KLOW Blend: Chemistry and Documentation of a Four-Peptide Research Formulation

For in-vitro laboratory research use only. Not for human consumption.

Multi-component research formulations let a laboratory hold several peptides in one vial, but they also raise documentation questions that a single-peptide vial does not. The KLOW Blend contains four chemically distinct compounds, ranging from a three-residue metal complex to a 43-residue acetylated peptide. This guide sets out the chemistry of each component, how a four-component formulation is characterized analytically, and how the lyophilized material should be stored and recorded.

What Is KLOW Blend?

KLOW Blend is a four-peptide research complex combining:

• GHK-Cu — a copper(II) complex of the tripeptide glycyl-L-histidyl-L-lysine
• BPC-157 — a synthetic 15-residue peptide
• TB-500 — synthetic material corresponding to thymosin beta-4 or a fragment of it
• KPV — the tripeptide lysyl-prolyl-valine, the C-terminal fragment of alpha-melanocyte-stimulating hormone

Each component is a separate chemical entity with its own molecular formula, mass, analytical profile and storage sensitivities. The product size reflects that: the formulation is supplied as 50 mg of GHK-Cu with 10 mg each of the other three components.

Chemistry of the Four Components

Molecular Data

Chemically Sensitive Features

• GHK-Cu is a coordination complex. Its blue-violet color comes from copper(II) d-d transitions, and its speciation depends on pH and on competing ligands. It must be kept away from chelating agents and strong acids or bases.
• BPC-157 contains no methionine, cysteine or tryptophan, so it is not prone to oxidation; its main liability is the adjacent aspartate pair at positions 10 and 11.
• TB-500 contains one methionine (oxidation, adding 16 Da) and several asparagine and glutamine residues (slow deamidation), so it should be kept sealed, cold, dry and away from air and light.
• KPV is a short, basic tripeptide with no aromatic residues, which means it has negligible absorbance at 280 nm and is detected in HPLC only at low wavelength.

Analytical Consequences

The four components span a mass range of more than an order of magnitude and include a metal complex, which has direct consequences for analysis. A single chromatographic method must resolve all four; the two tripeptides are very polar and elute early, while BPC-157 and thymosin beta-4 elute later and at different positions. Confirming the copper in GHK-Cu requires methods that a peptide-only analysis does not include, such as elemental analysis or UV-visible spectroscopy. Quantifying each component separately requires calibration against reference standards of each.

Research Context

Each component has been examined in published in-vitro and animal research, and none is approved for human use. The literature on each is separate: GHK-Cu appears in coordination chemistry and matrix-biology studies, BPC-157 and thymosin beta-4 in cell-culture and rodent studies, and KPV in studies of melanocortin-derived peptides and NF-κB signaling. Published work examining all four together in a single experimental design is limited, so a laboratory using a combined formulation generally needs the individual peptides as comparators in order to interpret its own data.

Sourcing Standards

Multi-component formulations require documentation covering every component. Laboratories typically look for:

• HPLC data with the method conditions stated, showing all components resolved
• Mass spectrometry consistent with each peptide sequence
• Copper determination for the GHK-Cu component
• A published Certificate of Analysis
• Lyophilized form with stated storage conditions

Excalibur Peptides is a U.S.-based research peptide supplier. A Certificate of Analysis is published for our KLOW Blend and can be reviewed on the product page and in our COA database.

View the KLOW Blend product page →

All products sold by Excalibur Peptides are intended for in-vitro laboratory research use only. Not for human consumption.

Deconstructing the Components: A Molecular Overview

To understand what a four-component formulation contains, it is worth examining each peptide's chemistry and the pathways each has been associated with in published cell-culture work. The descriptions below are mechanistic and refer to observations in laboratory models only.

GHK-Cu: A Copper Tripeptide

The tripeptide Glycyl-L-Histidyl-L-Lysine (GHK) binds copper(II) ions with high affinity, forming the GHK-Cu complex. In the published literature it has mostly been examined in fibroblast and matrix-biology cell models, where the readouts center on extracellular matrix (ECM) gene expression and on copper-dependent enzymes.

Its chemistry is twofold. As a coordination complex, copper(II) is bound by the imidazole nitrogen of histidine, a backbone amide nitrogen and the N-terminal amine, giving the square-planar or distorted geometry typical of copper(II) peptide complexes. In cell-culture work, published microarray studies using cultured fibroblasts have examined the expression of genes encoding matrix proteins such as collagen and elastin, of matrix metalloproteinases (MMPs) and of tissue inhibitors of metalloproteinases (TIMPs) (Pickart et al., 2015). Because both the peptide and the metal can influence such readouts, experiments in this area include the apo-peptide and a simple copper salt as separate comparators.

Copper is the catalytic metal of several enzymes that are standard readouts in matrix biology, including lysyl oxidase (LOX), which cross-links collagen and elastin, and copper-zinc superoxide dismutase (SOD1). Because GHK-Cu introduces a defined copper species into a culture system, studies that use it as a copper source typically measure LOX and SOD activity by enzymatic assay alongside gene-expression data, and they include copper-free and copper-salt conditions so that the contribution of the metal can be separated from that of the peptide. Total copper in the medium, measured by ICP-MS, is a further variable worth recording in such designs.

BPC-157: Signaling Pathway Studies in Cell Culture

BPC-157 is a synthetic pentadecapeptide (GEPPPGKPADDAGLV). No receptor for it has been confirmed, and the published literature has examined intracellular signaling pathways in cultured cells exposed to it.

A frequently cited pathway in these laboratory models is vascular endothelial growth factor (VEGF) signaling. Published work in cultured endothelial cells has measured the expression of VEGF receptor 2 (VEGFR2) in the presence of the peptide, a readout that concerns receptor-level expression rather than ligand concentration alone. Such designs typically include VEGF-only and vehicle controls, and they report receptor levels by western blotting or flow cytometry.

A second pathway examined in this literature is Focal Adhesion Kinase (FAK) signaling. FAK is a non-receptor tyrosine kinase that integrates signals from integrins and growth factor receptors at focal adhesions. Chang et al. (2011) examined the phosphorylation state of FAK and of its partner protein paxillin in cultured tendon fibroblasts exposed to BPC-157, using western blotting with phospho-specific antibodies. In designs of this kind, phosphorylation is quantified relative to total protein, time courses are run to capture transient signals, and a pharmacological FAK inhibitor is often included as a tool compound. Gap-closure (scratch) and endothelial network formation assays are the functional formats most often paired with such measurements. The published literature has also examined the nitric oxide system in relation to BPC-157, which is one reason nitric oxide synthase inhibitors are sometimes included as tool compounds in such designs.

TB-500: An Actin-Binding Peptide

TB-500 is synthetic material corresponding to thymosin beta-4 (Tβ4), the 43-residue, N-terminally acetylated peptide (approximately 4963 Da) found at high concentrations in platelets and many other cell types; as with any product sold under this name, the sequence stated in the documentation should be checked. The most thoroughly characterized biochemical property of Tβ4 is its binding to monomeric actin, a core component of the cytoskeleton.

The biochemistry centers on actin sequestration. In the cellular cytoplasm, actin exists in a dynamic equilibrium between monomeric globular actin (G-actin) and filamentous polymeric actin (F-actin). Tβ4 binds G-actin monomers in a 1:1 complex, preventing them from polymerizing. In cells, this maintains a large pool of unpolymerized G-actin. The cell-biology literature describes how this pool can be released to other actin-binding proteins, such as profilin, allowing rapid, localized F-actin polymerization at the leading edge of the cell, where protrusions like lamellipodia and filopodia form.

Actin binding makes thymosin beta-4 a common reagent for cell biologists studying cytoskeletal rearrangement. In endothelial cell migration assays, for example, it is used to examine the rate-limiting steps of actin polymerization. By providing a pool of sequestered G-actin, researchers can investigate how other signaling pathways, such as the Rho-family GTPases Rac1 and Cdc42, determine where and when actin assembly occurs. Published work has also examined cytokine and chemokine expression in cells exposed to thymosin beta-4, with reference to the NF-κB pathway (Goldstein et al., 2005). Within this formulation, the component therefore offers a way to study the interplay between cytoskeletal mechanics and cytokine signaling in cell models.

KPV: A Melanocortin-Derived Tripeptide

The tripeptide KPV (Lys-Pro-Val) corresponds to the C-terminal fragment of alpha-melanocyte-stimulating hormone (α-MSH). While α-MSH acts at melanocortin receptors such as MC1R, published work on KPV describes activity in cell models through both receptor-dependent and receptor-independent routes, which is one reason it is used as a tool for dissecting signaling pathways.

The pathway most often examined in KPV studies is Nuclear Factor-kappa B (NF-κB) signaling. NF-κB is a family of transcription factors that controls the expression of many cytokine genes (like TNF-α, IL-1β, and IL-6), chemokines, and adhesion molecules. In an unstimulated cell, NF-κB is held inactive in the cytoplasm by an inhibitory protein called IκBα. Upon receiving an inflammatory stimulus (e.g., lipopolysaccharide (LPS) in a macrophage cell line), IκBα is phosphorylated and degraded, allowing NF-κB to translocate to the nucleus and initiate transcription.

Published work, including that summarized by Brzoska et al. (2008), describes KPV entering cells and interfering with this sequence, apparently upstream of IκBα phosphorylation, so that NF-κB remains in the cytoplasm. In cell culture systems such as LPS-stimulated RAW 264.7 macrophages, researchers use KPV to examine how interrupting NF-κB signaling at this point changes downstream gene expression. Its ability to act intracellularly makes it a convenient probe for cytoplasmic signaling events.

Analytical Verification of a Multi-Component Formulation

In research, reproducibility depends on knowing exactly what a reagent contains. For a formulation with four components, that means documentation covering each one. The sections below describe the analytical methods involved and what each shows.

High-Performance Liquid Chromatography (HPLC) for Purity Assessment

HPLC is the standard technique for determining the chromatographic composition of synthetic peptides. It separates components according to how strongly each interacts with a stationary phase as a solvent gradient carries them through a column.

1. The Process: A small, precise amount of the dissolved sample is introduced into the system by an autosampler. For peptides, reversed-phase HPLC on a C18 column is typical, with a gradient of water and acetonitrile containing an ion-pairing additive.
2. Separation in a Four-Component Sample: The two tripeptides, GHK-Cu and KPV, are very polar and elute early, sometimes close to the solvent front, which makes retention of the early part of the gradient a real method-development problem. BPC-157 and thymosin beta-4 elute later and at different positions. A single method that resolves all four, along with each component's impurities, usually needs a shallower gradient than a single-peptide method and may require an alternative stationary phase or a HILIC method for the polar components.
3. Detection: A UV detector measures absorbance at 210 to 220 nm, where the peptide bond absorbs. Only thymosin beta-4 contains an aromatic residue (a single phenylalanine), so absorbance at 280 nm is of limited use here. For GHK-Cu, monitoring in the visible region provides a channel that is specific to the copper complex.
4. Interpretation: Because UV response at low wavelength scales roughly with the number of peptide bonds, a 43-residue peptide gives a much larger signal per mole than a tripeptide. Relative peak areas therefore cannot be read as a molar ratio without calibration against reference standards of each component. The method conditions should always accompany any reported figure.

Mass Spectrometry (MS) for Identity Verification

While HPLC confirms purity, it does not confirm identity. Mass spectrometry is used to verify that the peptide has the correct molecular weight, which corresponds to its amino acid sequence.

1. The Process: A sample is ionized, usually by electrospray ionization, and the resulting ions are separated by mass-to-charge ratio. Liquid chromatography coupled to mass spectrometry (LC-MS) performs the separation and the identification in one run, which is the practical approach for a multi-component sample.
2. What to Expect: Each component has its own signature. KPV appears near m/z 343.2 as the protonated molecule; GHK near m/z 341, with the copper complex identifiable by the distinctive 63Cu/65Cu isotope pattern, two mass units apart in roughly a 69:31 ratio; BPC-157 near m/z 710.8 as its doubly charged ion; and thymosin beta-4 as an envelope of multiply charged ions deconvoluted to about 4963 Da.
3. Why It Matters Here: With four components of very different mass, mass spectrometry is the only method that assigns each chromatographic peak unambiguously. It also detects the characteristic variants of each component, such as a species 16 Da heavier than thymosin beta-4 indicating methionine oxidation.

Endotoxin Analysis for Cellular Assay Viability

Endotoxins, specifically lipopolysaccharides (LPS), are components of the outer membrane of Gram-negative bacteria. Even trace amounts can elicit strong inflammatory or cytotoxic responses in in-vitro cell cultures, confounding experimental results. For any research involving immune cells, endothelial cells, or fibroblasts, controlling for endotoxin contamination is non-negotiable.

The industry standard for endotoxin detection is the Limulus Amebocyte Lysate (LAL) test.

1. The Principle: This test utilizes a protein lysate extracted from the blood cells (amebocytes) of the horseshoe crab (Limulus polyphemus). This lysate contains enzymes that trigger a coagulation cascade in the presence of endotoxins.
2. The Assay: In the chromogenic version of the test, the peptide sample is incubated with the LAL reagent. If endotoxins are present, they activate the enzyme cascade, which in turn cleaves a specific substrate, producing a colored product (often yellow). The intensity of the color is directly proportional to the amount of endotoxin in the sample and can be measured with a spectrophotometer.
3. Interpretation: Results are reported in Endotoxin Units (EU) per milligram (or per vial). A low EU/mg value helps ensure that an observed cellular response reflects the experimental conditions rather than bacterial contamination. When endotoxin testing is performed, results are reported in EU/mg; where the documentation for a material does not include an endotoxin value, a laboratory can commission the test itself before using that material in sensitive cell-based assays.

Net Peptide Content, Water, Counter-Ions and Copper

A lyophilized vial contains more than peptide: counter-ions from purification, residual water and, in this case, copper.

• Amino Acid Analysis (AAA): The established method for determining net peptide content. A weighed sample is hydrolyzed and the liberated amino acids are separated and quantified. For a four-component formulation, AAA reports total peptide content rather than the split between components, because all four contribute to the same amino acid pool. Some residues also need modified methods: tryptophan is destroyed by conventional acid hydrolysis and methionine recovery is variable.
• Karl Fischer Titration: Determines residual water, which contributes to total mass and, if high, accelerates degradation during storage.
• Counter-Ion Analysis: Ion chromatography, or 19F NMR for trifluoroacetate, quantifies the counter-ion. Two of the four components, GHK and KPV, are small basic peptides, so counter-ions account for a significant share of their mass; BPC-157 and thymosin beta-4 are acidic overall, but their protonated lysine side chains still carry counter-ions.
• Copper Determination: ICP-OES or ICP-MS gives an elemental copper value for the GHK-Cu component, which together with the peptide data indicates the stoichiometry of that complex.
• Residual Solvent Analysis: Headspace gas chromatography detects solvents carried through from synthesis and purification, which is relevant when material will be used in cell culture.

Together these values allow a laboratory to convert a weighed mass of powder into quantities of peptide, which is the basis of any molar calculation.

Laboratory Storage and Handling of the Lyophilized Formulation

Careful handling of a lyophilized formulation protects the material and keeps records accurate. With four components of different chemistry in one vial, the storage conditions must satisfy the most sensitive of them. The practices below apply to the dry material and describe laboratory practice only.

Storage Conditions

1. Temperature: Store sealed vials at -20°C, or -80°C for extended archiving, preferably in a manual-defrost freezer, because frost-free units periodically warm to remove ice.
2. Moisture: All four components are hygroscopic. Keep vials sealed and, where practical, in a secondary container with desiccant.
3. Light and Air: Because thymosin beta-4 contains a methionine and GHK-Cu absorbs visible light, keep vials in their carton and minimize the time they stand open.
4. Chemical Environment: Keep the material away from chelating agents and from strong acids or bases, which could alter the copper coordination of the GHK-Cu component.
5. Monitoring: A freezer temperature log documents that conditions were maintained through a project.

Receiving and Recording

On arrival, inspect each vial for an intact seal and cap, legible labeling and a dry, uniform powder; the GHK-Cu content gives the material a blue to violet cast, and a faded or patchy appearance may indicate moisture uptake. Confirm that the product name and any reference number match the Certificate of Analysis on file, then record the date of receipt, quantity, storage location and COA reference in the laboratory inventory.

Opening and Weighing the Dry Powder

1. Equilibration: Allow the sealed vial to reach room temperature for 15 to 20 minutes before opening, so that humid air does not condense on the cold powder.
2. Centrifugation: Briefly centrifuge the sealed vial so that any powder dislodged in transit collects at the bottom.
3. Weighing: Use a calibrated microbalance with static control, work quickly in low humidity and reseal the vial promptly.
4. Calculation Basis: Use the net content the COA reports for each component when converting powder mass into quantities of each peptide. Because the components differ in mass by more than a factor of ten, a mass ratio and a molar ratio for the same formulation are very different numbers, and any record should state which is meant.
5. Cleanliness: Use clean spatulas and weighing vessels. A laboratory that also performs trace elemental analysis should keep dedicated tools for a copper-containing material.

Protective Equipment, Records and Disposal

Wear gloves, a lab coat and eye protection, and weigh fine powders in a draft-shielded enclosure. Hazard and disposal information is available on our Safety Data Sheets page. Log each opening of a vial and the quantity removed, and dispose of expired or unneeded material through institutional chemical waste procedures; copper-containing waste is often subject to specific local requirements.

Comparative Framework for Research Peptide Selection

Which material suits an experiment depends on the question being asked. A multi-component formulation, a single peptide and a receptor-focused ligand are documented and used differently, as the table below sets out.

KLOW Blend Research FAQ

1. What is the rationale for combining these four peptides in one vial? The four components have been examined in separate areas of the published cell-biology literature: a copper tripeptide studied in matrix gene expression, a pentadecapeptide studied in signaling pathways, an actin-binding peptide studied in cytoskeletal dynamics, and a melanocortin-derived tripeptide studied in NF-κB signaling. Holding them in one vial is a matter of convenience and of a fixed, documented ratio. It does not by itself establish anything about their combined behaviour, which is why comparator arms with the individual peptides are needed in any experiment.

2. How is the ratio of the four peptides established? Fixed-ratio blends are generally prepared by combining measured masses of each component. The label amounts for this formulation are 50 mg of GHK-Cu with 10 mg each of BPC-157, TB-500 and KPV. Checking the ratio afterwards requires a chromatographic method calibrated with reference standards of each component, because UV response per mole differs sharply between a tripeptide and a 43-residue peptide.

3. What control groups are essential when using a four-component formulation? At minimum: a vehicle control with the solvent alone; each of the four components alone at the concentration it contributes in the formulation; the complete formulation; and a reference compound appropriate to the endpoint. For the GHK-Cu component, a copper salt and the apo-peptide are also useful arms, because an effect could arise from the metal, the peptide or the complex. Without these arms, a result obtained with the formulation cannot be attributed to any component or to the combination.

4. What in-vitro assays are used with these components? The published literature on the individual components uses standard cell-biology formats: gap-closure (scratch) assays and transwell assays for cell migration; endothelial network formation assays on a matrix substrate; quantitative PCR and western blotting for gene and protein expression, including phosphorylated signaling proteins; immunoassays for secreted proteins; and enzyme assays in purified systems for copper-dependent enzymes. Each requires its own controls, and each should be run with all the comparator arms described above.

5. Does the molecular weight difference between the components matter? Considerably. The formulation contains two tripeptides of about 340 g/mol, a 15-residue peptide of about 1420 g/mol and a 43-residue peptide of about 4963 g/mol. On an equal-mass basis, a tripeptide contributes roughly fourteen times as many molecules as the largest component. The size difference also affects chromatographic behaviour, UV response, diffusion in gels and adsorption to plastic surfaces. Any record of the formulation should therefore state whether a ratio is expressed by mass or by moles.

6. Why is the formulation supplied lyophilized? Lyophilization removes water by sublimation under vacuum, leaving a dry powder in which hydrolysis and other degradation pathways are much slower than in solution. It also allows the laboratory to choose the buffer and concentration appropriate to its own work rather than accepting a supplier's choice. For a four-component material, the dry state additionally avoids the possibility of interactions between components in solution during long storage.

7. Should all four components be visible in one HPLC chromatogram? In principle yes, provided the method has been developed for the formulation. In practice the two tripeptides elute very early and can be poorly resolved from the solvent front under a method optimized for the larger peptides, which is why a method for a mixture like this often uses a shallower initial gradient, an alternative stationary phase, or a separate HILIC method for the polar components. Peak assignment should always be confirmed by mass spectrometry rather than by retention time alone.

8. What does "salt form" or "counter-ion" mean on a Certificate of Analysis? Peptides are cleaved from the synthesis resin with a strong acid and purified by chromatography using acidic mobile phases, so the isolated product is a salt. The accompanying anion, commonly trifluoroacetate or acetate, is the counter-ion. It contributes to the total mass of the powder, which is why net peptide content is lower than the total, and residual trifluoroacetate can interfere with some cell-based assays. Two of the four components here, GHK and KPV, are small basic peptides with several protonatable groups on a low molecular weight, so counter-ions make up a meaningful share of their mass. BPC-157 and thymosin beta-4 are acidic overall, but their lysine side chains, and the free N-terminal amine of BPC-157, are protonated under acidic purification conditions and also pair with counter-ions.

9. How does the copper in GHK-Cu affect use in cell culture? Copper coordination is central to that component's chemistry, and it is also the part most easily disturbed. Culture media contain amino acids, serum proteins and buffer components that can compete for copper, and phosphate can form insoluble copper salts over time. For analytical work, a non-coordinating buffer and freshly prepared solutions are preferred, and the visible absorption band can be used to check that the complex is intact under the chosen conditions. Copper-only and apo-peptide controls are essential in any cell-based design.

10. What is the significance of the "pentadecapeptide" designation for BPC-157?

"Pentadecapeptide" simply means that the peptide is composed of 15 ("penta-" + "deca-") amino acids. This is a structural classification. Its length places it in a middle ground—larger than small signaling peptides like KPV but much smaller than proteins. This intermediate size influences its stability, diffusion properties, and how it interacts with cellular receptors and enzymes, making its structural identity a key piece of information for researchers designing experiments.

Glossary of Associated Research Terminology

• Actin Sequestration: The binding of G-actin monomers by actin-binding peptides, which prevents their polymerization into F-actin filaments and maintains a pool available for cytoskeletal assembly.
• Chelation: The binding of a single ligand molecule to a metal ion at more than one donor atom, as in the GHK-copper complex.
• Chemotaxis: The directed movement of a motile cell in response to a chemical gradient.
• Coordination Sphere: The set of donor atoms directly bound to a metal centre, together with their geometric arrangement.
• Counter-ion: An ion that accompanies a charged peptide to maintain electrical neutrality, commonly acetate or trifluoroacetate from purification.
• Cytokine: A small secreted protein that carries signals between cells, measured in many cell-culture assays.
• Cytoskeleton: A network of interlinking protein filaments in the cytoplasm that provides structure and supports cell movement.
• Extracellular Matrix (ECM): A three-dimensional network of extracellular macromolecules, such as collagen, elastin and glycoproteins, surrounding cells.
• Fibroblast: A cell type that synthesizes extracellular matrix components and collagen, widely used in cell-culture research.
• Focal Adhesion Kinase (FAK): A cytoplasmic tyrosine kinase that concentrates at sites of cell adhesion to the extracellular matrix and participates in migration signaling.
• HILIC: Hydrophilic interaction liquid chromatography, a separation mode suited to very polar compounds such as short peptides.
• ICP-MS / ICP-OES: Inductively coupled plasma mass spectrometry and optical emission spectrometry, elemental techniques used to quantify metals such as copper.
• In-Vitro: A process performed in a test tube, culture dish or elsewhere outside a living organism.
• Lamellipodia: Broad, sheet-like protrusions of the plasma membrane at the advancing edge of a migrating cell, driven by actin polymerization.
• Lyophilization: A freeze-drying process that removes water by sublimation under vacuum, giving a stable powder.
• Matrix Metalloproteinase (MMP): A family of zinc-dependent endopeptidases that degrade extracellular matrix proteins; their expression and activity are standard readouts in matrix biology.
• NF-κB: A transcription factor complex held inactive in the cytoplasm by IκBα and released on stimulation, which regulates transcription of cytokine genes.
• Pentadecapeptide: A peptide consisting of a chain of 15 amino acids linked by peptide bonds.
• Speciation: The distribution of a metal among its possible chemical forms in a given system, dependent on pH, concentration and competing ligands.
• VEGF (Vascular Endothelial Growth Factor): A signal protein that participates in blood vessel formation and is a common variable in endothelial cell assays.

Selected References

• Brzoska T, Luger TA, Maaser C, Abels C, Böhm M. Endocr Rev. 2008;29(5):581-602.
• Chang CH, Tsai WC, Lin MS, Hsu YH, Pang JH. J Appl Physiol. 2011;110(3):774-780.
• Goldstein AL, Hannappel E, Kleinman HK. Trends Mol Med. 2005;11(9):421-429.
• Maquart FX, Pickart L, Laurent M, Gillery P, Monboisse JC, Borel JP. FEBS Lett. 1988;238(2):343-346.
• Perkins CM, Rose NJ, Weinstein B, Stenkamp RE, Jensen LH, Pickart L. Inorg Chim Acta. 1984;82(1):93-99.
• Pickart L, Vasquez-Soltero JM, Margolina A. Biomed Res Int. 2015;2015:648108.
• Safer D, Elzinga M, Nachmias VT. J Biol Chem. 1991;266(7):4029-4032.
• Sikiric P, et al. J Physiol Pharmacol. 2013;64(2):177-187.

All compounds, including the KLOW Blend, are sold strictly for in-vitro laboratory research use. They are not intended for human or veterinary use of any kind, and they have not been approved by any regulatory agency for use in humans. The information presented here is for educational purposes for qualified researchers and describes laboratory methods only. Researchers are responsible for the proper handling, storage and disposal of these materials in accordance with institutional procedures and applicable regulations. For questions about our research products, please contact our support team at info@excaliburpeptides.com.