99% Purity Best Quality Pharmaceutical Bodybuilding Peptide Gdf-8
|FOB Price:||US $1 / Piece|
|Min. Order:||1 Piece|
|Min. Order||FOB Price|
|1 Piece||US $1/ Piece|
|Transport Package:||as for Customer′s Requirement|
|Payment Terms:||T/T, Western Union, Money Gram|
- Model NO.: GDF-8
- Customized: Non-Customized
- Suitable for: Elderly, Adult
- Purity: >99%
- Payment: Western Union, Moneygram, T/T
- Grade: Natural Plant Extract; Flavors & Fragrances
- Trademark: Shuangbojie
- Origin: China
- Powder: Yes
- Certification: ISO 9001
- State: Powder
- MOQ: 10vials
- Deivery: Within 24hours After Your Payment
- Storage: Shading, Confined Preservation
- Specification: USP/BP
- HS Code: 123456
|Product Name||GDF 8 Powder 1mg/vial Pharmaceutical Raw Materials High purity GDF-8(myostatin)|
|Application||Pharmaceutical raw materials|
|Assay||99.0% min||99. 3%|
|Loss on Drying||6.0%max.||4.80%|
|Acetate Content (HPIC)||12.0%max.||10.80%|
|Peptide Content (N%)||80.0%min.||88.00%|
|Amino Acid Composition||±10% of theoretical||Complies|
|Single Impurity (HPLC)||1.0%max.||0.85%|
The human FST gene is comprised of six exons spanning 5329 bp on chromosome 5q11.2 and gives rise to two main transcripts of 1122 bp (transcript variant FST344) and 1386 bp (transcript variant FST317). The first exon encodes the signal peptide, the second exon the N-terminal domain and exons 3-5 each code for a follistatin module. Alternative splicing leads to usage of either exon 6A, which codes for an acidic region in FST344 or exon 6B, which contains two bases of the stop codon of FST317 (Shimasaki et al., 1988).
Mature secreted follistatin protein exists in three main forms consisting of 288, 303, and 315 amino acids (Sugino et al., 1993). The FST344 transcript gives rise to a protein precursor of 344 amino acids, which results in the mature 315 amino acid form after removal of the signal peptide. A fraction of follistatin 315 is further converted to the 303 amino acid form by proteolytic cleavage at the C-terminus. Signal peptide removal of FST317 leads to the mature 288 amino acid form of follistatin. All forms of follistatin contain three follistatin domains (FSD) characterized by a conserved arrangement of 10 cysteine residues. The N-terminal subdomains of the FSD have similarity with EGF-like modules, whereas the C-terminal regions resemble the Kazal domains found in multiple serine protease inhibitors. The follistatin protein contains two potential N-glycosilation sites on asparagines 124 and 288.
The gene encoding myostatin was discovered in 1997 by geneticists Se-Jin Lee and Alexandra McPherron who produced a strain of mutant mice that lack the gene. These myostatin "knockout" mice have approximately twice as much muscle as normal mice. These mice were subsequently named "mighty mice".
Naturally occurring deficiencies of myostatin have been identified in cattle by Ravi Kambadur, whippets, and humans; in each case the result is a dramatic increase in muscle mass. A mutation in the 3' UTR of the myostatin gene in Texel sheep creates target sites for the microRNAs miR-1 and miR-206. This is likely to cause the muscular phenotype of this breed of sheep.
Human myostatin consists of two identical subunits, each consisting of 109 (NCBI database claims human myostatin is 375 residues long) amino acid residues. Its total molecular weight is 25.0 kDa. The protein is inactive until a protease cleaves the NH2-terminal, or "pro-domain" portion of the molecule, resulting in the active COOH-terminal dimer. Myostatin binds to the activin type II receptor, resulting in a recruitment of either coreceptor Alk-3 or Alk-4. This coreceptor then initiates a cell signaling cascade in the muscle, which includes the activation of transcription factors in the SMAD family - SMAD2 and SMAD3. These factors then induce myostatin-specific gene regulation. When applied to myoblasts, myostatin inhibits their differentiation into mature muscle fibers.
Myostatin also inhibits Akt, a kinase that is sufficient to cause muscle hypertrophy, in part through the activation of protein synthesis. However, Akt is not responsible for all of the observed muscle hyperthrophic effects which are mediated by myostatin inhibition Thus myostatin acts in two ways: by inhibiting muscle differentiation, and by inhibiting Akt-induced protein synthesis.
A technique for detecting mutations in myostatin variants has been developed. Mutations that reduce the production of functional myostatin lead to an overgrowth of muscle tissue. Myostatin-related muscle hypertrophy has an incomplete autosomal dominance pattern of inheritance. People with a mutation in both copies of the MSTN gene in each cell (homozygotes) have significantly increased muscle mass and strength. People with a mutation in one copy of the MSTN gene in each cell (heterozygotes) have increased muscle bulk, but to a lesser degree.
In 2004, a German boy was diagnosed with a mutation in both copies of the myostatin-producing gene, making him considerably stronger than his peers. His mother has a mutation in one copy of the gene. An American boy born in 2005 was diagnosed with a clinically similar condition but with a somewhat different cause: his body produces a normal level of functional myostatin; but, because he is stronger and more muscular than most others his age, it is believed that a defect in his myostatin receptors prevents his muscle cells from responding normally to myostatin. He appeared on the television show, World's Strongest Toddler.
Further research into myostatin and the myostatin gene may lead to therapies for muscular dystrophy. The idea is to introduce substances that block myostatin. A monoclonal antibody specific to myostatin increases muscle mass in mice and monkeys.
A two-week treatment of normal mice with soluble activin type IIB receptor, a molecule that is normally attached to cells and binds to myostatin, leads to a significantly increased muscle mass (up to 60%). It is thought that binding of myostatin to the soluble activin receptor prevents it from interacting with the cell-bound receptors.
It remains unclear as to whether long-term treatment of muscular dystrophy with myostatin inhibitors is beneficial, as the depletion of muscle stem cells could worsen the disease later on. As of 2012, no myostatin-inhibiting drugs for humans are on the market. An antibody genetically engineered to neutralize myostatin, stamulumab, which was under development by pharmaceutical company Wyeth., is no longer under development. Some athletes, eager to get their hands on such drugs, turn to the internet where fake "myostatin blockers" are being sold.
Myostatin levels are effectively decreased by creatine supplementation.
Inhibition of myostatin leads to muscle hyperplasia and hypertrophy. Myostatin inhibitors can improve athletic performance and therefore there is a concern these inhibitors might be abused in the field of sports. However, studies in mice suggest that myostatin inhibition does not directly increase the strength of individual muscle fibers.
Grape seed oil
Alias: Vitis vinifera
CAS Registry Number: 8024-22-4
Einecs No: 287-896-9
Grade: Natural Plant Extract; Flavors & Fragrances
Storage: Shading, confined preservation
Grape seed oil (also called grapeseed oil or grape oil) is pressed from the seeds of grapes, and is thus an abundant by-product of winemaking.
Grape seed oil is a preferred cosmetic ingredient for controlling moisture of the skin. Light and thin, grape seed oil leaves a glossy film over skin when used as a carrier oil for essential oils in aromatherapy. It contains more linoleic acid than many other carrier oils. Grape seed oil is also used as a lubricant for shaving. Grape seed oil is also used as a growth and strengthening treatment for hair.
|BOTANICAL NAME:||Vitis vinifera L|
|PART OF PLANT USED:||Seed|
|ORIGIN OF RAW MATERIAL:||China|
|COUNTRY OF PROCESSING:||China|
|APPEARANCE||Light yellow or green liquid, with grapeseed oil's peculiar smell and taste||STM 01.010|
|ACID VALUE, KOH mg /g:||≤2.0||AOCS Cd 3d-63|
|PEROXIDE VALUE, meq/kg:||≤10.0||AOCS Cd 8b-90|
|SAPONIFICATION VALUE,KOH mg /g:||188-194||AOCS Cd 3-25|
|INSOLUBLE IMPURITY, %(m/m):||≤0.05||AOCS Ca 3a-46|
|UNSAPONIFIABLE MATTER, %||≤2.0||AOCS Ca 6a-40|
|MOISTURE AND VOLATILES, %:||≤0.20||AOCS Ca 2d-25|
|GARDNER COLOR||≤5||AOCS Td 1a-64|
|COLD TEST||Clear after 5.5 hours at 0°C||AOCS Cc 11-53|
|RESIDUAL SOLVENT, mg/kg:||Negative||AOCS Ba 14-87|
|LEAD ppm||≤0.05||AOCS Ca 18c-91|
|ARSENIC ppm||≤0.1||AOAC 986.15|
|CADMIUM ppm||≤0.01||AOAC 986.15|
|MERCURY ppm||≤0.005||AOAC 971.21|
|FATTY ACID COMPOSITION||AOCS Ce 1e-91|
|C:14:0 MYRISTIC %||0-0.3|
|C:16:0 PALMITIC %||5.5-11.0|
|C:18:0 STEARIC %||3.0-6.5|
|C:18:1 OLEICO %||12.0-28.0|
|C:18:2 LINOLEIC %||58.0-78.0|
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