Month: August 2014

Download or view the PDF version of this article by clicking here

Click here to view our entire peptide selection

SNAP-8 is a peptide whose full name is Synaptososomal-associated protein 25.  As its name might suggest, the protein SNAP-8 is considered to be an octapeptide.  This means that it is a protein fragment that is comprised of eight amino acids that are linked in a polypeptide chain.  Its molecular formula is C₁₄H₇₀N₁₆O₁₆S, and it possesses a molecular weight of 1075.16.  When it is used in conjunction with scientific study on animal test subjects, it typically has an appearance of a white powder, although it can also be administered to an animal test subject via a transparent solution.  It has also been determined that it works best for scientific study when it is stored desiccated below -18 ° C, and that it should be stored at 4 ° C up to three weeks for future usage upon reconstitution.  Typically, the shelf-life of the peptide is twelve months, but can be extended to up to eighteen months under the proper storage conditions.

Function of SNAP-8

Scientific study based on animal test subjects has determined that the primary function of SNAP-8 is to act as a muscle contraction inhibitor.  This act of inhibition allows for muscles to achieve a more consistent level of homeostasis, as it allows for the neurotransmitters that are responsible that are responsible for bringing about homeostasis to be released on a much more efficient basis.

SNAP-8 and SNAP-25

According to scientific study that has been conducted on animal test subjects, it has been determined that SNAP-8 works in relation to the protein SNAP-25.  Also known as Synaptosomal-associated protein 25, SNAP-25 is what is known as a t-SNARE protein.  T-Snares are part of a large protein superfamily containing more than 60 members; in this case, it is proposed to account for the specificity of membrane fusion and to specifically carry out fusion by forming a tight complex that joins the synaptic vesicle and plasma membranes together.

Specifically, SNAP-25 is a membrane bound protein that is connected to the cytosolic face of membranes through the palmoitoyl side chains in the middle of the molecule.  In other words, it the protein forms a covalent bond within the cell through its liquid matrix.  It works to block P/Q and L-type voltage-gated calcium channels, which are groups of ion channels that possess permeability to the calcium ion Ca²⁺.  The activation of these channels allows the ion to rush inside of the cell, which could produce various results depending on the cell type.

Some of the results include:

• The activation of calcium-sensitive potassium channels
• Excitation of neurons
• A boost in the regulation of gene expression
• The release of hormones
• The release of neurotransmitters
• Muscular contraction

In the case of muscles, SNAP-25’s ability to regulate muscular contraction through the activation of the Ca²⁺ ion allows animal test subjects to experience a level of homeostasis in terms of muscular contraction and ultimately muscular performance.

The downside to SNAP-25 is that when it becomes destabilized in the slightest, the cellular unit cannot release the proper neurotransmitters that would properly signal the activation of muscular contraction.  As a result of this, the consistent level of muscular contraction is disrupted.  When this degradation of performance occurs, the muscles respond by forming lines and wrinkles within animal test subjects.  Scientific study that has been conducted on animal test subjects has noted that this physical reaction to the degradation is most prominent around the eyes and the face.

According to scientific study that has been based on animal test subjects, SNAP-8 functions by boosting the regulatory functions of the N-terminal end of SNAP-25.  This elevation allows for the SNARE complex to stay stabilized, which in turn allows for SNAP-25 to remain stabilized for a significantly longer period of time.  At the same time, SNAP-8 has been shown to inhibit the release of catecholamine, which is a general class of neurotransmitters that are derived from the amino acid tyrosine containing catechol and amine groups.  This blockage also contributes to the stabilizing process in terms of the regulation of muscular contraction through the activation of the Ca²⁺ ion.

SNAP-8 and Acetyl hexapeptide-3

Scientific studies that have been based on animal test subjects have determined that the presence of SNAP-8 acts similarly to acetyl hexapeptide-3, which is a peptide that is derived from a fragment of SNAP-25.  The two peptides differ in structure, as SNAP-8 is considered to be an octapeptide as opposed to a hexipeptide.  Clinical studies on animal test subjects have determined that SNAP-8’s stabilizing functionality tends to work with more efficiency than its hexipeptide counterpart.

Click here to read SNAP-8 – Part 2

Download or view the PDF version of this article by clicking here

Follistatin 344 and Muscle Mass

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.

No Side Effects

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.

Purely for Scientific Research

Despite the fact that there has been a significant amount of research on Follistatin 344 in relation to how it functions as well as the benefits that can be derived from such functionality, it should be emphasized that the peptide is still just intended for scientific study on animal test subjects at this point in time.  All matters of research that relate to the way in which Follistatin 344 operates and functions has all been culled from scientific study that has been done on animal test subjects.  As a result of this, any findings or observations that can be tied to Follistatin 344’s overall functionality, operational mechanics, potential benefits, and potential side effects should exclusively be the product of study performed in a strictly contained environment such as a medical research facility or a laboratory.

Click here to read Follistatin 344 – Part 1

Download or view the PDF version of this article by clicking here

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.

Operational Mechanics of Follistatin 344

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.

Follistatin 344 and the Life Cycle

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.

Click here to read Follistatin 344 – Part 2