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Copper Matrix Research Blend

Three-peptide research blend · lyophilised
$140 USD / vial
In stock, ships Mon to Fri
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Independent third-party Certificate of Analysis issued per batch.

📄 Certificate of Analysis available on request

Three-peptide research blend · lyophilised
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🇺🇸Made in the USASynthesised domestically
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About this compound

This is a research blend combining three peptides in a single lyophilised vial: GHK-Cu, the copper(II) complex of the tripeptide glycyl-L-histidyl-L-lysine; BPC-157, a synthetic pentadecapeptide derived from a protective fragment of gastric juice protein; and TB-500, a synthetic peptide corresponding to an actin-binding region of thymosin beta-4.

At the molecular level, GHK-Cu belongs to the metal-binding tripeptide class and coordinates a copper(II) ion; BPC-157 belongs to the pentadecapeptide class; and TB-500 belongs to the actin-binding peptide class. The three are supplied together as a research compound and are not intended for human or veterinary use.

Form
Supplied as a single lyophilised (freeze-dried) vial.
Blend composition
GHK-Cu, BPC-157, and TB-500 combined in one vial.
CAS, GHK-Cu
89030-95-5
CAS, BPC-157
137525-51-0
CAS, TB-500
77591-33-4
Storage
Store the sealed lyophilised vial at -20°C, away from direct sunlight and protected from light.
Shelf life
The lyophilised form has a shelf life of up to 24 months when stored as directed.
Handling
Handle in accordance with standard laboratory safety practice. A Certificate of Analysis and a Safety Data Sheet are available on request.
Intended use
For research use only. Not for human or veterinary use. Not for use in diagnostic or therapeutic procedures.

Research

Each component of this blend has been characterised in preclinical laboratory models. The primary studies below are grouped by component, in animal, cell-free, and cultured-cell systems, and examine molecular, biomechanical, histological, and cellular endpoints. The literature is preclinical; it describes the compounds, not any outcome in humans.

GHK-Cu research


In vitro / ex vivo
Copper-GHK increases integrin expression and p63 positivity by keratinocytes
Kang et al. · 2009 · Archives of Dermatological Research
In cultured keratinocytes and skin-equivalent constructs, the study assayed integrin alpha-6 and beta-1 expression by Western blot and quantified PCNA and p63 positivity by immunostaining as cellular endpoints.
Read the study ↗


In vitro
The tripeptide-copper complex glycyl-L-histidyl-L-lysine-Cu2+ stimulates matrix metalloproteinase-2 expression by fibroblast cultures
Siméon et al. · 2000 · Life Sciences
In cultured dermal fibroblasts, the study measured matrix metalloproteinase-2 protein in conditioned media and its mRNA level, alongside TIMP-1 and TIMP-2 expression, separating the copper-ion contribution from the bare tripeptide.
Read the study ↗

BPC-157 research


Animal and in vitro
Gastric pentadecapeptide BPC 157 and transected rat Achilles tendon with paired in vitro tendocyte culture
Staresinic et al. · 2003 · Journal of Orthopaedic Research
In a rat Achilles tendon transection model paired with cultured tendocytes, the peptide was studied for biomechanical, functional, and histological tissue endpoints and for tendocyte outgrowth in vitro, including its effect against the oxidative modulator 4-hydroxynonenal.
Read the study ↗


Animal model
Stable gastric pentadecapeptide BPC 157 in a rat Achilles tendon-to-bone detachment model with a corticosteroid co-treatment arm
Krivic et al. · 2006 · Journal of Orthopaedic Research
In a rat Achilles tendon-to-bone detachment model, the peptide was studied across functional, biomechanical, and microscopic tissue endpoints relative to saline controls and a corticosteroid (6-alpha-methylprednisolone) co-treatment arm.
Read the study ↗

TB-500 research


In vitro
Thymosin beta-4 binds the actin monomer in an extended conformation, contacting both the barbed-end and pointed-end faces
Safer et al. · 1997 · Biochemistry
Using circular dichroism, NMR, and cross-linking, the study placed thymosin beta-4 in an extended conformation along the actin monomer, contacting both the barbed-end and pointed-end faces and forming a 1:1 complex that blocks polymerization and nucleotide exchange.
Read the study ↗


In vitro
The ATP and ADP nucleotide state of the actin monomer modulates its interaction with thymosin beta-4
Carlier et al. · 1993 · Proceedings of the National Academy of Sciences USA
In cell-free assays, thymosin beta-4 bound MgATP-actin with roughly fifty-fold higher affinity than MgADP-actin, tying its monomer-sequestering activity to the nucleotide state of the actin monomer as a measured endpoint.
Read the study ↗

Full documentation, on the record. A Certificate of Analysis and a Safety Data Sheet are available on request for every batch.

Links open the original study on PubMed. For research and educational purposes, descriptive of the published preclinical literature, not therapeutic claims about any ai-peptides product.

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