Description

KLOW — 80 mg
BPC-157 (10 mg)  •  TB-500 (10 mg)  •  GHK-Cu (50 mg)  •  KPV (10 mg)
Lyophilized Multi-Peptide Research Formulation  |  For Laboratory Research Purposes Only

1. Product Specifications

Parameter	Specification
Product Name	KLOW
Total Content	80 mg lyophilized powder per vial
Formulation	GHK-Cu (50 mg) | BPC-157 (10 mg) | TB-500 (10 mg) | KPV (10 mg)
CAS Numbers	89030-95-5 (GHK-Cu) | 137525-51-0 (BPC-157) | 77591-33-4 (TB-500) | 67727-97-3 (KPV)
Molecular Formulas	C₁₄H₂₂CuN₆O₄ | C₆₂H₉₈N₁₆O₂₂ | C₂₁₂H₃₅₀N₅₆O₇₈S | C₁₆H₃₀N₄O₄
Molecular Weights	401.91 g/mol | 1,419.56 g/mol | 4,963.50 g/mol | 342.43 g/mol
Sequences	Gly-His-Lys·Cu²⁺ | Gly-Glu-Pro-Pro-Pro-Gly-Lys-Pro-Ala-Asp-Asp-Ala-Gly-Leu-Val | Ac-SDKPDMAEIEKFDKSKLKKTETQEKNPLPSKETIEQEKQAGES | Lys-Pro-Val
Purity	≥99% (HPLC verified)
Form	White to off-white lyophilized powder
Storage	Store at −20°C, desiccated, protected from light. After reconstitution: 2–8°C, use within 30 days.
Third-Party Testing	Certificate of Analysis (COA) available per lot; HPLC and MS verified
Classification	Research Use Only (RUO) — Not for human consumption or veterinary use

2.1 Molecular Structure & Chemistry

KLOW is a quaternary peptide blend combining four structurally and mechanistically distinct compounds. GHK-Cu is a copper(II)-complexed tripeptide (Gly-His-Lys·Cu²⁺) with a molecular weight of 401.91 g/mol. The copper ion is coordinated in a square-planar geometry through the glycine amino terminus, the histidine imidazole nitrogen, and the deprotonated amide nitrogen between glycine and histidine. This coordination chemistry silences copper(II) redox activity, permitting non-oxidative metal transport in experimental systems.

BPC-157 is a 15-amino-acid synthetic peptide (MW 1,419.56 g/mol) with the sequence Gly-Glu-Pro-Pro-Pro-Gly-Lys-Pro-Ala-Asp-Asp-Ala-Gly-Leu-Val. Its high proline content contributes to conformational rigidity and resistance to enzymatic degradation under acidic conditions. TB-500 corresponds to the full 43-amino-acid sequence of thymosin beta-4 (MW 4,963.50 g/mol), an actin-sequestering polypeptide with an N-terminal acetylated serine. The central actin-binding domain (residues 17–23) is the primary region of interest in cytoskeletal research.

KPV is a linear tripeptide (Lys-Pro-Val, MW 342.43 g/mol) corresponding to residues 11–13 of the C-terminal region of alpha-melanocyte-stimulating hormone (α-MSH). It is the smallest fragment of α-MSH reported to retain interaction with melanocortin-associated signaling cascades in cell-based assay systems.

2.2 Laboratory Research Applications

The KLOW formulation was designed to facilitate multi-pathway investigation within a single reconstituted preparation. In cell culture systems, the four components engage distinct molecular targets: GHK-Cu participates in copper-mediated metalloprotein interactions and extracellular matrix protein expression studies. BPC-157 has been employed in nitric oxide synthase pathway analyses and growth factor receptor characterization experiments. TB-500 serves as a tool for studying G-actin monomer sequestration and filament polymerization dynamics. KPV has been utilized in NF-κB transcription factor translocation assays and cytokine secretion profiling in immune cell lines.

In animal model research, these peptides have been examined independently across rodent injury paradigms to characterize their effects on cell migration kinetics, vascular formation markers, extracellular matrix deposition rates, and inflammatory mediator concentrations. The combined formulation enables researchers to study potential cross-pathway interactions that single-peptide preparations cannot address.

2.3 Quality Specifications & Testing

Each lot of KLOW undergoes third-party analytical characterization. Identity and purity are confirmed via reverse-phase high-performance liquid chromatography (RP-HPLC) with UV detection, achieving ≥99% chromatographic purity. Mass spectrometric analysis (ESI-MS or MALDI-TOF) verifies molecular identity for each peptide component. The lyophilized product is tested for residual solvent content, endotoxin levels, and microbiological contamination. A lot-specific Certificate of Analysis is provided with each shipment.

2.4 Storage & Handling

Lyophilized product: Store at −20°C in a dry, desiccated environment protected from light. Under these conditions, the product maintains stability for up to 24 months. Reconstituted product: Reconstitute with sterile bacteriostatic water or an appropriate research-grade buffer. Store reconstituted aliquots at 2–8°C and use within 30 days. For extended storage of reconstituted material, aliquot into single-use volumes and store at −20°C. Avoid repeated freeze-thaw cycles, which may compromise peptide integrity.

3. Research Background

3.1 Discovery & Historical Context

The four peptides comprising KLOW were independently discovered across several decades of biochemical research. GHK was first isolated from human plasma albumin in 1973 by Loren Pickart during investigations into age-dependent differences in hepatocyte fibrinogen synthesis. The observation that younger plasma could modulate older tissue behavior led to identification of the glycyl-L-histidyl-L-lysine sequence and its high-affinity copper(II) complex.

BPC-157 emerged from research on human gastric juice proteins conducted by Predrag Sikiric and colleagues at the University of Zagreb. The stable gastric pentadecapeptide was derived from a larger body protection compound (BPC) and was first characterized in the early 1990s for its unusual stability in acidic environments.

Thymosin beta-4, the parent protein of TB-500, was discovered in the mid-1960s by Allan Goldstein at the Albert Einstein College of Medicine during studies on the role of the thymus gland in vertebrate immune system development. The 43-amino-acid polypeptide was later identified as the most abundant intracellular G-actin-sequestering protein.

KPV was identified as the minimal bioactive C-terminal fragment of α-MSH through structure-activity relationship studies conducted in the 1990s. Researchers determined that this three-amino-acid sequence retained the capacity to interact with melanocortin-associated signaling pathways independently of the melanotropic activity attributed to the full-length hormone.

3.2 Structural Characteristics

GHK-Cu adopts a defined coordination geometry in which copper(II) occupies a square-planar environment. X-ray crystallographic and spectroscopic studies established that the metal center is coordinated by the amino terminal nitrogen of glycine, the imidazole Nπ of histidine, and the deprotonated peptide bond nitrogen between glycine and histidine, with an additional carboxylate oxygen from a neighboring complex completing the coordination sphere. This arrangement effectively quenches Fenton-type redox chemistry, distinguishing GHK-Cu from free copper ions in biological research systems.

BPC-157 features three consecutive proline residues (positions 3–5) that constrain the peptide backbone into polyproline II helical segments, conferring resistance to pepsin and trypsin digestion. The absence of disulfide bonds and the overall negative charge at physiological pH contribute to its aqueous solubility and chemical stability in acidic media.

TB-500 contains two helical domains (residues 4–15 and 30–40) connected by an extended loop region. The LKKTETQ motif at positions 17–23 constitutes the primary G-actin binding domain. N-terminal acetylation of serine-1 is a characteristic post-translational modification that contributes to the protein’s biological behavior in research systems.

KPV’s proline residue introduces a rigid kink in the backbone, while the lysine and valine side chains provide cationic and hydrophobic character, respectively. This amphipathic profile facilitates interaction with the PepT1 oligopeptide transporter, a proton-coupled di/tripeptide transporter expressed in intestinal epithelial cell models.

3.3 Receptor Systems & Signaling Pathways Studied in Research

GHK-Cu has been studied in the context of copper-dependent metalloprotein regulation. Microarray analyses reported that GHK modulated the expression of over 4,000 human genes in cultured fibroblasts, including genes associated with extracellular matrix assembly, oxidative stress response, and growth factor signaling. Research examined the tripeptide’s capacity to transfer copper ions to and from intracellular compartments via interaction with cellular receptors.

BPC-157 research has focused on interactions with the nitric oxide (NO) system and growth factor receptor pathways. Studies examined the peptide’s effects on endothelial NO synthase (eNOS/NOS3) and inducible NO synthase (iNOS/NOS2) gene expression in various cell types. Research also investigated downstream signaling through VEGFR2, FAK/paxillin, and ERK1/2 phosphorylation cascades in endothelial cell models.

TB-500 research has centered on the actin cytoskeleton. The peptide’s LKKTETQ domain sequesters G-actin monomers, modulating the equilibrium between monomeric actin and filamentous actin (F-actin). This interaction has been studied using fluorescence microscopy, actin polymerization assays, and cell migration scratch assays. Additional research explored TB-500’s effects on integrin-linked kinase (ILK) signaling and its downstream targets.

KPV research has examined its interactions with melanocortin receptor-associated signaling pathways and the NF-κB transcription factor system. Studies demonstrated that KPV enters cells via the PepT1 transporter and modulates IκB-α stability, preventing p65/RelA nuclear translocation. Research also investigated KPV’s effects on cytokine secretion profiles, including TNF-α, IL-1β, and IL-6 concentrations in macrophage and epithelial cell culture models.

3.4 Laboratory Methodologies

Researchers have employed a range of standard laboratory techniques to characterize the individual peptides in this blend. Common methodologies documented in published literature include: cell viability assays (MTT, WST-1) for concentration-response profiling; scratch/wound migration assays for quantifying cell motility; enzyme-linked immunosorbent assays (ELISA) for cytokine and growth factor quantification; Western blot and immunoprecipitation for protein expression and phosphorylation state analysis; quantitative PCR (qPCR) for gene expression profiling; immunohistochemistry and immunofluorescence microscopy for tissue-level localization; and actin polymerization kinetic assays for cytoskeletal dynamics.

In vivo research has utilized rodent models with standardized injury paradigms. Outcome measures in published studies included histological scoring, tensile strength measurements, vessel density quantification via CD31 immunostaining, and enzyme activity profiling (myeloperoxidase, superoxide dismutase, catalase).

3.5 Analytical Characterization

Analytical methods for each KLOW component are well-established in the scientific literature. Reverse-phase HPLC with C18 columns and acetonitrile/water gradients containing 0.1% trifluoroacetic acid (TFA) is the standard method for purity determination. Electrospray ionization mass spectrometry (ESI-MS) provides molecular mass confirmation. For GHK-Cu specifically, inductively coupled plasma mass spectrometry (ICP-MS) or atomic absorption spectroscopy (AAS) may be used to confirm copper content and stoichiometry. Circular dichroism (CD) spectroscopy has been applied to characterize secondary structure elements in TB-500.

3.6 References

1. Sikiric P, et al. Stable gastric pentadecapeptide BPC 157: novel therapy in gastrointestinal tract. Current Pharmaceutical Design. 2018;24(18):1990–2001.
2. Pickart L, Vasquez-Soltero JM, Margolina A. GHK peptide as a natural modulator of multiple cellular pathways in skin regeneration. BioMed Research International. 2015;2015:648108.
3. Goldstein AL, Hannappel E, Kleinman HK. Thymosin beta-4: actin-sequestering protein moonlights to repair injured tissues. Trends in Molecular Medicine. 2005;11(9):421–429.
4. Getting SJ, et al. Molecular determinants of the anti-inflammatory actions of the melanocortins. Journal of Immunology. 1999;163(10):5959–5967.
5. Pickart L. The human tri-peptide GHK and tissue remodeling. Journal of Biomaterials Science, Polymer Edition. 2008;19(8):969–988.

 

5. Regulatory & Compliance Statement

FOR RESEARCH USE ONLY NOT FOR HUMAN CONSUMPTION OR VETERINARY USE This product is sold exclusively for laboratory research applications. It is not approved by the U.S. Food and Drug Administration (FDA) for human use, clinical applications, or therapeutic purposes. This product is not intended to diagnose, treat, cure, or prevent any disease. Peptide Minds is a chemical supplier. Peptide Minds is not a compounding pharmacy or chemical compounding facility as defined under 503A of the Federal Food, Drug, and Cosmetic Act. Peptide Minds is not an outsourcing facility as defined under 503B of the Federal Food, Drug, and Cosmetic Act. All products are sold for research, laboratory, or analytical purposes only and are not for human consumption of any kind. The statements made on this website have not been evaluated by the U.S. Food and Drug Administration. Purchase and use of this product constitutes agreement to these terms.