R 1,060.00


Follistatin (FST) is a secreted glycoprotein that was first identified as a follicle­stimulating hormone inhibiting substance in ovarian follicular fluid (1, 2). Human Follistatin cDNA encodes a 344 amino acid (aa) protein with a 29 aa signal sequence, an N­terminal atypical TGF binding domain, three Follistatin domains that contain EGF­like and kazal­like motifs, and a highly acidic C­terminal tail. Follistatin is a secreted protein that binds to ligands of the TGF-Beta family and regulates their activity by inhibiting their access to signaling receptors. It was originally discovered as activin antagonists whose activity suppresses expression and secretion of the pituitary hormone FSH (follicle stimulating hormone). In addition to being a natural antagonist, follistatin can inhibit the activity of other TGF-Beta ligands including BMP-2,-4,-6,-7, Myostatin, GDF-11, and TGF-Beta1. Follistatin is expressed in the pituitary, ovaries, decidual cells of the endometrium, and in some other tissues. Recombinant human Follistatin is a 37.8 kDa protein containing 344 amino acids.

Follistatin 344 is an autocrine glyocoprotein that is expressed in nearly every tissue that is found within animal test subjects.  It is occasionally referred to as Activin-binding Protein or FST.  It possesses a molecular weight of 36KDa, and its molecular formula is C13H16O3.


According to scientific study based on animal test subjects, the primary function of Follistatin 344 is to bind and bioneutralize members of the TGF-β superfamily; a large group of structurally related cell regulatory proteins.  The peptide has been shown to have a particular focus on activin, a protein complex that works to enhance follicle stimulating hormone biosynthesis and secretion.  Studies have indicated that Follistatin 344 binds directly to activin and works specifically as an activin antagonist to inhibit the biosynthesis and secretion of follicle-stimulating hormone (FSH)

The roots of Follistatin 344’s overall functionality can be traced back to the solliculostellate (FS) cells of the anterior pituitary gland.  This is the pea-sized gland that is located at the bottom of the hypothalamus at the base of the brain and is chiefly responsible for the control and regulation of several endocrine-related operations in an animal test subject’s body.

Some of these regulatory functions include:

  • Metabolism
  • Pain relief
  • Temperature Regulation
  • Growth

The connection that Follistatin 344 has with the cells is based on the fact that the presence of the peptide has been demonstrated to play a key role in the regulatory control of cellular proliferation.  In essence, Follistatin 344 works to protect an animal test subject’s body from uncontrolled cellular growth.  At the same time, the peptide acts an instrument of cellular differentiation; that is, the process in which a non-specialized cellular unit becomes a more specialized cell type.  According to scientific study conducted on animal test subjects, it has been determined that both of these functions play a key role in tissue building and tissue repair.  This determination has led some studies to conclude that this particular aspect of functionality correlates to the peptide’s elevated presence in the skin.

It has also been determined through scientific study that Follistatin 344 plays an active role in the blood of animal test subjects.  Specifically, it has been known to invoke an inflammatory response, meaning that its presences plays a role in triggering the complex biological response of vascular tissues to irritants, pathogens, damaged cells, or other potentially harmful stimuli.  While it has not yet been determined where exactly the peptide generates in circulating blood plasma, it has been theorized that because of its autocrine characteristic, it may come from the endothelial cells, which are the thin layer of cells that align the inner surface of blood vessels.  It has also been suggested that the peptide may originate from the white blood cells known as monocytes and or the macrophages.


Further scientific studies based on animal test subejcets have also determined that the peptide plays a role in embryo development.  It has been shown that the presence of the peptide has the capacity to block the proliferation of bone morphogenic proteins; a process that helps to enable the neural plate to form properly.

It has also been determined that the peptide plays a role in folliculogenesis within the ovary of female animal test subjects, meaning that their presence allows the ovarian follicle to mature and be properly equipped for the reproduction process.   According to scientific study based on animal test subjects, the primary role of the peptide appears to be attached to the progression of the follicle from the early antral stage to the antral/dominant stage, as well as the promotion of cellular differentiation of estrogen producing granulose cells into the progestrone producing large lutein cells.  One of the reasons that the peptide has been connected to the ovaries in this manner is due to the fact that the highest concentration of FS cells produced by the anterior pituitary gland is found within the female ovary.

Because of the way in which Follistatin 344 has been shown to work in conjunction with the ovaries of female animal test subjects, scientific studies have conducted research that may theoretically tie the peptide with the presence of polycystic ovary syndrome, also known as PCOS, hyperandrogenic anovulation or Stein-Leventhal syndrome.  This particular condition, which is one of the more common endocrine disorders found amongst female animal test subjects, is thought to be one of the chief causes behind female subfertility.  Some studies have theorized that a mutation of this particular peptide could be linked to the onset of the condition.  That said, the particular role that the peptide may have in the development of polycycstic ovary syndrome is still the subject of scientific scrutiny.


Additional scientific study that has been conducted on animal test subjects has also determined that Follistatin 344 acts as an antagonist to myostatin; a protein that is known for the regulation and control of muscle mass and size when it is released.  Studies that were conducted on laboratory mice demonstrated that Follistatin 344’s ability to block the protein resulted in an increase of muscular mass within the rodents over a set period of time.

Because of the way in which Follistatin 344 works in conjunction with myostatin, there have been a host of scientific studies conducted on animal test subjects that have determined that the peptide could be hypothetically linked to a growth in muscle mass and increases in strength.  This particular theory has been built around the notion that the peptide’s ability to inhibit the secretion of myostatin would allow an animal test subject to experience a boost in the proliferation of muscle cells, which in turn would allow for an increase in muscle mass to occur.  This particular theory was the central focus on a study that was built around macaque monkeys; the resultant data that was derived from studying the primates demonstrated that regulating the peptide through the process of gene therapy led to the growth of muscle and the increase in strength.

The monkey-based study has led to the hypothesis that the inclusion of Follistatin 344 into the process of gene therapy could contain several potentially positive ramifications in relation to a host of muscle-related ailments.  Studies in this field are particularly focused on the ways in which the peptide could theoretically aid in the treatment of muscular dystrophy.  This particular condition is representative of several muscle diseases that have been shown to weaken the musculoskeletal system, which in turn has a negative impact on mobility.  Some of these diseases include Becker muscular dystrophy, Duchenne muscular dystrophy, Limb-girdle muscular dystrophy, and myotonic muscular dystrophy.  The diseases are characterized by defects in muscle proteins, progressive skeletal muscle weakness, and the death of muscular cells and muscular tissue.  It is thought that the presence of Follistatin 344 could aid in replenishing strength levels to the affected muscles, which in turn could reverse the negative effects of the condition.

Further studies that have been conducted on animal test subjects in relation to Follistatin 344’s presence has determined that an increased volume of the peptide and its ability to increase muscle mass of specific core muscular groups, can hypothetically lead to an increase in life expectancy in cases of spinal muscular atrophy.  Also known as SMA, this autosomal recessive disease is caused by a genetic defect; this defect can lead to the death of neuronal cells in the anterior horn of the spinal cord and lead to subsequent atrophy (that is, muscle wasting) throughout the entire system.


It has been determined through scientific study based on animal test subjects that there are no negative side effects that have been linked to the presence of Follistatin 344.  Despite the fact that there are still ongoing studies that are being conducted in order to determine if there is any correlation that could conceivably link a mutation of the peptide with polycystic ovary syndrome, it should be reiterated that such studies do not involve instances of Follistatin 344 that are considered to be non-mutated in its form.  As of now, there has been no negative association linked to Follistatin 344’s non-mutated iteration.

1mg Follistatin 344

• Recombinant Human FST•

Follistatin 344 is a myostatin inhibitor. Myostatin is a hormone used to prevent muscle cells from growing too large. It is run for a period of 10 days at 100mcg per day.

Box includes:
2 x 500mcg vials Follistatin 344
1 x 1.2ml vial Bacteriostatic Water