Fs344 Peptide Follistatin 315 Green Caps

Bodybuilding Peptide Follistatin 344
Ace 031 1mg /Vial
Follistatin-315
White Lyophilized Powder Follistatin 315
Peptide Follistatin 315
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Fs344 Peptide Follistatin 315 Green Caps for Bodybuilding 

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Follistatin 315 Contact Mitchell: Whatsapp +8618124076819 Skype: hk@chembj.com

Bodybuilding Peptide Follistatin 344

Ace 031 1mg /Vial

Follistatin-315

White Lyophilized Powder Follistatin 315

Peptide Follistatin 315
Follistatin 315  price
FST 315 1mg/Vial


Quick Details:
Other name: Follistatin 315 / FST 315
Specification: ( 1mg/vial, 10vial/box )
Standard: USP Grade
Purity: Greater than 99.9%
Appearance: Sterile Filtered White lyophilized (freeze-dried) powder.
Vails : 1mg/vail


Follistatin 315 Descriptions:
Follistatin  will remain stable at room temperature for up to 90 days. Ideally it should be stored in a freezer at or below -9C. Follistatin should be refrigerated after reconstitution.


Follistatin 315 Application:
Follistatin is fascinating protein that can increase muscle mass beyond natural potential by suppressing myostatin. Scientists first identified follistatin while examining porcine (re: pig) follicular fluid in the ovaries.
Follistatin is naturally found in the skeletal muscle of almost all mammals with advanced or developed characteristics, such as humans, rodents, and cows. Follistatin is high in the non-essential amino acid cystine but unlike most proteins discussed in the fitness world, follistatin has carbohydrates attached to it.

Dosage Example for a 10 day cycle:

Day 1: Split bilaterally into the muscle you want to bring up the most: 300mcg.
Day 3: Split bilaterally into the muscle you want to bring up the most: 200mcg.
Day 5: Split bilaterally into the muscle you want to bring up the most: 200mcg.
Day 7: Split bilaterally into the muscle you want to bring up the most: 300mcg.
The muscle building effects can last for up to 3 months afterwards, slowly diminishing.
 
The recommended duration of the course of 30 days.
Total vials on one course - 2 Follistatin 344 vial to 1 mg of active ingredient each. Makes 1 injection per day in the morning for 100 mcg subcutaneously in the abdominal oblique muscles. Peptide may be used locally. There are versions that in this case the drug increases the target muscle to a greater extent than others. After 10 days of use is the same 10-day break. After this break, it is recommended to start a new 10-day cycle.

Description of  Follistatin 315 :

Follistatin (FST) is a secreted glycoprotein that was first identified as a follicle stimulating 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 Specifications:

Appearance

White to off white powder

Consistent

Purity(HPLC)

≥98%

99%

Water

<6.0%

5.43%

Acetic Acid

3.0-8.0%

6.45%

Trifluoroacetic Acid

<0.25%

0.08%

Peptide

≥80%

88.45%

MS

Consistent

Consistent

Follistatin and Muscle Growth:

Follistatin works by binding to and inhibiting transforming growth factr- (TGF-) 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). [1] 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.

What are Peptides?

Peptides are biologically appearing short chains of amino acid monomers bridged by peptide (amide) bonds.

The covalent chemical bonds are constructed when the carboxyl family of one amino acid performs with the amine family of another. The shortest peptides are dipeptides, inculding 2 amino acids joined by a single peptide bond, followed by tripeptides, tetrapeptides, etc. Polypeptides are long, consistent, and unbranched peptide chains. Thus, peptides fall under the broad chemical series of biological oligomers and polymers, along with nucleic acids, oligosaccharides and polysaccharides, etc.

Peptides are diffrentiated from proteins on the basis of size, and as an arbitrary benchmark can be understood to have approximately 50 or fewer amino acids.  Proteins consist of one or more polypeptides organized in a biologically functional way, often bound to ligands such as coenzymes and cofactors, or to another protein or other macromolecule (DNA, RNA, etc.), or to complicated macromolecular assemblies.  Finally, while aspects of the lab techniques utilized to peptides versus polypeptides and proteins divers (e.g., the specifics of electrophoresis, chromatography, etc.), the size boundaries that distinguish peptides from polypeptides and proteins are not absolute: long peptides such as amyloid beta have been referred to as proteins, and smaller proteins like Arginine have been regarded as peptides.

Amino acids that have been incorporated into peptides are called "residues" due to the release of either a hydrogen ion from the amine end or a hydroxyl ion from the carboxyl end, or both, as a water molecule is released during formation of each amide bond. All peptides except cyclic peptides have an N-terminal and C-terminal impurity at the end of the peptide (as shown for the tetrapeptide in the image).

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