BPC-157 + TB-500 Blend 15mg / 15mg

BPC-157 15 mg + TB-500 15 mg is a high-purity dual-peptide research preparation supplied exclusively for scientific investigation and controlled laboratory experimentation. For research use only — not for human or veterinary use.  

Product Overview

BPC-157 15 mg + TB-500 15 mg is a dual-peptide research preparation combining two independently characterised peptide components within a single lyophilized research vial. The formulation contains 15 mg BPC-157 and 15 mg Thymosin Beta 4 (TB-500), providing a total nominal peptide content of 30 mg. Both components represent established areas of experimental peptide research. BPC-157 is investigated within controlled laboratory models involving peptide-mediated molecular interactions and cellular signalling, while Thymosin Beta 4 is studied within experimental peptide biology, molecular communication and cellular research systems. Independent third-party laboratory analysis of this production batch measured an assay content of 17.29 mg for BPC-157 and 17.92 mg for Thymosin Beta 4 (TB-500). Chromatographic analysis confirmed 99.5 percent purity for BPC-157 and 99.2 percent purity for Thymosin Beta 4 (TB-500), while identity was independently evaluated through retention time analysis and mass spectrometry. Microbiological testing reported 0 CFU/g for both total aerobic microbial count and total yeast and mold count, while bacterial endotoxin analysis returned a result of 0.007 EU/mg. Comprehensive elemental impurity screening additionally reported arsenic, cadmium, mercury, lead, nickel, vanadium and cobalt below 0.001 ppm. With both peptide components independently characterised, this dual-peptide preparation provides researchers with transparent batch-specific analytical documentation suitable for advanced peptide investigations and controlled in vitro laboratory studies.  

Peptide Overview

BPC-157 and Thymosin Beta 4 (TB-500) are structurally distinct peptide research compounds commonly investigated within experimental peptide biology and molecular research. BPC-157 is a synthetic peptide research compound utilised in controlled investigations involving peptide-mediated molecular interactions, intracellular communication and cellular signalling systems. Thymosin Beta 4 is a peptide research compound investigated within experimental cellular biology, molecular interactions and peptide-mediated signalling research. Combining both compounds within a single research preparation provides investigators with a dual-component material for controlled comparative and combined peptide research. For this production batch, Liquilabs independently evaluated assay content, purity, retention time identity and molecular ion mass for both peptide components.  

Historical Background and Scientific Context

Advances in peptide synthesis and analytical chemistry have enabled researchers to develop increasingly sophisticated combined peptide preparations for controlled scientific investigation. Modern analytical technologies make it possible to independently characterise individual compounds within dual-peptide preparations rather than evaluating only the formulation as a whole. Chromatographic techniques can independently determine assay content, purity and retention time characteristics for each peptide component, while mass spectrometry provides additional molecular identity verification. Microbiological analysis, bacterial endotoxin testing and elemental impurity screening further contribute to comprehensive batch-specific analytical characterisation. BPC-157 15 mg + TB-500 15 mg represents a dual-peptide research preparation in which both components have been independently evaluated within the same production batch.  

Mechanistic Focus in Research

Within controlled laboratory environments, BPC-157 and Thymosin Beta 4 may be investigated in relation to peptide signalling, molecular interactions and cellular communication systems. Research investigations frequently explore:

• Dual-peptide interaction research
• Peptide-mediated signalling pathways
• Intracellular molecular communication
• Cellular regulatory mechanisms
• Biochemical pathway analysis
• Molecular peptide interactions
• Comparative peptide investigations
• Combined peptide research models
• Controlled in vitro peptide studies

These experimental models allow researchers to investigate multiple peptide-related molecular systems while maintaining carefully controlled laboratory conditions.  

Analytical Verification (COA)

Each batch of BPC-157 15 mg + TB-500 15 mg supplied by Grail Formula undergoes comprehensive independent third-party laboratory verification to characterise both peptide components and important laboratory quality parameters. Analytical testing for this batch was performed by Liquilabs s.r.o. Czechia using chromatographic, microbiological and mass spectrometry techniques. Batch: GF-BPCTB15-B241

• BPC-157 Content: 15 mg
• BPC-157 Assay Content: 17.29 mg
• BPC-157 Purity: 99.5 %
• BPC-157 Identification by Retention Time: 0.997
• BPC-157 Molecular Ion Mass: 1418 Da
• Thymosin Beta 4 (TB-500) Content: 15 mg
• Thymosin Beta 4 (TB-500) Assay Content: 17.92 mg
• Thymosin Beta 4 (TB-500) Purity: 99.2 %
• Thymosin Beta 4 (TB-500) Identification by Retention Time: 0.996
• Thymosin Beta 4 (TB-500) Molecular Ion Mass: 4963 Da
• Bacterial Endotoxins: 0.007 EU/mg
• Total Aerobic Microbial Count: 0 CFU/g
• Total Yeast and Mold Count: 0 CFU/g

Independent peptide screening measured an assay content of 17.29 mg for BPC-157 with a reported analytical uncertainty of ±0.09 mg. Thymosin Beta 4 (TB-500) assay content was measured at 17.92 mg with a reported analytical uncertainty of ±0.09 mg. Purity analysis confirmed 99.5 percent purity for BPC-157 and 99.2 percent purity for Thymosin Beta 4 (TB-500). Retention time analysis returned 0.997 for BPC-157 and 0.996 for Thymosin Beta 4 (TB-500). Mass spectrometry identified molecular ion masses of 1418 Da for BPC-157 and 4963 Da for Thymosin Beta 4 (TB-500). Bacterial endotoxin testing returned a result of 0.007 EU/mg. Microbiological testing reported 0 CFU/g for total aerobic microbial count and 0 CFU/g for total yeast and mold count. Independent elemental impurity analysis reported arsenic, cadmium, mercury, lead, nickel, vanadium and cobalt below 0.001 ppm. These analytical procedures provide extensive independent batch-specific characterisation of both peptide components together with microbiological, endotoxin and elemental impurity testing.  

Research Applications

Within controlled laboratory environments, BPC-157 15 mg + TB-500 15 mg may be utilised in experimental models designed to investigate peptide biology, molecular signalling and biochemical interactions. Examples of research applications include:

• Dual-peptide interaction investigations
• BPC-157 peptide research
• Thymosin Beta 4 peptide research
• Peptide-mediated signalling studies
• Intracellular signalling investigations
• Molecular pathway analysis
• Comparative peptide investigations
• Combined peptide research models
• Controlled in vitro peptide studies

These applications are intended exclusively for scientific and laboratory investigation.  

Grail Formula Quality

Every Grail Formula research compound is supported by comprehensive independent analytical verification and transparent batch-specific laboratory documentation. For this dual-peptide production batch, independent laboratory testing included:

• Individual assay determination for both peptide components
• Individual purity assessment for both peptide components
• Retention time identity verification
• Molecular ion mass identification
• Bacterial endotoxin analysis
• Total aerobic microbial count
• Total yeast and mold count
• Comprehensive elemental impurity screening
• Complete batch-specific traceability

Independent analysis of both peptide components provides researchers with detailed analytical information relating directly to the tested production batch rather than relying solely on the nominal formulation. This approach supports analytical transparency, batch traceability and consistency across Grail Formula research compounds.  

When You Choose Grail Formula

When selecting Grail Formula, researchers receive independently analysed research compounds supported by detailed Certificates of Analysis and transparent batch-specific laboratory documentation. For BPC-157 15 mg + TB-500 15 mg batch GF-BPCTB15-B241, independent analysis was performed by Liquilabs s.r.o. Czechia and the Certificate of Analysis was published on 20 September 2026. Both peptide components were independently evaluated for assay content, purity, retention time identity and molecular ion mass. The analytical programme additionally included bacterial endotoxin testing, microbiological analysis and comprehensive elemental impurity screening. This multi-method analytical approach provides researchers with extensive independent information regarding both components within the tested dual-peptide research preparation.  

Research Use Limitation

• Used solely for laboratory and in vitro research
• Not approved for human consumption
• Not approved for veterinary use
• Not intended for diagnostic purposes
• Not intended for therapeutic applications
• Not permitted for clinical administration
• For research use only

• Independently analysed by Liquilabs s.r.o. Czechia
• Contains 15 mg BPC-157 and 15 mg Thymosin Beta 4 (TB-500)
• BPC-157 purity confirmed at 99.5 %
• Thymosin Beta 4 (TB-500) purity confirmed at 99.2 %
• BPC-157 assay content verified at 17.29 mg
• Thymosin Beta 4 (TB-500) assay content verified at 17.92 mg
• Identity confirmed by retention time and mass spectrometry analysis
• Molecular ion masses identified at 1418 Da and 4963 Da
• Bacterial endotoxin level of 0.007 EU/mg
• No detectable heavy metals or microbial contamination
• Dual-peptide research preparation with complete COA traceability
• For research use only – not for human or veterinary use

For laboratory research only. Not intended for human consumption, injection, or cosmetic use.

This product is for research purposes only. Not for human use or diagnostic/therapeutic applications. Keep out of reach of children.