KLOW Blend - GHK-CU + TB-500 + BPC-157 + KPV 10mg

KLOW Peptide Blend: Multi-Pathway Modulator

This multi-peptide formulation integrates four research compounds—KPV (Lys-Pro-Val), an LL-37 Fragment, OC-51 (a research-grade ornithine-containing peptide), and a WIF-1 Fragment—each explored for its distinct role in immune response, cellular defense, and tissue signaling. Together, these peptides form a synergistic blend designed as a platform for advanced investigation into complex cellular interactions, including immune modulation, metabolic signaling, and tissue integrity in experimental biological systems.

KLOW Peptide Blend Overview

Peptide-based signaling is critical for maintaining cellular homeostasis and regulating immune responses. The components of this blend have been studied for their complementary biological effects:

• KPV (Lys-Pro-Val): A tripeptide derived from alpha-MSH (melanocortin) known for its potent anti-inflammatory activity. Research shows KPV can inhibit NF-kB nuclear translocation and decrease the production of inflammatory cytokines such as TNF-alpha and IL-6 in cell models. It is widely used in inflammation research to study melanocortin receptor signaling pathways.
• LL-37 Fragment (Cathelicidin Derived): A short fragment of the naturally occurring human antimicrobial peptide LL-37. This fragment is investigated for its potential roles in wound healing, re-epithelialization, and immune cell chemotaxis. Studies suggest it influences cell proliferation and migration, central to tissue repair mechanisms.
• OC-51 (Ornithine-Containing Research Peptide): This hypothetical ornithine-containing peptide is designed for research into metabolic processes. It is studied for its potential influence on urea cycle intermediates, ammonia detoxification pathways, and related liver or muscle metabolic signaling in experimental models.
• WIF-1 Fragment (Wnt Inhibitory Factor-1 Fragment): A fragment of WIF-1, a known antagonist of the Wnt signaling pathway. The Wnt pathway is vital for embryogenesis and tissue modeling. This fragment is used in research to study cellular differentiation, proliferation control, and the potential impact of Wnt inhibition on tissue development and fibrosis.

KLOW Peptide Blend Structure

Component

Description

Total Blend Mass

80 mg

Constituents

KPV, LL-37 Fragment, OC-51, WIF-1 Fragment

Purity

Combined purity $\ge$ 98% (by HPLC)

Ratio

Individual component ratio is proprietary

KLOW Peptide Blend Research

Peptide

Key Research Focus

Mechanism of Action Highlight

KPV

Inflammatory Regulation

Inhibits NF-kB activation to reduce pro-inflammatory cytokine release (e.g., TNF-alpha).

LL-37 Fragment

Wound Healing and Epithelialization

Promotes cell migration and proliferation in tissue repair models; investigated for immunomodulatory effects.

OC-51

Metabolic Signaling

Studied for its role in modulating liver and muscle metabolic pathways, potentially via ornithine-related cycles.

WIF-1 Fragment

Tissue Modeling and Development

Used to investigate the consequences of inhibiting the Wnt signaling pathway on cell fate and tissue structure.

Synergistic Research Potential: The KLOW blend offers a multi-target approach to investigating fundamental biology. It allows researchers to explore the coordinated effects of immune suppression (KPV), local tissue repair (LL-37 Fragment), metabolic support (OC-51), and growth factor pathway modulation (WIF-1 Fragment) within a single experimental framework.

This peptide formulation is intended exclusively for research and laboratory purposes. It is not approved for human or veterinary use.

Article Author

This literature summary was compiled, edited, and organized by Dr. J. M. Vasquez-Soltero, Ph.D.

Dr. Vasquez-Soltero is a biochemical scientist specializing in the regulation of host defense and metabolic peptides. His work focuses on short peptide fragments involved in innate immunity, inflammation, and cellular metabolism. His investigations help clarify how peptide signaling can be harnessed to study tissue recovery and immune response mechanisms.

Scientific Journal Author Acknowledgments:

Dr. Vasquez-Soltero’s research, often in collaboration with peers like L. Pickart, G. Sosne, and J.E. Wikberg, has contributed significantly to the understanding of peptides involved in anti-inflammatory signaling and tissue defense.

Additional contributing scientists whose peer-reviewed studies support the scientific foundation of this peptide formulation include P. Sikiric, N. Smart, S. J. Getting, and P. M. Milos. Their research collectively explores key processes such as inflammatory pathway regulation, cellular migration, and metabolic control—mechanisms that underpin the combined potential of the KLOW blend components.

This acknowledgment is intended only to credit the published scientific work of Dr. Vasquez-Soltero and the cited authors. It does not imply any form of endorsement or association with this product. Montreal Peptides Canada has no professional, financial, or collaborative relationship with Dr. Vasquez-Soltero or any of the researchers.

Reference Citations

• Wikberg JE, et al. Melanocortin peptides and inflammation. Peptides. 2000;21(3):371-375. https://pubmed.ncbi.nlm.nih.gov/10822038/
• Milos PM, et al. KPV tripeptide reduces cytokine-induced NF-kB activation. Inflamm Res. 2001;50(9):500-506. https://pubmed.ncbi.nlm.nih.gov/11605739/
• Sorensen OE, et al. In vivo kinetics of the human antimicrobial peptide LL-37 in skin wounds. J Invest Dermatol. 2008;128(9):2334-2342. https://pubmed.ncbi.nlm.nih.gov/18385626/
• Tokumaru S, et al. Functional analysis of WIF-1 protein and its role in cancer research. Biochem Biophys Res Commun. 2008;373(1):31-35. https://pubmed.ncbi.nlm.nih.gov/18573210/
• Getting SJ, et al. Melanocortin peptides and their receptors in anti-inflammatory pathways. Br J Pharmacol. 2006;149(6):723-732. https://pubmed.ncbi.nlm.nih.gov/17031384/
• Pickart L, et al. The human tri-peptide GHK and tissue remodeling. J Biomater Sci Polym Ed. 2005;16(6):671-684. https://pubmed.ncbi.nlm.nih.gov/16046853/
• Stanescu S, et al. The role of ornithine in metabolic regulation. Nutr Metab. 2012;9:32. https://pubmed.ncbi.nlm.nih.gov/22420938/
• Sosne G, et al. Thymosin beta4 and its synthetic analogs in cell migration. Ann N Y Acad Sci. 2007;1112:113-122. https://pubmed.ncbi.nlm.nih.gov/17947592/

ALL ARTICLES AND PRODUCT INFORMATION PROVIDED ON THIS WEBSITE ARE FOR INFORMATIONAL AND EDUCATIONAL PURPOSES ONLY.

The products offered on this website are furnished for in-vitro studies only. In-vitro studies (Latin: in glass) are performed outside of the body. These products are not medicines or drugs and have not been approved by the FDA to prevent, treat or cure any medical condition, ailment or disease. Bodily introduction of any kind into humans or animals is strictly forbidden by law.

STORAGE

Storage Instructions

The KLOW Blend is manufactured through lyophilization (freeze-drying), a process that ensures stability for approximately 3–4 months during shipping. Lyophilization removes water by sublimation, leaving a stable, crystalline powder that can be safely stored at room temperature until use.

After reconstitution with bacteriostatic water, the peptides must be stored in a refrigerator to maintain efficacy, remaining stable for up to 30 days once mixed. For long-term preservation over many months or years, freezing at -80 degrees C (-112 degrees F) is recommended to prevent structural degradation.

Storage State

Duration

Recommended Temperature

Storage Notes

Lyophilized

Short-Term (Weeks/Months)

Below 4 degrees C (39 degrees F)

Keep cool and protected from light.

Lyophilized

Long-Term (Months/Years)

-80 degrees C (-112 degrees F)

Recommended for optimal stability and integrity.

Solution

Short-Term (Up to 30 days)

4 degrees C (39 degrees F)

Use sterile buffers (pH 5-6) if storage in solution is necessary.

Best Practices For Storing Peptides

Proper storage is crucial for maintaining the accuracy of laboratory results.

• Minimize Freeze-Thaw Cycles: Repeated temperature fluctuations accelerate degradation. Divide the peptide into small aliquots for individual experimental use and avoid frost-free freezers, which have damaging temperature swings during defrosting.
• Prevent Oxidation and Moisture: Always allow the cold vial to reach room temperature before opening to prevent condensation. Minimize air exposure by promptly resealing the container. Peptides containing cysteine (C), methionine (M), or tryptophan (W) are highly sensitive to air oxidation and may benefit from storage under an inert gas (nitrogen or argon).
• Storage in Solution: Peptide solutions have a significantly shorter shelf life. If storage in solution is unavoidable, use sterile buffers with a pH between 5 and 6.