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

KLOW Peptide Blend: Interconnected Regulatory Research Platform

This sophisticated multi-peptide blend consists of four high-purity research compounds—KPV, an LL-37 Fragment, OC-51, and a WIF-1 Fragment—chosen for their crucial roles in interconnected biological regulation. The formulation serves as a powerful research platform to study how immune responses, tissue repair processes, and metabolic control pathways coordinate to maintain or restore biological integrity.

KLOW Peptide Blend Overview

The individual components provide targeted experimental control over key regulatory systems:

• KPV (Lys-Pro-Val): A melanocortin-derived tripeptide, widely researched for its capacity to suppress inflammatory signals. Its mechanism involves blocking the critical NF-kB pathway, leading to a decrease in the production of key inflammatory signaling molecules.
• LL-37 Fragment (Cathelicidin Derived): A fragment utilized in studies of host defense and epithelial healing. It is linked to enhancing cell migration and proliferation in wound models, as well as influencing local immune cell traffic.
• OC-51 (Ornithine-Containing Research Peptide): This peptide provides a means to investigate metabolic signaling and detoxification. Research targets its influence on nitrogen metabolism and the urea cycle, which are critical for balancing systemic metabolic conditions.
• WIF-1 Fragment (Wnt Inhibitory Factor-1 Fragment): An essential tool for research on cell differentiation and morphogenesis. By inhibiting the Wnt signaling cascade, it allows investigators to study the effects of specific pathway blockade on tissue development and structural changes.

KLOW Peptide Blend Structure

• Constituents: KPV, LL-37 Fragment, OC-51, WIF-1 Fragment
• Purity: Combined purity is $\ge$ 98% (by HPLC).
• Mass: Total Blend Mass is 80 mg.
• Ratio: The specific mixing ratio of the components is proprietary.

KLOW Peptide Blend Research

The combination of these peptides enables research into the integration of different physiological defenses:

• KPV: Research focuses on its ability to provide localized control over inflammation, offering insight into melanocortin receptor function in inflammatory diseases.
• LL-37 Fragment: Studies explore its dual function: strengthening host defense mechanisms while directly promoting the cellular proliferation required for tissue repair.
• OC-51: Used as a metabolic probe to study how shifts in nitrogen balance and ornithine-related pathways affect cellular energy and function.
• WIF-1 Fragment: Allows for the study of developmental control, specifically how the suppression of Wnt signaling impacts cell fate and structural patterning during tissue remodeling.

Synergistic Research Potential: The KLOW blend provides researchers with the unique ability to investigate the simultaneous interplay of these four crucial regulatory pathways, enhancing the complexity and translatability of cellular and systemic research models.

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

(List of 8 references, consistent with previous versions.)

• 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 product is supplied in a lyophilized (freeze-dried) state, ensuring stability during transit (3–4 months). After reconstitution with bacteriostatic water, the peptide solution must be refrigerated at 4 degrees C (39 degrees F), where it remains stable for up to 30 days.

Peptide State

Recommended Temperature

Storage Duration

Preservation Tip

Lyophilized

-80 degrees C (-112 degrees F)

Long-Term (Years)

Optimal storage for maintaining structural integrity.

Lyophilized

Below 4 degrees C (39 degrees F)

Short-Term (Months)

Protect from light and moisture.

Reconstituted

4 degrees C (39 degrees F)

Up to 30 Days

Avoid temperature cycling and use sterile buffers.

Best Practices for Peptide Storage

To maintain experimental accuracy, minimize freeze-thaw cycles by aliquoting the lyophilized peptide. Avoid opening cold vials until they reach room temperature to prevent condensation damage. Store all peptides in a cold, dry, and dark environment, protected from air to prevent oxidation.