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Follistion 344
Follistion 344 - Beligas Pharmaceuticals

Follistion 344 - Beligas Pharmaceuticals

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1 mg
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$150.00 - $150.00
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A remarkable feature of follistatin is its production of multiple isoforms through alternative splicing and post-translational modifications, leading to variants like FS288 and FS315. These isoforms have distinct biological roles based on their structures: FS288, the shortest form, has the highest affinity for cell surface proteoglycans, anchoring it to cellular sites and making it highly effective in regulating activin's local action. Conversely, FS315 has minimal cell-binding affinity. These structural differences allow follistatin to control activin’s effects on tissue development, growth, and cell differentiation across diverse biological systems.

References:

Ledger, W. (2001). Inhibin, Activin, and Follistatin in Human Reproductive Physiology. Singapore: Imperial College Press.

Disclaimer: Information provided it this page is for general information only and does not substitute for professional medical advice.

For detailed information about Follistion 344 by Beligas Pharmaceuticals, consult with your doctor or healthcare professional.

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FAQ
What are the main isoforms of follistatin?
The main isoforms are FS288 and FS315, which differ in structure due to post-translational modifications, resulting in unique binding properties.
References:

Ledger, W. (2001). Inhibin, Activin, and Follistatin in Human Reproductive Physiology. Singapore: Imperial College Press.

How are FS288 and FS315 different?
FS288 is the shortest isoform and has the highest affinity for cell surface proteoglycans, while FS315 is longer and has minimal affinity for cell surfaces.
References:

Ledger, W. (2001). Inhibin, Activin, and Follistatin in Human Reproductive Physiology. Singapore: Imperial College Press.

What role does FS288 play in activin regulation?
FS288 effectively binds to cell membranes, localizing its action and making it highly potent in blocking activin and influencing cell signaling.
References:

Ledger, W. (2001). Inhibin, Activin, and Follistatin in Human Reproductive Physiology. Singapore: Imperial College Press.