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Product Usage: This PRODUCT IS INTENDED AS A RESEARCH CHEMICAL ONLY. This designation is allowed to use of research chemicals strictly for in vitro testing and laboratory experimentation only. All product information available on this website for educational purpose only. Bodily introduction of any kind into humans and animals is strictly forbidden by law. This product should only be handled by licenced qualified professionals. This product is not a drug, food, or cosmetic and may not be misbranded, misused as a drug, food and cosmetic.
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For this product you will need: BACTERIOSTATIC WATER For reconstitution.
BPC-157 is comprised of 15 amino acids and synthetically derived from a specific sequence of amino acids found on the same protein molecule referred to as “Body protective compound” (i.e BPC). From the molecular classification viewpoint, it is a peptide fragment model and has been employed in the laboratory environment for analytical and structural studies.
In non-clinical research settings, BPC-157 is employed as a reference compound for examining peptide stability characteristics, molecular interaction behaviour, and signalling pathway architecture within controlled experimental systems. Investigative work involving this peptide is limited to pathway mapping, signal correlation analysis, and evaluation of peptide-associated regulatory frameworks under reductionist laboratory conditions. These activities are conducted without attribution to physiological function, biological performance, or organism-level outcomes.
BPC-157 for sale on our website is supplied strictly for laboratory and research use only. It is not approved for human or animal use, and no clinical, diagnostic, therapeutic, or biological applications are expressed or implied.
From Pubchem
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Synonyms: BPC-15, Booly protection compound 15 Molecular Weight: 1419.5 g/molMolecular Formula: C62H98N16O22 Sequence: GEPPPGKPADDAGLV CAS number: 137525-51-0 PubChem CID: 108101
BPC-157 has been referenced in experimental and analytical literature as a synthetic peptide fragment utilised to examine signalling pathways associated with endothelial-adjacent molecular markers and pathway-level regulatory nodes. In controlled laboratory systems, research involving this peptide has focused on mapping signal transduction frameworks, pathway convergence, and regulatory interactions related to growth-signal intermediates commonly cited in angiogenesis-associated literature, without attribution to functional or organism-level outcomes [1,2].
Further analytical investigations have explored associations between BPC-157 exposure and modulation of receptor-linked signalling intermediates, including pathways frequently referenced in nitric-oxide–adjacent and kinase-mediated signalling networks. These studies are limited to pathway architecture description and molecular interaction analysis within defined experimental environments [3].
In laboratory research contexts, BPC-157 has been incorporated into reductionist experimental models to study signalling pathways associated with cellular structural organisation and extracellular matrix–adjacent molecular frameworks. Investigations focus on transcriptional and signalling markers related to epithelial-adjacent systems and structural remodelling pathways, analysed strictly at the molecular and pathway-mapping level [4].
Additional experimental systems have evaluated signalling responses associated with neuronal-adjacent cellular frameworks, concentrating on intracellular signalling markers, pathway modulation parameters, and stress-associated signal propagation within controlled analytical conditions [5,6].
Experimental literature has referenced BPC-157 in studies designed to examine signalling architectures related to connective-tissue–derived cellular models. These investigations focus on peptide-associated modulation of cytoskeletal signalling, transcriptional regulation markers, and pathway-level molecular interactions within defined experimental systems [7].
Additional in-vitro and reductionist analyses have evaluated associations between BPC-157 exposure and signalling intermediates related to fibroblast-adjacent cellular models, including pathways involving focal-adhesion-linked proteins and actin-associated regulatory components. Such evaluations are limited to molecular interaction mapping and signalling correlation analysis [8,9].
BPC-157 has also been referenced in experimental research as a molecular probe for examining signalling pathways associated with neuronal-adjacent cellular models. These studies focus on pathway-level signalling markers, intracellular regulatory networks, and signal propagation dynamics under controlled laboratory conditions, without implication of functional, protective, or behavioural outcomes [10–12].
TB-500, a synthetic peptide model derived from thymosin beta-4, and BPC-157 have been utilised in comparative laboratory investigations to analyse peptide-associated signalling convergence, divergence, and interaction dynamics. Experimental systems evaluate pathway overlap related to cytoskeletal organisation, actin-associated signalling, and extracellular structural-adjacent molecular frameworks [8,13].
Analytical literature also references TB-500 in studies examining actin-binding behaviour, signalling regulation parameters, and pathway-level interactions associated with growth-signal intermediates and programmed cellular turnover markers. These observations are interpreted strictly within molecular signalling and interaction-mapping contexts [14].
BPC-157 is not approved for human or animal use by the U.S. Food and Drug Administration. All existing investigative work involving this peptide is confined to controlled laboratory and experimental research environments.
BPC-157 is classified strictly as a research material, intended solely for laboratory, analytical, and investigative purposes. Purchase and use are restricted to qualified research professionals only.
BPC-157 is a 15-amino-acid synthetic pentadecapeptide derived from a partial sequence of a protein found endogenously in mammalian tissue. The molecule's compact structure provides notable resistance to proteolytic degradation under in vitro conditions, which makes it well suited to laboratory workflows where compound integrity must be preserved across long incubation windows.
In cell-based pharmacology research, BPC-157 is investigated for its engagement with growth factor receptor signalling — particularly the focal adhesion kinase / paxillin axis and the phosphorylation events that propagate downstream of it. Published in vitro work has also mapped its activity within nitric oxide synthase signalling and characterised its influence on extracellular matrix protein expression across multiple cell culture backgrounds.
Element CRP supplies this product at 5mg per vial. USA-manufactured via solid-phase peptide synthesis and verified at 99%+ purity by HPLC and Mass Spectrometry. Reconstitution with bacteriostatic water required. Store lyophilised at -20°C; stable for 24 months.
WARNING: For research use only. Not for human or animal consumption. Not intended to diagnose, treat, cure, or prevent any disease. For use by qualified research professionals only.
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All products on this site are for Research, Development use only. Products are Not for Human consumption of any kind. The statements made within this website have not been evaluated by the US Food and Drug Administration. The statements and the products of this company are not intended to diagnose, treat, cure or prevent any disease.
Element CRP is a chemical supplier. Element CRP is not a compounding pharmacy or chemical compounding facility as defined under 503A of the Federal Food, Drug, and Cosmetic act. Element CRP is not an outsourcing facility as defined under 503B of the Federal Food, Drug, and Cosmetic act.
