Follistatin 344

Growth Hormone & Body Composition Research
Myostatin & Muscle-Signaling Research Protein
Myostatin · Activin · TGF-β Signaling
1mg

$169.99

Availability: In stock

For research purposes only.
Emma Lindsay research guide in a white lab coat with a steel blue blouse

Emma Lindsay

RESEARCH GUIDE

I’ve pulled together the key product details, research context, and supporting information so you can quickly decide whether this item lines up with your research goals.

Overview

Follistatin 344 is most commonly researched for its connection to muscle growth, body composition, and the biological systems that place limits on muscle development. Rather than directly stimulating muscle tissue like a growth hormone, follistatin interacts with regulatory proteins such as myostatin, often described as one of the body’s natural “brakes” on skeletal-muscle growth. This has made Follistatin 344 particularly interesting in research involving muscle development, age-related muscle loss, muscular disease, and the mechanisms that control how muscle tissue grows and adapts.

At the molecular level, Follistatin 344 is a precursor form that gives rise primarily to the circulating FS315 follistatin isoform. Follistatin acts as an extracellular binding protein for members of the TGF-β superfamily, particularly activin A and myostatin (GDF-8), limiting their ability to activate downstream activin type-II receptor and SMAD2/3 signaling. Human research involving FS344 has primarily used gene-transfer approaches, including early studies in muscular dystrophy, rather than direct administration of recombinant Follistatin 344 protein. For that reason, the strong mechanistic and preclinical evidence should be distinguished from the much more limited evidence for the research product itself in humans

The Science Behind Follistatin 344
Explore how Follistatin 344 interacts with myostatin, activin, and TGF-β signaling involved in skeletal-muscle regulation.

Follistatin is a naturally occurring binding protein that regulates several members of the transforming growth factor-beta, or TGF-β, superfamily. Two of its best-known targets are activin A and myostatin (GDF-8). Myostatin acts as an important negative regulator of skeletal-muscle growth, while activin participates in reproductive, metabolic, inflammatory, and tissue-regulatory pathways. By binding these signaling proteins before they reach their receptors, follistatin can reduce downstream signaling activity.

The term Follistatin 344, or FS344, refers to the 344-amino-acid precursor that is processed to produce the longer circulating FS315 isoform. This longer form differs from the shorter FS288 isoform in its tissue distribution and binding characteristics. That distinction matters because many commercial descriptions incorrectly treat “Follistatin 344” as though it were simply a 344-amino-acid injectable peptide with a single straightforward muscle-building mechanism. In reality, follistatin biology involves several ligands and multiple regulatory systems.

Much of the interest in Follistatin 344 comes from animal studies and gene-transfer experiments showing increased skeletal-muscle mass after suppression of myostatin signaling. Human FS344 research has also been performed, but the best-known studies delivered the FS344 gene through an adeno-associated viral vector, causing muscle cells to produce follistatin themselves. That is biologically and pharmacologically different from administering recombinant Follistatin 344 protein directly.

Is Follistatin 344 Right for Your Research Goals?
Discover where Follistatin 344 fits within myostatin, skeletal-muscle, body-composition, and TGF-β signaling research.

Follistatin 344 may be relevant for research focused on myostatin inhibition, skeletal-muscle regulation, muscle-fiber growth, age-related muscle decline, activin signaling, and TGF-β biology. It is particularly useful when the research question involves the biological mechanisms that normally restrain muscle growth rather than pathways that directly stimulate growth-hormone secretion.

Human research provides an important but frequently misunderstood part of the evidence. Small early-stage studies in people with muscular disorders investigated AAV-mediated delivery of the FS344 gene. In Becker muscular dystrophy, investigators reported exploratory improvements in functional measures such as the six-minute walk test, but participant numbers were very small and the studies were not large randomized trials.

Other approaches targeting the follistatin/myostatin pathway have demonstrated an equally important lesson: increasing muscle size does not automatically mean increasing muscle function. For example, the engineered follistatin-based agent ACE-083 increased localized muscle volume in clinical research but failed to produce corresponding improvements in strength or function, and its development was discontinued. That makes Follistatin 344 scientifically interesting while reinforcing the need to distinguish muscle-mass signaling from demonstrated functional benefit.

Research Use, Reconstitution & Storage
General research information on Follistatin 344 preparation, experimental use, reconstitution, and storage.

There is no established human dosing protocol for direct recombinant Follistatin 344 protein supported by controlled clinical trials. Published positive human research involving FS344 has primarily used gene-transfer technology, where a vector causes cells to express follistatin over time. Those study protocols cannot be converted into dosing guidance for a lyophilized research vial.

Because Follistatin 344 is substantially larger and structurally more complex than many short research peptides, laboratory preparation should follow validated protocols appropriate to recombinant proteins. Reconstitution should use a compatible research solvent and careful sterile technique. Vigorous shaking should be avoided, as unnecessary agitation can contribute to protein denaturation or aggregation.

Store the lyophilized material under the validated conditions supplied with the research product and protect it from heat, light, moisture, and repeated temperature changes. After reconstitution, appropriate refrigerated or frozen storage should be determined from the specific laboratory protocol, and repeated freeze-thaw cycles should be minimized.

The SilverLeaf Reconstitution Calculator may assist with basic mass and concentration calculations, but experimental concentration and handling requirements should always be based on the specific research design.

-SILVERLEAF MULTI-BUY OFFER-

BUY 4.
GET 1 FREE.

Add any 5 eligible peptides to your cart. The lowest-priced item is automatically free.

No coupon code required.

Related Research Products for Follistatin 344

Research Guides & Resources

How to Pay With Bitcoin in Canada

Follow a simple step-by-step guide to buying Bitcoin in Canada and completing your SilverLeaf Bio order securely.

Peptide Research Beginner’s Guide

Learn the basics of peptide research, including reconstitution, measurement, handling, record-keeping, and good research practices.

Questions About This Peptide?

Meet NOVA — Your AI Research Assistant

Get instant answers about peptide biology, research applications, storage requirements, research pairings, shipping details, and more.

Trained on SilverLeaf Bio product information, educational resources, and research content.

Third-Party Tested

Quality you can trust.

FREE Shipping

On all Orders over $300

Earn Rewards

Collect points on every purchase

Canadian Focused

Family Owned & Operated

Shopping Cart
Ask Nova Ask Nova