BPC 157
Visit Peptides for Sale for BPC 157 Buy online today at Peptides for Sale. BPC 157 comes in a small sterile container containing 5mg of BPC 157.
BPC 157 is also known as the following:
Booly protection compound 15, Bpc-157, BPC-15, BPC 157, BPC 15; UNII-8ED8NXK95P
Chemical Structure
Chemical Sequence
Gly-Glu-Pro-Pro-Pro-Gly-Lys-Pro-Ala-Asp-Asp-Ala-Gly-Leu-Val
Chemical Formula
C62H98N16O22
Molar mass
1419.556 g/mol
Description
Body Protection Compound-157, or Bpc 157, is a pentadecapeptide which is 15 amino acids. The amino acid’s sequence in BPC157 is similar to a portion of the human BPC amino acid sequence, found in the gastric juice.
Studies
Experiments have shown that BPC-157 enhances the healing of wounds, including tendons wounds such as transected Achilles tendons of rats. The aim of this study was to investigate the probable mechanism that it utilizes to accelerate the healing process in an injured tendon. Two groups of explants were studied. The first group, cultured in a bpc 157 containing medium, the other group was cultured in a medium lacking the body protection compound. The cultures were examined for tendon fibroblasts outgrowths. This indicated tendon regeneration. The explants’ outgrowth was significantly accelerated in the culture containing BPC157 as compared to the culture lacking BPC157.
Also, a MTT assay did show that BPC157 does not directly affect cellular proliferation in a culture of rat-derived Achilles tendon. However, results also showed that bpc 157 significantly increased the survival of cells under oxidative stress. Furthermore, the Transwell filter migration assay showed that BPC-157 significantly increased in-vitro fibroblast migration in a dose-dependent fashion. Moreover, bpc 157 accelerated the dispersal of the fibroblasts in culture dishes in a dose-dependent manner.
Additionally, FITC-phalloidin staining was able to demonstrate that BPC157 induces F-actin formation in fibroblasts. Likewise, Western blot analysis was able to detect the production and activation of paxillin and FAK proteins. The western blot analysis also showed that it increases the extent of phosphorylation of paxillin and FAK proteins without affecting the amounts produced.
In conclusion, BPC157 enhances the ex-vivo growth and in-vitro cellular migration of fibroblasts derived from rat tendon explants. BPC157 also increases the probability of a cell surviving under oxidative stress. The activation (through phosphorylation) of the proteinic FAK-paxillin pathway mediate the actions of this peptide.
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