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Follistatin 315 1mg

 

Product Name:Follistatin 315
Unit Size :1 mg/vial
Unit Quantity :1 Vial
Synonyms :Follistatin
Appearance :White Powder
Purity :99%
Source :Chemical Synthesis
Storage :Lyophilized Follistatin 315 is stable at room temperature for 90 days,however it should be stored in a freezer below -8C for any extended period of time. After reconstituting MGF should be refrigerated at temperatures not to exceed 36 F.

Please note:This product is for research use only.

 

Follistatin 315 (FST-315):

 

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 315 is a 34.7 kDa protein containing amino acids 30-344 of the FST-344 protein.

 

Biochemistry:

 

Follistatin is part of the inhibin-activin-follistatin axis.

Currently there are three reported isoforms, FS-288, FS-300, and FS-315. Two, FS-288 and FS-315, are known to be created by alternative splicing of the primary mRNA transcript. FS-300 (porcine follistatin) is thought to be the product of posttranslational modification via truncation of the C-terminal domain from the primary amino-acid chain.

Although FS is ubiquitous its highest concentration has been found to be in the female ovary, followed by the skin.

The activin-binding protein follistatin is produced by folliculostellate (FS) cells of the anterior pituitary. FS cells make numerous contacts with the classical endocrine cells of the anterior pituitary including gonadotrophs.

In the tissues activin has a strong role in cellular proliferation, thereby making follistatin the safeguard against uncontrolled cellular proliferation and also allowing it to function as an instrument of cellular differentiation. Both of these roles are vital in tissue rebuilding and repair, and may account for follistatin’s high presence in the skin.

In the blood, activin and follistatin are both known to be involved in the inflammatory response following tissue injury or pathogenic incursion. The source of follistatin in circulating blood plasma has yet to be determined, but due to its autocrine nature speculation suggests the endothelial cells lining all blood vessels, or the macrophages and monocytes also circulating within the whole blood, may be sources.

Follistatin is involved in the development of the embryo. It has inhibitory action on bone morphogenic proteins (BMPs); BMPs induce the ectoderm to become epidermal ectoderm. Inhibition of BMPs allows neuroectoderm to arise from ectoderm, a process which eventually forms the neural plate. Other inhibitors involved in this process are noggin and chordin.

Follistatin and BMPs are also known to play a role in folliculogenesis within the ovary. The main role of follistatin in the oestrus/menstrus ovary, so far, appears to be progression of the follicle from early antral to antral/dominant, and importantly the promotion of cellular differentiation of the estrogen producing granulosa cells (GC) of the dominant follicle into the progesterone producing large lutein cells (LLC) of the corpus luteum.

 

Follistatin and Muscle Growth:

 

Follistatin works by binding to and inhibiting transforming growth factor-β (TGF-β) peptides such as myostatin which is responsible for regulating and limiting muscle growth. It’s also worth pointing out that myostatin may have a regulatory role in skeletal muscle fibrosis; too much myostatin can impair tissue function and cause chronic disease in vital organs, tissues, and bone marrow.

In additional to suppressing the degenerative properties of myostatin, follistatin also suppresses the pituitary gland synthesis and secretion of follicle-stimulating hormone (FSH). High FSH levels in men may indicate that testicles are not functioning correctly; this condition limits muscle growth, recovery, and normal hormonal function. However, FSH levels that are too low can also negatively impact health and reproductive capabilities.

Whereas some myostatin inhibitors like Trichostatin A (TSA) require daily administration, increased levels of FS344 were observed up to 15 months after initial injection. The lack of need for daily administration makes follistatin an attractive alternative for suppressing myostatin. The recent increase in attention in the science community on follistatin and other myostatin inhibitors is primarily due to the desire to find an alternative means to treat muscle disorders; the most popular current option is androgen steroids which pose a number of side-effects and long-term health risks. At this point you might be wondering why follistatin use isn’t more widespread in bodybuilders and other athletes. In the next section we will examine the current research on follistatin and whether it builds muscle mass.

 

Does Follistatin Build Muscle?

 

In short, follistatin does build muscle but not necessarily in humans. A number of studies support the muscle-building and anti-degenerative effects follistatin in rodents. Unfortunately there is no formal research examining follistatin usage in human subjects but a quick Google search will yield countless amateur follistatin logs on bodybuilding and fitness forums. When scientists bred a mouse producing no myostatin and extra follistatin it had 117% larger muscle fibers and 73% more total muscle fibers compared to the mice in the control group. This study demonstrates that follistatin positively impacts muscle growth in ways beyond simply suppressing myostatin. Mice with suppressed myostatin had twice the muscle mass but mice with the follistatin transgene and suppressed myostatin had four times as much muscle mass compared to the control group. Administering FS344 via a small virus (re: adeno-associated virus/AAV) can increase muscle size and strength in animal species ranging from mice to monkeys with no significant adverse effects on organs, reproductive capabilities, serum estradiol (re: primary female sex hormone), luteinizing hormone (LH), and FSH levels. When scientists administered follistatin in mice with spinal muscular atrophy, the mice experienced increased muscle mass, improved motor function, and a 30% longer lifespan compared to mice in the control group. Not only do increased follistatin levels correlate to increased muscle mass, but a lack of the follistatin protein at birth directly correlates to less muscle mass. Less muscle mass at birth can negatively impact bone, organ, and tissue development as well as normal hormonal function.

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