KLOW – GHK-Cu (50mg) / KPV (10mg) / BPC-157 (10mg) / TB500 (10mg)

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

Composition

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

Research Focus (non-clinical)

• Combined evaluation of copper peptide, KPV tripeptide, BPC-157, and TB-500 in in-vitro or ex-vivo assay systems
• Assay development, including chromatographic separation of four co-formulated peptides
• Stability characterization of a four-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.

What It Is

KLOW Blend is a research formulation combining four peptides — GHK-Cu (glycyl-L-histidyl-L-lysine copper(II) complex, a naturally occurring human tripeptide-copper chelate), KPV (Lys-Pro-Val, the C-terminal tripeptide of alpha-melanocyte-stimulating hormone), BPC-157 (a 15-amino-acid pentadecapeptide with the sequence Gly-Glu-Pro-Pro-Pro-Gly-Lys-Pro-Ala-Asp-Asp-Ala-Gly-Leu-Val, corresponding to a partial sequence of a protein from human gastric juice), and TB-500 (the N-acetylated heptapeptide Ac-LKKTETQ, corresponding to the actin-binding domain at positions 17-23 of the endogenous 43-amino-acid polypeptide thymosin beta-4) — assembled for in vitro and preclinical research into the distinct and potentially complementary mechanisms of these four peptides.

Research Background

GHK-Cu was first isolated in 1973 as an activity in human albumin and has since been studied in cultured human fibroblasts, keratinocytes, and cancer cell lines, as well as in rabbit, rat, mouse, pig, and dog wound-healing models, with additional placebo-controlled clinical trials examining skin biopsy outcomes; a 2018 review summarized evidence across skin, lung connective tissue, bone, liver, and gastrointestinal tissue models. KPV has been examined in murine models of crystal-induced peritonitis and chemically induced colitis (DSS and TNBS protocols), in intestinal epithelial cell lines (Caco-2-BBE, HT29-Cl.19A), and in human Jurkat T cells, characterizing its transport and signaling at nanomolar concentrations. BPC-157 research has centered on small-animal models (predominantly rats and mice) across musculoskeletal, gastrointestinal, and central-nervous-system injury paradigms, including intramuscular, intraperitoneal, subcutaneous, intragastric, and intravenous administration routes; a 2025 literature and patent review noted that a Phase I human trial begun in 2015 was subsequently abandoned, leaving the compound without completed clinical evidence. TB-500 research has focused on the actin-sequestering properties of thymosin beta-4 studied in human umbilical vein endothelial cell migration assays and chick aortic arch sprouting assays; analytical identification of the synthetic Ac-LKKTETQ fragment in equine biological matrices has also been published.

Observed Areas of Interest in Research

For GHK-Cu, investigators have studied its coordination chemistry — the Cu(II) ion is coordinated by the imidazole nitrogen of histidine, the alpha-amino nitrogen of glycine, and the deprotonated amide nitrogen of the glycine-histidine peptide bond — alongside its modulation of matrix metalloproteinases and their inhibitors (TIMP-1 and TIMP-2), stimulation of TGF-beta pathway gene expression in COPD-model fibroblasts, NF-kB suppression, upregulation of integrin expression in basal keratinocytes, and broad genomic effects including DNA repair gene expression, with one review noting regulation of thousands of human genes identified in microarray analyses. For KPV, researchers have characterized its uptake via the intestinal transporter PepT1 in epithelial and immune cells, inhibition of NF-kB and MAP kinase inflammatory signaling cascades at nanomolar concentrations, and receptor-dependence studies using melanocortin-receptor-deficient mice to dissect receptor-mediated versus receptor-independent mechanisms. For BPC-157, the primary investigated mechanism involves the nitric oxide (NO) signaling system, with additional studies examining upregulation of the VEGFR-2 receptor in endothelial cell cultures and ischemic hind-limb models, and antioxidant activity through stabilization of free-radical scavengers. For TB-500 / the thymosin beta-4 actin-binding fragment, researchers have investigated G-actin sequestration, endothelial cell migration, tubule formation, and aortic ring sprouting activity, with the seven-amino-acid actin-binding motif LKKTETQ reported to show angiogenic activity at approximately 50 nM in cell-based assays and its inhibition by soluble actin establishing the mechanistic link between actin binding and proangiogenic signaling.

Research Notes

Purity verified by third-party laboratory analysis (Certificate of Analysis available on request). Supplied strictly for in-vitro and laboratory research use only. Not for human consumption.

All information above is provided for research and educational reference only and summarizes findings from published scientific literature (predominantly in-vitro and animal models). It does not describe outcomes in humans. This product is not a drug, dietary supplement, or article intended for human or veterinary use.

All products from Blitz Health 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.