BPC-157 Molecular Profile: CAS Number, Formula, and Amino Acid Sequence

BPC-157 is a synthetic pentadecapeptide studied in preclinical research for its interactions with gastric mucosal, vascular, and connective tissue systems. In laboratory models, it has been investigated for modulation of nitric oxide signaling and VEGFR2-associated angiogenic pathways. CAS 137525-51-0, molecular weight ~1419.5 Da, sequence GEPPPGKPADDAGLV.

Chemical Properties Table

Analytical Identification

Laboratories verifying BPC-157 batch identity typically rely on a combination of reversed-phase HPLC for purity assessment and mass spectrometry (MS) for molecular weight confirmation against the theoretical mass of ~1,419.5 Da. Amino acid analysis or Edman degradation sequencing can additionally confirm the GEPPPGKPADDAGLV sequence order, which is useful when comparing peptide lots across suppliers or synthesis batches. Reported molecular weight can vary slightly (1419.53–1419.56 g/mol) among analytical sources, depending on the degree of hydration in a given batch, which is a known source of minor discrepancies when comparing certificates of analysis across manufacturers.

What Is BPC-157?

BPC-157, short for Body Protection Compound-157, is a synthetic 15-amino-acid peptide fragment. Its sequence is derived from a segment of a partial peptide originally isolated from human gastric juice.

Unlike full-length endogenous proteins, BPC-157 is a stable, short-chain synthetic construct designed for reproducibility across laboratory research settings. Its short sequence length and defined structure make it a common reference compound in studies examining pentadecapeptide behavior in cellular and tissue models.

In research contexts, BPC-157 Peptide is classified as a non-approved investigational peptide. It is not evaluated or approved by the FDA for any human therapeutic indication, and no clinical dosing standard exists.

BPC-157 belongs to a broader class of gastric-derived regulatory peptides that researchers use as tools for probing mucosal defense mechanisms. Within this class, it is distinguished by its short 15-residue length relative to larger endogenous gastric peptides, which makes synthesis and batch-to-batch analytical consistency more straightforward for laboratory suppliers.

WADA Status: BPC-157 is listed under the WADA prohibited list category S0 (Non-Approved Substances), relevant to anti-doping research and detection-method development contexts.

2026 Regulatory Update: In April 2026, BPC-157 (both free base and acetate forms) was removed from the FDA's 503A Category 2 restricted compounding list. Removal from Category 2 is a distinct regulatory step from authorization to compound — the FDA's Pharmacy Compounding Advisory Committee (PCAC) was scheduled to review BPC-157, alongside several other peptides, for potential addition to the Section 503A bulk drug substances list at a hearing on July 23, 2026. A favorable PCAC recommendation would still require formal FDA rulemaking, including a public comment period, before taking effect. This status change affects compounding pharmacy regulation specifically and does not alter BPC-157's classification for laboratory research use — RCDbio's BPC-157 products remain for laboratory and research purposes only and are not authorized for human administration.

Amino Acid Sequence and Structural Notes

BPC-157's 15-residue chain includes three consecutive proline residues near the N-terminus (Pro-Pro-Pro), a structural feature associated with conformational rigidity in short peptide chains. This proline-rich segment is thought to contribute to the peptide's resistance to enzymatic degradation relative to many other short-chain peptides studied in gastric and vascular research models.

The C-terminal region carries a paired aspartic acid motif (Asp-Asp) followed by Ala-Gly-Leu-Val, contributing acidic character to that portion of the molecule. Researchers examining structure-activity relationships in pentadecapeptides often reference this sequence when comparing stability and receptor-interaction profiles against other gastric-derived peptide fragments.

BPC-157 does not contain a cysteine residue, meaning it lacks disulfide bridging — its structural stability in solution is attributed instead to the proline-driven backbone conformation described above.

The compound is also referenced in older literature under the designations PL 14736 and PL-10, names used during earlier phases of its investigational history before "BPC-157" became the standard identifier in preclinical publications. Some suppliers also list the acetate salt form (CAS 1628202-19-6) alongside the free-base form (CAS 137525-51-0); researchers should note which salt form a given batch represents, since salt content affects the peptide's effective mass per milligram of lyophilized powder.

One structural property that has drawn particular research interest is BPC-157's apparent resistance to gastric enzymatic breakdown relative to other short peptide fragments. Because BPC-157 originates from a segment of gastric juice protein, researchers have examined whether its proline-rich N-terminal region confers partial protection against pepsin and other proteolytic enzymes present in the gastric environment. This property has made BPC-157 a reference point in structure-stability studies comparing how sequence composition — particularly proline placement and the absence of easily cleaved peptide bonds — influences a short peptide's half-life in enzymatically active in vitro systems. Findings in this area remain model-specific, and stability observed in isolated enzymatic assays does not necessarily predict behavior in more complex biological matrices.

Research Context

BPC-157 is studied primarily within three preclinical research domains:

• Gastrointestinal mucosal models — used to examine epithelial barrier dynamics and mucosal integrity pathways in rodent models. Researchers in this domain frequently reference BPC-157 alongside other gastroprotective peptide fragments when characterizing mucosal defense mechanisms.

• Vascular and angiogenesis research — investigated for interaction with VEGFR2 signaling and nitric oxide synthase (eNOS) activity in endothelial cell cultures and isolated vessel preparations. This line of research has extended to Src-Caveolin-1-eNOS signaling as a parallel pathway distinct from the classical VEGFR2-Akt-eNOS cascade. This alternate route represents a non-receptor-dependent path to nitric oxide upregulation, which researchers use as a tool to separate NO-dependent effects from VEGFR2-dependent effects within a given experimental model.

• Connective tissue and fibroblast models — used in tendon and ligament explant studies examining fibroblast migration, F-actin formation, and cell survival under oxidative stress conditions.

Findings across these models are not consistent across all species or tissue types, and data from in vitro systems do not necessarily translate to in vivo outcomes. BPC-157 remains an active subject of mechanistic characterization rather than a compound with an established, agreed-upon primary receptor target.

Research Volume: A 2025 systematic review by Vasireddi et al. (published in HSS Journal) searched PubMed, Cochrane, and Embase and identified 544 total database entries referencing BPC-157 published between 1993 and 2024. After removing duplicates and screening for relevance, 36 studies met inclusion criteria — 35 preclinical and 1 clinical. The review's scope centered on musculoskeletal and orthopedic sports-medicine research; it reported preclinical improvements in functional, structural, and biomechanical outcomes in muscle, tendon, ligament, and bone injury models, while noting that clinical safety data remain limited to a single small retrospective study.

Related Compounds in Pentadecapeptide Research

Researchers comparing BPC-157 against other short-chain regulatory peptides often reference TB-500 (a synthetic fragment of thymosin beta-4) for parallel work in tissue repair models, or growth-hormone secretagogue peptides such as Ipamorelin when contrasting receptor-mediated versus non-receptor-mediated mechanisms of action. These comparisons are typically framed around differences in molecular weight, sequence length, and the specific signaling pathways each compound has been reported to interact with in published preclinical literature.

Frequently Asked Questions

What is the molecular weight of BPC-157?

BPC-157 has a molecular weight of approximately 1,419.5 g/mol (reported 1419.53–1419.56 across analytical sources), corresponding to the molecular formula C₆₂H₉₈N₁₆O₂₂ for the free-base pentadecapeptide.

Does BPC-157 have a CAS registry number?

Yes. The CAS number for BPC-157 free base is 137525-51-0. A separate CAS number (1628202-19-6) is used for the acetate salt form supplied by some manufacturers, so researchers should confirm which salt form a CAS number refers to before comparing analytical data across suppliers.

What is the difference between BPC-157 free base and BPC-157 acetate salt?

Both forms contain the same 15-amino-acid sequence but differ in counterion content. The acetate salt carries acetate counter-ions that add mass per milligram of lyophilized powder, meaning effective peptide content per unit weight differs between the two forms. Researchers should confirm which form a given batch represents when preparing concentration-specific laboratory work.

What is the purity standard for research-grade BPC-157?

Research-grade BPC-157 is typically supplied at ≥98% purity by HPLC. A batch-specific Certificate of Analysis from a named third-party laboratory, confirming both HPLC purity and MS identity against the theoretical ~1,419.5 Da mass, represents standard documentation for procurement in analytical and preclinical research settings.

How is BPC-157 identified analytically in a research setting?

Laboratories typically confirm identity through mass spectrometry against the theoretical ~1,419.5 Da mass, combined with reverse-phase HPLC purity data and, where available, amino acid sequencing to confirm the GEPPPGKPADDAGLV chain order.

Is BPC-157 a receptor-targeted peptide?

Current preclinical literature has not established a single confirmed primary receptor for BPC-157. Research has instead focused on its association with signaling nodes such as VEGFR2, eNOS, and FAK-paxillin pathways across different tissue models, and findings vary by model system.

Is BPC-157 the same as PL 14736 or Bepecin?

Yes. PL 14736, Bepecin, PL-10, and BPC-157 all refer to the same 15-amino-acid peptide with CAS 137525-51-0 and molecular formula C₆₂H₉₈N₁₆O₂₂. PL 14736 and PL-10 were identifiers used during earlier phases of investigational history before "BPC-157" became the standard identifier in preclinical publications.

BPC-157 Peptide in stock at RCDbio →

PubMed References

1. Hsieh MJ, Liu HT, Wang CN, et al. The therapeutic potential of pro-angiogenic BPC157 is associated with VEGFR2 activation and up-regulation. J Mol Med (Berl). 2017;95(3):323-333. https://pubmed.ncbi.nlm.nih.gov/27847966/
   
   

2. Sikiric P, Barisic I, Udovicic M, et al. Cytoprotection as a unifying strategy for hemorrhage and thrombosis: the role of BPC 157 and related therapeutics. Pharmaceuticals (Basel). 2026;19(3):463. https://pubmed.ncbi.nlm.nih.gov/41901308/
   
   

BPC-157 Peptide in stock at RCDbio →

This article is for research and educational purposes only. All compounds described are for laboratory use only and are not approved by the FDA for human use. RCDbio products are not intended to diagnose, prevent, treat, or cure any disease or medical condition.

Last Reviewed: July 6, 2026 | Prepared for laboratory research reference only.

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