BPC-157 + TB-500 Blend
BPC-157 + TB-500 Blend
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Product details
BPC-157 + TB-500 is a research blend supplied in a single lyophilised vial that combines two synthetic peptides. BPC-157 is a pentadecapeptide derived from a protective fragment of gastric juice protein, stable in acidic conditions. TB-500 is a peptide corresponding to an actin-binding region of thymosin beta-4, a small, highly polar actin-sequestering protein.
Each component has been characterised at the molecular level in the published preclinical literature. BPC-157 has been examined in preclinical models around angiogenesis and the vascular endothelial growth factor and nitric oxide pathways, while TB-500, as a fragment of thymosin beta-4, binds monomeric G-actin in a 1:1 complex and shifts the equilibrium between monomeric and filamentous actin. The blend is supplied as a research compound and is not intended for human or veterinary use.
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Research
BPC-157 and TB-500 have each been characterised in preclinical laboratory models. The primary studies below are grouped by component: BPC-157 in animal and in-vitro tendon and ligament models examining biomechanical, histological, and cellular endpoints, and TB-500, as a fragment of thymosin beta-4, in cell-free biochemical assays and cultured cells examining how it binds the actin monomer and sets the monomer-to-filament equilibrium. The literature is preclinical; it describes each compound, not any outcome in humans.
6 preclinical studies indexed · bpc-157 research and tb-500 research · links open on PubMed
BPC-157 research 3 studies
Animal and in vitro
Gastric pentadecapeptide BPC 157 and transected rat Achilles tendon with paired in vitro tendocyte culture
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.
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Animal model
Stable gastric pentadecapeptide BPC 157 in a rat Achilles tendon-to-bone detachment model with a corticosteroid co-treatment arm
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.
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Animal model
Pentadecapeptide BPC 157 in a rat medial collateral ligament transection model
In a rat medial collateral ligament transection model, the peptide was studied across intraperitoneal, oral, and topical routes for biomechanical and collagen-organisation tissue endpoints over a 90-day course.
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TB-500 research 3 studies
In vitro
Thymosin beta-4 binds the actin monomer in an extended conformation, contacting both the barbed-end and pointed-end faces
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.
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In vitro
The ATP and ADP nucleotide state of the actin monomer modulates its interaction with thymosin beta-4
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.
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Cell-based
Raising thymosin beta-4 or beta-10 reorganizes filamentous actin structures in cultured cells
In transfected cultured macrophages and fibroblasts, raising thymosin beta-4 and beta-10 levels reorganized filamentous actin structures, showing the monomer-sequestering activity carries through into intact cells as a cellular endpoint.
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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. A Certificate of Analysis and a Safety Data Sheet are available on request for every batch.
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