BPC-157 Molecular Weight, Sequence & CAS Reference

Chemical Identity and Structural Overview of BPC-157

BPC-157, chemically designated as Body Protection Compound 157, is a synthetic pentadecapeptide derived from a naturally occurring partial sequence of human gastric juice protein. In basic chemical literature, it is categorized as a tissue repair research compound evaluated in preclinical models for its role in cellular migration, extracellular matrix remodeling, and microvascular stabilization. To maintain strict analytical reproducibility, laboratory investigators must verify the chemical specifications, primary structure, and salt-form variations of the peptide prior to assay integration.

When purchasing high-purity research materials through our all-peptides catalog, evaluating structural parameters ensures that in vitro assays and animal model trials maintain controlled concentrations. PX1 Research synthesizes BPC-157 utilizing automated solid-phase peptide synthesis (SPPS), yielding a sequence-defined, highly purified compound suitable for demanding biochemical assays.

Primary Amino Acid Sequence and Molecular Structure

The primary sequence of BPC-157 consists of 15 L-amino acid residues arranged in a specific linear conformation. The single-letter amino acid code for BPC-157 is H-GEPPP-GKPADDAGLV-OH, while the complete three-letter amino acid sequence is represented as:

H-Gly-Glu-Pro-Pro-Pro-Gly-Lys-Pro-Ala-Asp-Asp-Ala-Gly-Leu-Val-OH

The N-terminus of the peptide terminates with an unblocked free amine (Glycine), and the C-terminus terminates with a standard free carboxylic acid group (Valine). The presence of three sequential proline residues near the N-terminal region confers unique conformational flexibility and structural stability in aqueous buffers, influencing how the peptide interacts with extracellular matrix proteins and cell-surface receptors in cell culture models.

Molecular Formula, Exact Mass, and CAS Identification

For accurate analytical stoichiometry and mass spectrometry verification, researchers must reference the verified chemical formula and monoisotopic molecular weight of the unprotonated free base:

Chemical Formula: C62H98N16O22 Monoisotopic Mass: 1418.6963 Da Average Molecular Weight: 1419.53 g/mol CAS Registry Number: 137525-51-0

The CAS Registry Number 137525-51-0 uniquely identifies the chemical structure of the BPC-157 free base sequence. When evaluating synthesized batches via High-Performance Liquid Chromatography (HPLC) coupled with Mass Spectrometry (MS), the primary [M+H]+ ion peak typically resolves at m/z 1420.5 (±0.5 Da), confirming the identity and structural integrity of the synthesized pentadecapeptide.

Salt Counter-Ions and Net Peptide Content Dynamics

Lyophilized research peptides are rarely isolated as pure free bases; rather, they are synthesized and purified in salt forms due to the protonation of basic amino acid residues (such as Lysine) and the N-terminal amine. BPC-157 is primarily produced in two distinct salt forms: Trifluoroacetate (TFA) salt and Acetate salt, though L-Arginine salt complexes (BPC-157 L-Arginate) are also investigated in specific stability studies.

The salt counter-ion adds distinct mass to the overall bulk product, directly influencing the calculation of Net Peptide Content (NPC). While analytical HPLC purity reports the percentage of the target peptide sequence relative to peptide impurities (e.g., >98%), NPC reports the actual weight percentage of the peptide molecule relative to counter-ions, residual water, and trace salts.

For example, a vial containing 5 mg of BPC-157 TFA salt with a 98.5% HPLC purity may have a Net Peptide Content of 80% to 85%. In this scenario, the total weight of pure BPC-157 peptide in the vial is approximately 4.0 mg to 4.25 mg, with the remaining mass composed of trifluoroacetate counter-ions and bound hydration water. For exact batch-specific NPC values and counter-ion profiles, researchers can consult the lot-specific certificate of analysis via our COA lookup.

Biological Mechanisms in Preclinical Models

In preclinical laboratory research, BPC-157 has been widely studied for its involvement in cellular repair signaling pathways. In vitro assays demonstrate that the peptide upregulates the expression of vascular endothelial growth factor receptor 2 (VEGFR2) and activates the focal adhesion kinase (FAK)-paxillin pathway. These intracellular signaling cascades drive endothelial cell migration, capillary tube formation, and accelerated angiogenesis at lesion sites.

Rodent models of tissue trauma show that BPC-157 administration correlates with accelerated repair across diverse tissue types, including tendon, ligament, skeletal muscle, and gastrointestinal mucosal lining. Preclinical findings suggest that the compound promotes fibroblast proliferation, enhances type I collagen synthesis, and blunts acute pro-inflammatory cytokine cascades, establishing a favorable microenvironment for structural matrix regeneration.

Comparative Analysis: BPC-157 vs. Related Repair Peptides

To contextualize BPC-157 within the broader landscape of preclinical tissue regeneration compounds, researchers frequently compare its sequence and mechanism to other regulatory peptides. While BPC-157 operates primarily via VEGFR2 activation and local extracellular matrix organization, compounds such as TB-500 (a synthetic fragment of Thymosin Beta-4) promote actin sequestration and cell motility.

Similarly, GHK-Cu modulates copper-dependent enzyme pathways to stimulate collagen synthesis and remodeling, whereas KPV exhibits potent anti-inflammatory activity via NF-κB pathway suppression. The table below highlights key chemical differences across these benchmark research compounds:

Laboratory Solubilization, Handling, and Reconstitution

BPC-157 exhibits favorable aqueous solubility due to its polar amino acid residues, including Glutamic Acid, Lysine, and Aspartic Acid. For laboratory reconstitutions, sterile bacteriostatic water or sterile 0.9% sodium chloride solution is recommended. When preparing stock solutions for cell culture or enzymatic assays, investigators should reconstitute the lyophilized powder under a laminar flow hood using aseptic techniques.

To calculate exact solvent volumes and target concentrations for volumetric assays, researchers can utilize the PX1 reconstitution calculator. Stock solutions should be aliquoted into polypropylene microcentrifuge tubes and stored at -20°C or -80°C to prevent degradation from freeze-thaw cycles. To purchase research-grade material manufactured under GMP-compliant parameters, visit the official BPC-157 product page.

Analytical Quality Assurance and Verification at PX1 Research

High-rigor preclinical research demands strict chemical verification of peptide reagents. Every lot of BPC-157 supplied by PX1 Research undergoes rigorous analytical verification within ISO 17025 accredited testing facilities located in the USA.

Analytical procedures include reverse-phase HPLC (RP-HPLC) to establish purity (>98%), Electrospray Ionization Mass Spectrometry (ESI-MS) to verify molecular weight sequence identity, and Kinetic Chromogenic LAL testing to ensure endotoxin levels remain strictly below <0.01 EU/mg. Institutional buyers looking for bulk manufacturing contracts or dedicated analytical documentation can review options on our wholesale account portal.