyms: Myostatin Peptide, Growth Differentiation Factor 8, GDF-8

Research Applications/Benefits of GDF-8 Peptide

• Receptor–Ligand Interaction Studies: GDF-8 is widely used in experimental models to investigate binding interactions with activin type II receptors and downstream signaling mechanisms. [2]
• SMAD2/3 Signaling Pathway Research: This protein serves as a model ligand for studying SMAD-dependent intracellular signaling and transcriptional regulation in controlled laboratory systems. [3]
• Cellular Differentiation and Developmental Pathway Studies: GDF-8 is utilized in in-vitro systems to explore pathways associated with cellular differentiation and regulatory signaling networks. [1][4]
• TGF-β Superfamily Signaling Models: As part of the TGF-β family, GDF-8 supports comparative studies of ligand-specific signaling behavior and pathway modulation in preclinical models. [3]

Why Choose BehemothLabz for GDF-8 Peptide?

Choose BehemothLabz, choose quality! We are among the few online sellers that believe in the integrity and purity of products. Our GDF-8 peptide 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 GDF-8 Peptide 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: 

1. McPherron, A. C., Lawler, A. M., & Se-Jin Lee. (1997). Regulation of skeletal muscle mass in mice by a new TGF-beta superfamily member. Nature, 387, 83–90.
2. Se-Jin Lee, & McPherron, A. C. (2001). Regulation of myostatin activity and muscle growth. Proceedings of the National Academy of Sciences, 98(16), 9306–9311.
3. Rebbapragada, A., Benchabane, H., Wrana, J. L., Celeste, A. J., & Attisano, L. (2003). Myostatin signals through a transforming growth factor beta-like signaling pathway to block adipogenesis. Molecular and Cellular Biology, 23(20), 7230–7242.
4. Sako, D., Grinberg, A. V., Liu, J., Davies, M. V., Castonguay, R., Maniatis, S., Andreucci, A. J., Pobre, E. G., Tomkinson, K. N., Monnell, T. E., Ucran, J. A., Martinez-Hackert, E., Pearsall, R. S., Underwood, K. W., Seehra, J., & Kumar, R. (2010). Characterization of the ligand binding functionality of the extracellular domain of activin receptor type IIB. Journal of Biological Chemistry, 285(27), 21037–21048.