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Home » Research Catalogue » Structural Research Peptides » BPC-157 Research Reference
Molecular Weight
Purity
Storage
Appearance
Solubility
01
BPC-157 (“Body Protection Compound-157”) is a synthetic 15-residue peptide, Gly-Glu-Pro-Pro-Pro-Gly-Lys-Pro-Ala-Asp-Asp-Ala-Gly-Leu-Val. Its sequence corresponds to part of a protein originally described in human gastric juice.
Structurally, it is notable for a cluster of prolines near the N-terminus, an Asp-Asp pair near the C-terminus, and the absence of aromatic residues. These features make it a useful model peptide for chromatography and degradation studies. In published cell-culture work it has been examined in signalling and cell-migration models, although its direct molecular target has not been identified. It is supplied as a lyophilized reference material for in vitro research only, and no biological function is claimed for it here.
02
BPC-157’s short, unmodified sequence has several features that shape its behaviour.
Proline cluster (Pro3–Pro5, plus Pro8)
Three consecutive prolines restrict backbone flexibility and favour an extended, polyproline II-type conformation over part of the chain. Prolines also undergo slow cis–trans isomerisation, which can affect chromatographic peak shape.
Acidic residues (Glu2, Asp10, Asp11)
Together with the C-terminal carboxylate, these give the peptide a net charge of about −2 at pH 7.4. The adjacent Asp10-Asp11 pair is its main chemical weak point.
Lys7
The only basic side chain, giving an uneven charge distribution along the chain.
No aromatic residues
With no tryptophan, tyrosine or phenylalanine, UV detection relies on the peptide bond (around 214 nm); absorbance at 280 nm is negligible.
Unmodified termini
The N-terminus is a free amine and the C-terminus is a free acid (Val15-OH). There is no methionine, cysteine, asparagine or glutamine.
03
Published in vitro studies have examined BPC-157 in several cell-based models.
Nitric oxide signalling
Endothelial cell studies have reported changes in nitric oxide production, with effects that vary between experimental systems and concentrations.
Growth factor signalling
Studies in endothelial and fibroblast cultures have reported changes in VEGFR2 phosphorylation and related pathways, without identifying a direct binding partner.
Cell migration
Scratch-wound and migration assays have examined focal adhesion kinase (FAK) and paxillin signalling and cytoskeletal changes after treatment.
These observations come from controlled in vitro systems and do not establish function in living organisms. How a short peptide without a known receptor-binding motif influences these pathways remains an open research question.
04
Proline-peptide chromatography
A reference compound for reversed-phase methods for proline-rich peptides, where cis–trans isomerisation can cause broadened or split peaks.
Degradation model
Its Asp10-Asp11 pair makes it a practical model for studying aspartimide formation, isoaspartate formation and Asp-related backbone cleavage under stress.
Cell-based studies
Used at defined concentrations in migration, scratch-wound and tube-formation assays in cultured cells.
Mass spectrometry reference
Its moderate size and proline-directed fragmentation make it a convenient check compound for LC-MS methods.
05
Storage
Store the lyophilized powder at −20 °C, sealed and desiccated. Let the vial reach room temperature before opening.
Asp-Asp chemistry
The Asp10-Asp11 pair is the main degradation site. Aspartimide formation and conversion to isoaspartate are fastest in the mildly acidic range (around pH 4–6) and at higher temperatures, while strongly acidic conditions (below about pH 3) mainly promote backbone cleavage next to aspartate. Near-neutral pH and cold storage minimise both.
Reconstitution
Readily soluble in water or near-neutral buffer, and also in dilute acetic acid. Choose the solvent to suit the experiment and use solutions promptly.
Proline isomers
In solution, slow cis–trans isomerisation at the proline bonds can produce closely eluting conformers. These are not impurities and usually merge at higher column temperatures.
Solutions
Divide into single-use aliquots in low-binding polypropylene tubes and freeze; avoid repeated freeze–thaw cycles.
06
BPC-157’s composition determines how it is detected and which impurities matter.
HPLC
Reversed-phase C18 with 0.1% TFA in water/acetonitrile normally gives one main peak. If peaks are broad or split, raising the column temperature reduces proline isomer effects. Detect at 214 nm.
Mass spectrometry
Positive-mode ESI-MS shows [M+2H]²⁺ at m/z 710.4 and [M+3H]³⁺ at m/z 473.9 (monoisotopic). MS/MS gives proline-directed b- and y-ion series for sequence confirmation.
Isoaspartate detection
Isoaspartate forms have the same mass as the parent peptide and often elute very close to it, so they need an optimised HPLC method or specific techniques such as enzymatic isoAsp assays.
Impurity profile
Typical checks include isoAsp10 and isoAsp11 variants, Asp-related cleavage fragments, deletion and truncated sequences from synthesis, and residual counter-ion content.
07
Gly-Glu-Pro-Pro-Pro-Gly-Lys-Pro-Ala-Asp-Asp-Ala-Gly-Leu-Val (GEPPPGKPADDAGLV), 15 residues with a free N-terminal amine and a free C-terminal acid.
Its proline cluster (Pro3–Pro5, plus Pro8), which makes part of the chain rigid and extended, combined with an Asp-Asp pair and no aromatic residues. These features affect its chromatography, UV detection and stability.
The Asp10-Asp11 pair. It can form an aspartimide ring and convert to isoaspartate, fastest at mildly acidic pH (around 4–6) and higher temperatures, and can undergo backbone cleavage under strongly acidic conditions. There is no methionine, cysteine, asparagine or glutamine.
BPC-157 is most often combined with TB-500, and some multi-peptide blends also include GHK-Cu and other peptides. Check the blend listings in this catalogue for the exact composition of each product.
Because BPC-157 is only 15 residues long, MS/MS of the intact peptide can usually cover the full sequence without digestion. Full b- and y-ion coverage, with accurate intact mass, is a reasonable target for identity confirmation.
It contains no tryptophan, tyrosine or phenylalanine, so it absorbs almost nothing at 280 nm. Detection relies on the peptide bond at around 214 nm.
No. It is supplied strictly as a reference compound for laboratory and analytical research and is not for human or animal use.
BPC-157 Research Reference. (2026). Pure Peptides Labs Research Catalogue. Retrieved from https://purepeptideslabs.net/research-catalogue/structural-research-peptides/bpc-157/
Materials listed on this platform are supported by independent testing and published documentation for laboratory research contexts.