GLOW GHK-Cu (50mg) / BPC-157 (10mg) / TB500 (10mg)

$165.00

SKU: YPB.218 Categories: ,

Description

A three-component co-formulation supplied for controlled research environments. Suitable for studies involving peptide characterization and method development in model systems.


Composition

• GHK-Cu
• BPC-157
• TB-500 (Thymosin Beta 4)
Appearance: Lyophilized powder in a sealed research vial


Research Focus (non-clinical)

• Combined evaluation of copper peptide, BPC-157, and TB-500 in in-vitro or ex-vivo assay systems
• Assay development, including chromatographic separation of three co-formulated peptides
• Stability characterization of a three-analyte lyophilized blend under laboratory storage conditions
• Method documentation for HPLC/LC-MS identity and purity assessments

For qualified research professionals and institutional laboratories. Not for human use.


Documentation & Quality Assurance

Each lot is sourced through our verified global supply chain with emphasis on traceability and quality control. We work diligently to obtain and maintain third-party analytical reports (HPLC/LC-MS) and Certificates of Analysis for each batch, as part of our ongoing quality process. These documents are reviewed internally and displayed as they become available. Independent third-party testing is also performed on select lots to confirm identity, purity, and alignment with our internal specifications.


Important Notice

This product is intended for laboratory research use only. It is not intended for human or veterinary use, and must not be used for diagnostic, therapeutic, or clinical purposes.
This material is not a drug, medical device, or dietary supplement, and has not been evaluated by the U.S. Food and Drug Administration.


Quality & Manufacturing

All materials are sourced from carefully vetted domestic and international manufacturing partners who follow quality systems consistent with ISO and cGMP principles. Each supplier is reviewed for reliability, documentation integrity, and transparency in testing.

We require a verified purity of 99% or higher and perform independent third-party spot testing to confirm that select lots meet our internal standards for identity, purity, and composition. Where available, endotoxin testing results are included on Certificates of Analysis to verify laboratory purity; their inclusion is for research quality assessment only and does not imply suitability for human or veterinary use.

All research materials are sealed for integrity and packaged for stability during storage and transport from manufacturing through final delivery.

Additional information

Weight 0.2 lbs

Storage Instructions

All our research peptides are manufactured using a lyophilization (freeze-drying) process. This method is designed to maintain product integrity and allows vials to remain stable during shipping for approximately 3–4 months.

Once a vial is reconstituted with bacteriostatic water, it should be stored in the refrigerator to help maintain stability. Under these conditions, reconstituted material is generally considered stable for up to 30 days.

Lyophilization is a dehydration technique in which compounds are frozen and then exposed to low pressure. This causes the water in the vial to sublimate directly from solid to gas, leaving behind a stable, crystalline white structure. This powder can be kept at room temperature until reconstitution.

Upon receipt, products should be stored away from heat and light. For short-term use, refrigeration at approximately 4°C (39°F) is suitable. For long-term storage (several months to years), vials may be placed in a freezer at approximately -80°C (-112°F). Freezing is the preferred method for preserving product stability over extended periods.

⚠️ Important Notice: These products are intended for research use only. Not for human consumption.

Certificate of Analysis

Every batch undergoes rigorous third-party laboratory testing to verify identity, purity (≥98%), and quality before release.

View Certificate of Analysis
Third-Party Verified ≥98% Purity HPLC & MS Tested

Research Use Only

These studies reference research-grade peptides for laboratory and scientific investigation only. Not for human consumption. Not intended to diagnose, treat, cure, or prevent any disease.

Published Scientific Research

Peer-reviewed laboratory research investigating regenerative peptides from leading scientific databases

Molecular Analysis
PubMed

Growth arrest specific-6 and angiotoxin receptor-like signaling drive oral regenerative wound repair.

Science translational medicine 2025

Rapid and scarless wound repair is a hallmark of the oral mucosa, yet the cellular and molecular mechanisms that enable this regeneration remain unclear. By comparing populations of murine oral mucosal fibroblasts (OMFs) and facial skin fibroblasts (FSFs), we have identified mechanisms that facilitate regeneration over fibrosis.

View Full Study
Molecular Analysis
PubMed

RALF33-FERONIA signaling orchestrates postwounding root-tip regeneration via TPR4-ERF115 dynamics.

The Plant cell 2025

The molecular mechanisms underlying wound-induced tissue and organ regeneration in plants are unclear. Here, we identified a signaling pathway that governs the wound-induced regeneration of Arabidopsis (Arabidopsis thaliana) roots, highlighting a key role for the peptide RAPID ALKALINIZATION FACTOR33 (RALF33) and its receptor FERONIA (FER).

View Full Study
Molecular Analysis
PubMed

Lycium barbarum glycopeptide alleviates neuroinflammation in spinal cord injury via modulating docosahexaenoic acid to inhibiting MAPKs/NF-kB and pyroptosis pathways.

Journal of translational medicine 2023

Previous studies have shown that LbGp can regulate the immune microenvironment, but its specific mechanism of action remains unclear. In vitro, LbGp was administered to mimic the inflammatory microenvironment by activating microglia, and its mechanism of action in suppressing neuroinflammation was further elaborated using metabolomics and molecular biology techniques such as western blotting and q-PCR.

View Full Study
Molecular Analysis
PubMed

Structure-activity relationships of antibacterial peptides.

Microbial biotechnology 2023

Indeed, the exploration of the immune system over the past 40 years has revealed a number of natural peptides playing a pivotal role in the defence mechanisms of vertebrates and invertebrates, including amphibians, insects, and mammalians. This review provides a discussion regarding the antibacterial mechanisms of peptide-based agents and their structure-activity relationships (SARs) with the aim of describing a topic that is not yet fully explored.

View Full Study
Molecular Analysis
PubMed

mtDNA Activates cGAS Signaling and Suppresses the YAP-Mediated Endothelial Cell Proliferation Program to Promote Inflammatory Injury.

Immunity 2020

Cytosolic DNA acts as a universal danger-associated molecular pattern (DAMP) signal; however, the mechanisms of self-DNA release into the cytosol and its role in inflammatory tissue injury are not well understood. We found that the internalized bacterial endotoxin lipopolysaccharide (LPS) activated the pore-forming protein Gasdermin D, which formed mitochondrial pores and induced mitochondrial DNA (mtDNA) release into the cytosol of endothelial cells.

View Full Study
Molecular Analysis
PubMed

Derivation of enteric neuron lineages from human pluripotent stem cells.

Nature protocols 2019

Considerable improvements in the understanding of the molecular mechanisms underlying NC induction and regional specification have recently led to the development of a robust method to re-create the process in vitro using human pluripotent stem cells (hPSCs).

View Full Study