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Klow Blend (80mg)
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Klow Blend (80mg)

Original price was: $189.99.Current price is: $174.99.

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*Disclaimer: This product is intended solely for laboratory research purposes. It is not suitable for consumption by humans, nor for medical, veterinary, or household purposes. Kindly review our Terms & Conditions before making a purchase.

Always quality-tested, verified with third party COA’s

 

At every step, we prioritize quality by conducting rigorous third-party testing on all our products. These tests focus on five key characteristics- identity, purity, sterility, and endotoxin levels, and heavy metal content-ensuring that each product meets the highest standards of quality with independent third-party Certificates of Analysis (COAS) to verify our commitment to excellence.

Identity Test

Identity testing ensures that the product contains the correct ingredient as labeled, verifying its authenticity and matching it to established reference standards.

Purity Test

Purity and concentration testing verifies that the ingredient is present in the correct amount, with a purity of 99% or higher to meet stringent quality standards.

Sterility Test

Sterility testing ensures that the product is completely free from bacteria, fungi, and other microorganisms.

Endotoxin Test

Endotoxicity testing specifically detects and quantifies lipopolysaccharides (LPS), components of bacterial cell walls, to ensure the product is free from endotoxins.

Heavy Metals Test

Heavy metals testing ensures that the product is free of heavy metals such as lead, arsenic, mercury, cadmium, and other heavy metals.

Identity Test

Identity testing ensures that the product contains the correct ingredient as labeled, verifying its authenticity and matching it to established reference standards.

Purity Test

Purity and concentration testing verifies that the ingredient is present in the correct amount, with a purity of 99% or higher to meet stringent quality standards.

Sterility Test

Sterility testing ensures that the product is completely free from bacteria, fungi, and other microorganisms.

Endotoxin Test

Endotoxicity testing specifically detects and quantifies lipopolysaccharides (LPS), components of bacterial cell walls, to ensure the product is free from endotoxins.

Heavy Metals Test

Heavy metals testing ensures that the product is free of heavy metals such as lead, arsenic, mercury, cadmium, and other heavy metals.

*Disclaimer: This product is intended solely for laboratory research purposes. It is not suitable for consumption by humans, nor for medical, veterinary, or household purposes.Kindly review our Terms & Conditions before making a purchase.

Klow Blend (80 mg) is a synthetic multi-peptide research formulation combining bioactive signaling fragments such as BPC-157, TB-500 (thymosin β4–derived), KPV, and GHK-Cu. These peptides are usually characterized across wound-healing, extracellular matrix, and inflammatory signaling studies and investigated for pathways involving tissue remodeling, cytoprotection, and peptide-mediated cellular communication. Researchers can buy 99.9%+ purity Klow Blend from Spark Peptide, produced to exacting standards and verified via HPLC and mass spectrometry, with Certificates of Analysis. Sold for research use only.

Klow Blend Overview

Researchers who buy our Klow Blend often use this multi-peptide formulation to examine coordinated biological processes related to tissue repair, inflammatory signaling, and extracellular matrix regulation. The blend combines several well-studied bioactive peptides frequently investigated in regenerative biology and cellular signaling research.  Spark Peptide provides Klow Blend for sale with rigorous analytical verification and batch-specific COA documentation, supporting reproducible work in receptor signaling studies, cellular pathway investigations, and experimental tissue-repair models.

Molecular Origin

Klow Blend is a composite research formulation composed of several short bioactive peptides derived from naturally occurring signaling molecules involved in tissue maintenance and cellular repair pathways. The blend typically includes peptides such as:
  • BPC-157, a fragment derived from a gastric protective protein
  • TB-500, a synthetic fragment modeled after thymosin beta-4
  • KPV, a tripeptide fragment of the proopiomelanocortin (POMC) peptide hormone α-MSH, and
  • GHK-Cu, a copper-binding tripeptide originally isolated from human plasma.
These molecules originate from distinct physiological systems, including inflammatory signaling networks, extracellular matrix regulation, and cellular migration pathways. Many of the parent molecules were first characterized in biochemical and physiological research between the 1970s and 1990s, during early investigations into wound healing, immune signaling, and peptide-mediated cellular communication. Structurally, these peptides are defined by short amino acid sequences that correspond to biologically active domains within larger proteins or hormones. Synthetic replication of these sequences allows researchers to isolate specific signaling effects associated with those active regions. Modern peptide production relies on solid-phase peptide synthesis (SPPS), a laboratory method that sequentially assembles amino acids onto a solid resin support, enabling precise control of peptide sequence and purity. The individual peptide components are produced separately and then carefully blended under controlled laboratory conditions to maintain compositional accuracy and analytical purity across the final formulation.  Because these peptides represent defined signaling fragments, they are frequently used in experimental systems designed to investigate receptor interactions, inflammatory mediators, and intracellular signaling pathways involved in tissue remodeling.

Purity & Quality Standards

Klow Blend supplied by Spark Peptide is manufactured to 99.9%+ purity verified through high-performance liquid chromatography (HPLC) analysis, supporting consistency in laboratory research applications. Production follows cGMP-certified manufacturing processes and aligns with ISO 9001:2015 quality management standards to maintain strict batch-to-batch quality control. Additionally, each lot undergoes Spark Peptide’s 6X Safety Testing protocol, which includes HPLC purity verification, mass spectrometry identity confirmation, heavy metal screening, endotoxin testing, bacterial contamination analysis, and solubility and stability testing. To support this, verified Certificates of Analysis (COAs) are provided for every batch. Spark Peptides packages lyophilized peptides using protective materials designed to reduce temperature fluctuations during shipping. This improves stability during transit under typical ambient conditions. 

Klow Blend Mechanism of Action

Klow Blend combines several short bioactive peptides that have been investigated in experimental systems for their roles in cellular signaling, cytoskeletal regulation, and inflammatory pathway modulation. Because each component peptide interacts with distinct molecular targets, the blend represents multiple mechanistic pathways operating in parallel. The following section outlines the primary receptor interactions and molecular signaling events associated with the individual peptide components based on findings from preclinical and biochemical studies.

Receptor Binding & Primary Signaling

Klow Blend contains several short bioactive peptides that interact with distinct molecular targets involved in cellular signaling, cytoprotection, and inflammatory regulation. For starters, KPV (Lys-Pro-Val), is derived from the C-terminal sequence of α-melanocyte-stimulating hormone (α-MSH) and retains partial affinity for melanocortin receptor family members, particularly the G-protein-coupled melanocortin-1 receptor (MC1R). Activation of melanocortin receptors typically couples to Gs proteins, promoting adenylyl cyclase activation and elevation of intracellular cAMP, which subsequently initiates protein kinase A (PKA) signaling cascades(1). GHK-Cu, a copper-binding tripeptide, interacts with extracellular matrix components and cell surface integrins rather than classical GPCRs. Experimental studies suggest that GHK-Cu can modulate integrin-mediated signaling pathways and influence cellular migration and extracellular matrix remodeling through copper-dependent redox and metalloproteinase regulatory mechanisms(2). Another component, TB-500 (a synthetic thymosin β4 fragment), does not bind a single classical receptor but instead interacts with intracellular actin monomers. Thymosin β4 derivatives regulate actin polymerization by sequestering G-actin, thereby influencing cytoskeletal organization and cell motility in experimental systems(3). For its part, BPC-157, a gastric peptide fragment originally isolated from human gastric juice, has been investigated in receptor-independent signaling contexts, including modulation of nitric oxide–related pathways and interactions with vascular endothelial growth factor (VEGF) signaling networks in cellular models(4). Together, these peptides represent distinct molecular classes whose primary biochemical interactions involve GPCR signaling, integrin-mediated pathways, cytoskeletal regulation, and nitric oxide–associated signaling mechanisms.

Downstream Biological Cascades

Following the initial receptor or molecular interactions, the peptides present in Klow Blend influence multiple intracellular signaling cascades that regulate gene transcription, cytoskeletal dynamics, and inflammatory mediator production in experimental systems. Melanocortin receptor activation by KPV-related signaling has been associated with increased intracellular cAMP and activation of the PKA pathway, which can modulate transcription factors such as CREB and influence cytokine expression patterns in immune cell models(1). These signaling events have been observed to affect inflammatory mediator production and cellular stress responses in vitro. GHK-Cu has been shown in cellular assays to influence gene expression patterns related to extracellular matrix remodeling and tissue architecture. Transcriptomic analyses indicate modulation of pathways associated with metalloproteinases, integrin signaling, and antioxidant responses, often involving MAPK/ERK and PI3K/Akt signaling intermediates(2). TB-500–derived thymosin β4 fragments affect actin dynamics and cytoskeletal organization, processes that regulate cell migration and differentiation in developmental and regenerative biology studies. These effects are mediated through regulation of actin polymerization and downstream activation of cell motility pathways, including focal adhesion kinase signaling networks(5). BPC-157 has been reported in preclinical models to interact with nitric oxide signaling systems and endothelial regulatory pathways, with downstream involvement of PI3K/Akt and ERK signaling cascades that influence vascular and cellular stress responses(4). Collectively, these pathways illustrate how the individual peptides within the blend engage multiple intracellular signaling networks frequently examined in studies of inflammatory signaling, extracellular matrix regulation, and cellular adaptation processes.

Key Scientific Features & Chemical Profile of KLOW Blend

Klow Blend represents a multi-component research compound rather than a single defined peptide, so its chemical profile reflects the individual characteristics of each constituent molecule.

Molecular Data

Property Value
Molecular Formula KPV: C16H30N4O4 GHK-Cu: C28H48N12O8TB-500: C212H350N56O78S BPC-157: C62H98N16O22
Molecular Weight KPV: 342.43 g/mol GHK-Cu: 744.3 g/molTB-500: 4963 g/mol BPC-157: 1419.5 g/mol
Amino Acid Sequence KPV: H-Lys-Pro-Val-OH GHK-Cu: (glycyl-L-histidyl-L-lysine)TB-500: SDKPDMAEXEKFDKSKLKKXEXQEKNPLPSKEXXEQEKQAGES BPC-157: GEPPPGKPADDAGLV
CAS Number KPV: 67727-97-3 GHK-Cu: 89030-95-5TB-500: 885340-08-9 BPC-157: 137525-51-0
PubChem CID KPV: 125672 GHK-Cu: 133697840TB-500: 45382195 BPC-157: 9941957
Synonyms Klow Blend, KLOW Peptide Blend
Physical Form Lyophilized white powder
Solubility Soluble in sterile water, bacteriostatic water, or DMSO depending on laboratory protocol
Storage −20 °C, desiccated, protected from light

Analytical Verification

Each batch of Klow Blend supplied by Spark Peptide is accompanied by a verified Certificate of Analysis (COA) documenting batch-specific analytical data used to confirm identity, composition, and purity. High-Performance Liquid Chromatography (HPLC) is applied to evaluate peptide purity, allowing separation and quantification of peptide components within the formulation and confirming purity levels exceeding 99.9%. Molecular identity of the constituent peptides is further confirmed using mass spectrometry, which compares the experimentally observed molecular mass to the theoretical mass expected for each peptide sequence. Beyond identity and purity confirmation, Spark Peptide applies a 6X Safety Testing protocol designed to support experimental reproducibility and laboratory confidence. This verification process includes:
  • HPLC purity analysis to quantify peptide composition
  • Mass spectrometry (MS) for molecular identity confirmation
  • Heavy metals screening to detect trace metal contaminants
  • Endotoxin testing to identify bacterial endotoxin presence
  • Bacterial contamination analysis for microbiological safety
  • Solubility and stability assessment under controlled laboratory conditions
Together, these analytical procedures provide researchers with documented verification of peptide integrity and batch consistency prior to laboratory use.

Storage, Handling, and Reconstitution

Proper storage and handling practices are essential for maintaining peptide stability and preserving experimental reproducibility. As a multi-peptide formulation, Klow Blend should be stored and prepared using standard laboratory protocols for lyophilized peptides. The following guidance outlines recommended storage conditions, reconstitution procedures, and routine laboratory handling precautions.

Recommended Storage Conditions

Lyophilized Klow Blend should be stored at -4°F (-20°C) in a sealed vial under dry, desiccated conditions to preserve peptide stability. The compound should be protected from direct light and moisture exposure. Under appropriate storage conditions, lyophilized peptides typically maintain stability for up to 24 months. After reconstitution, the solution should be stored under refrigeration at 36–46°F (2–8°C) and used within the recommended laboratory timeframe to minimize degradation.

Reconstitution Protocol

  1. Remove the vial from frozen storage and allow it to reach room temperature before opening.
  2. Using sterile technique, prepare an appropriate solvent such as bacteriostatic water (get Bacteriostatic Water from Spark Peptide).
  3. Slowly add the solvent along the inner wall of the vial to minimize peptide foaming or denaturation.
  4. Typical laboratory preparations use approximately 1–5 mL of solvent depending on the desired experimental concentration.
  5. Avoid vortexing or vigorous agitation. Instead, gently swirl the vial until the peptide fully dissolves.
  6. The resulting solution should appear clear and free of visible particulates.
  7. After reconstitution, store the solution at 36–46°F (2–8°C) and follow standard laboratory timelines for peptide stability.

Handling Precautions

  • Handle the compound in a clean or sterile laboratory environment.
  • Avoid repeated freeze–thaw cycles after reconstitution.
  • Use appropriate personal protective equipment (PPE), including gloves and lab coats.
  • Follow established laboratory research handling protocols.
  • Supplied strictly for laboratory research use only and not intended for human consumption.

Klow Blend Research & Scientific Applications

Klow Blend is investigated in laboratory research as a multi-peptide system representing several biologically active signaling fragments involved in cytoskeletal dynamics, inflammatory signaling, extracellular matrix regulation, and cellular stress responses. Preclinical data suggest that its individual components are frequently studied in experimental models examining cell migration, inflammatory mediator signaling, and gene expression pathways associated with tissue remodeling and cellular adaptation.

Preclinical & Diagnostic Research

In vitro studies involving the individual peptides contained within Klow Blend have been widely used to investigate cellular signaling pathways related to inflammatory regulation, extracellular matrix turnover, and cytoskeletal organization. Cell culture models examining the tripeptide KPV (Lys-Pro-Val), derived from α-melanocyte-stimulating hormone, have demonstrated modulation of inflammatory cytokine signaling in epithelial and immune cell systems. Published findings indicate that KPV can influence transcriptional activity of pro-inflammatory mediators such as NF-κB–regulated cytokines in cultured intestinal and epithelial cells, suggesting its utility in experimental studies of inflammatory signaling pathways(6). GHK-Cu, another component of the blend, has been extensively examined in fibroblast and keratinocyte culture models. Transcriptomic studies have shown that the copper-binding tripeptide influences gene expression profiles associated with extracellular matrix remodeling, metalloproteinase regulation, and antioxidant defense systems. In vitro experiments have also demonstrated changes in integrin signaling and collagen-related gene expression markers following exposure to GHK-Cu in cultured dermal cells(7). Thymosin β4–derived peptides such as TB-500 are frequently used in cytoskeletal and cell migration studies due to their interaction with actin monomers. Experimental assays investigating actin polymerization and focal adhesion signaling have demonstrated that thymosin β4 peptides regulate actin filament dynamics, providing a useful research tool for studying cellular motility and cytoskeletal reorganization in epithelial and endothelial cell systems[3]. BPC-157 has been investigated in biochemical and endothelial cell models examining nitric oxide signaling and vascular regulatory pathways. Published findings indicate that this peptide can influence signaling intermediates associated with nitric oxide synthase activity and vascular endothelial growth factor (VEGF) pathway regulation in cultured cells[4].

Animal Model Observations

Animal model research involving the individual peptide components of Klow Blend has provided experimental insights into several physiological signaling systems, including inflammatory regulation, cytoskeletal dynamics, and extracellular matrix remodeling. Rodent studies investigating thymosin β4–derived peptides have demonstrated measurable changes in cell migration and actin-dependent cellular processes in tissue injury models.  Experimental observations in murine models have shown increased activation of cytoskeletal remodeling pathways and enhanced migration of endothelial and epithelial cells in response to thymosin β4–related peptides[3]. Research involving the copper-binding tripeptide GHK-Cu has also been explored in animal systems examining gene expression responses associated with extracellular matrix maintenance. Published studies have reported modulation of metalloproteinase activity and altered transcription of collagen-related genes in dermal tissue models following peptide exposure. These findings suggest that GHK-Cu participates in signaling pathways involved in connective tissue organization and cellular stress responses[2]. Experimental work examining KPV in rodent inflammatory models has reported measurable changes in cytokine expression profiles and reduced activity of inflammatory transcription factors such as NF-κB in intestinal and immune tissue systems. These experimental observations support the peptide’s role as a tool for studying melanocortin-related inflammatory signaling pathways in vivo[1]. Studies investigating BPC-157 in rodent models have also explored its interactions with nitric oxide signaling systems and endothelial regulatory pathways. Experimental findings suggest measurable changes in vascular signaling markers and endothelial pathway activity in preclinical models, contributing to ongoing research into peptide-mediated modulation of vascular and inflammatory signaling networks[4].

Klow Blend Comparative Analysis

Klow Blend differs from single-compound research peptides by combining several biologically active peptide fragments that influence distinct molecular pathways. Comparative analysis with commonly studied peptides helps clarify how this multi-component formulation differs in receptor targets, signaling mechanisms, and experimental research applications.

Comparison to Standard Analogs

Klow Blend differs from individual research peptides because it combines several short bioactive sequences that operate through distinct signaling systems rather than a single receptor pathway. In experimental research, two commonly studied comparator peptides are BPC-157 and TB-500 (thymosin β4–derived fragments), both of which are included as components within the blend but are frequently investigated independently. Comparative studies indicate that BPC-157 is primarily examined in experimental models involving nitric oxide signaling and endothelial pathway regulation, whereas TB-500 is associated with actin-binding activity and regulation of cytoskeletal dynamics through interactions with G-actin monomers. By contrast, Klow Blend integrates multiple signaling fragments, including KPV and GHK-Cu, in addition to BPC-157 and TB-500. This structural diversity means the blend engages several biochemical systems simultaneously, including GPCR-associated inflammatory signaling, cytoskeletal regulation, integrin-mediated pathways, and nitric oxide–related endothelial signaling. Experimental models suggest that individual peptides such as BPC-157 or TB-500 are often used to isolate a single mechanistic pathway, whereas peptide blends like Klow Blend may be examined in systems where multiple signaling pathways are studied concurrently, such as complex cellular stress models or extracellular matrix remodeling research.
Parameter Klow Blend BPC-157 TB-500
Half-life Variable; dependent on component peptides Short peptide stability; rapid enzymatic degradation in vitro Short peptide fragment; intracellular actin interaction
Receptor Selectivity Multi-target signaling fragments Nitric oxide–associated and endothelial signaling pathways Actin-binding peptide fragment affecting cytoskeletal dynamics
Primary Mechanism Multi-pathway signaling including melanocortin, cytoskeletal, and ECM-related pathways Nitric oxide signaling and endothelial pathway interactions Regulation of actin polymerization and cell motility pathways
Research Applications Multi-pathway cellular signaling and ECM studies Endothelial signaling and inflammatory pathway research Cytoskeletal dynamics and cell migration studies

Peer-Reviewed Research & Citations

  1. Luger TA, Brzoska T. "alpha-MSH related peptides: a new class of anti-inflammatory and immunomodulating drugs." Annals of the Rheumatic Diseases, vol. 66, no. Suppl 3, pp. iii52–iii55, 2007. PMID: 17934097 / DOI: 10.1136/ard.2007.079780
  2. Pickart L, Vasquez-Soltero JM, Margolina A. "GHK Peptide as a Natural Modulator of Multiple Cellular Pathways in Skin Regeneration." BioMed Research International, vol. 2015, no. 1, pp. 648108–648108, 2015. PMID: 26236730 / DOI: 10.1155/2015/648108
  3. Morita T, Hayashi K. "G-actin sequestering protein thymosin-β4 regulates the activity of myocardin-related transcription factor." Biochemical and Biophysical Research Communications, vol. 437, no. 3, pp. 331–335, 2013. PMID: 23811404 / DOI: 10.1016/j.bbrc.2013.06.069
  4. Józwiak M, Bauer M, Kamysz W, Kleczkowska P. "Multifunctionality and Possible Medical Application of the BPC 157 Peptide—Literature and Patent Review." Pharmaceuticals, vol. 18, no. 2, pp. 185–185, 2025. DOI: 10.3390/ph18020185
  5. Rahman OF, Lee SJ, Seeds WA. "Therapeutic Peptides in Orthopaedics: Applications, Challenges, and Future Directions." Journal of the American Academy of Orthopaedic Surgeons Global Research & Reviews, vol. 10, no. 1, pp. e25.00236–e25.00236, 2026. PMID: 41490200 / DOI: 10.5435/JAAOSGlobal-D-25-00236
  6. Dalmasso G, Charrier-Hisamuddin L, Nguyen HT, Yan Y, Sitaraman S, Merlin D. "PepT1-mediated tripeptide KPV uptake reduces intestinal inflammation." Gastroenterology, vol. 134, no. 1, pp. 166–178, 2008. PMID: 18061177 / DOI: 10.1053/j.gastro.2007.10.026
  7. Pickart L, Margolina A. "Regenerative and Protective Actions of the GHK-Cu Peptide in the Light of the New Gene Data." International Journal of Molecular Sciences, vol. 19, no. 7, pp. 1987–1987, 2018. PMID: 29986520 / DOI: 10.3390/ijms19071987

Certificate of Analysis & Lab Reports

Every Spark Peptide product is supplied with batch-specific analytical documentation generated by independent third-party laboratories. These reports support confirmation of compound identity, verification of purity, and screening for potential contaminants. The documentation forms part of Spark Peptide’s 6X Safety Testing protocol, providing researchers with traceable analytical data relevant to laboratory reproducibility and quality assurance.

Certificate of Analysis (COA)

The Certificate of Analysis documents the batch-specific analytical results for the manufacturing lot supplied to researchers. The report confirms compound identity, purity verification, and tested safety parameters while providing traceability through lot numbers, analytical methods, and testing dates. This documentation allows laboratories to verify the analytical characteristics of the exact batch used in experimental work.

HPLC Analysis Report

High-Performance Liquid Chromatography (HPLC) is used to evaluate peptide purity by separating the compound from potential impurities present in the sample matrix. The technique generates a chromatogram that quantifies the relative composition of the peptide components, enabling precise purity determination through peak analysis.

Mass Spectrometry Report

Mass spectrometry is used to confirm molecular identity by measuring the mass-to-charge ratio (m/z) of ionized peptide molecules. The experimentally observed molecular mass is then compared to the theoretical mass expected from the peptide sequence. Agreement between these values supports confirmation of compound identity within the analytical batch.

Additional Safety Screening

In addition to HPLC purity verification and mass spectrometry identity confirmation, Klow Blend undergoes additional analytical screening as part of Spark Peptide’s 6X Safety Testing protocol. These procedures include heavy metals screening for lead, mercury, arsenic, and cadmium; endotoxin testing using the Limulus Amebocyte Lysate (LAL) assay; and bacterial contamination analysis. Together, these tests support chemical safety and laboratory suitability. Complete analytical reports are available upon request or through the Spark Peptide Tests & Safety page.

Legal Disclaimer

For Laboratory Research Use Only. All products sold by Spark Peptide are strictly intended for laboratory research use only. These materials are not for human consumption and are not intended for medical, veterinary, diagnostic, or household use of any kind. Spark Peptide operates solely as a research chemical supplier. We are not a compounding pharmacy and do not operate as a compounding facility as defined under Section 503A of the Federal Food, Drug, and Cosmetic Act. Additionally, Spark Peptide is not registered as an outsourcing facility under Section 503B of the Act. By purchasing from our site, you agree to use our products exclusively for lawful laboratory research purposes. Any misuse is strictly prohibited.

Product FAQ for Researchers

What purity level does SparkPeptide’s Klow Blend achieve?

Spark Peptide manufactures Klow Blend to 99.9%+ purity verified through High-Performance Liquid Chromatography (HPLC). Each batch also undergoes Spark Peptide’s 6X Safety Testing protocol, which includes mass spectrometry identity confirmation, heavy metals screening, endotoxin testing, bacterial contamination analysis, and solubility and stability assessment. These analytical steps support consistent batch quality and reproducibility for laboratory research applications.

How should Klow Blend be reconstituted for laboratory use?

Klow Blend is typically reconstituted using sterile bacteriostatic water to maintain peptide stability during laboratory preparation. Researchers should allow the vial to reach room temperature before adding solvent slowly along the vial wall. Gentle swirling is recommended to dissolve the peptide without agitation. For laboratory preparation, Spark Peptide provides a compatible solvent option: Bacteriostatic Water 10ml.

What is the shelf life of Klow Blend?

When stored in lyophilized form at -4°F (-20°C) in a sealed, desiccated vial protected from light and moisture, Klow Blend typically maintains stability for up to 24 months. After reconstitution, the peptide solution should be refrigerated at 36–46°F (2–8°C) and used within the standard laboratory stability window to minimize peptide degradation.

Does this product include a Certificate of Analysis?

Yes. Every batch of Klow Blend supplied by Spark Peptide includes a batch-specific Certificate of Analysis (COA). The COA documents the analytical testing results for that manufacturing lot, including purity verification and identity confirmation. Researchers can view or download the COA directly from the product page to verify the analytical data associated with their batch.

What types of research systems commonly investigate peptides contained in Klow Blend?

The peptide components within Klow Blend are commonly studied in experimental systems examining cytoskeletal dynamics, extracellular matrix signaling, inflammatory pathway regulation, and cellular stress responses. Research models often include in-vitro cell culture systems, receptor pathway investigations, gene expression assays, and preclinical models evaluating signaling pathways related to tissue remodeling and cellular adaptation processes.

Property Detail
Name KLOW Blend (GHK-Cu + TB-500 + BPC-157 + KPV)
Components Glycyl-L-Histidyl-L-Lysine Copper Complex (GHK-Cu); Thymosin Beta-4 Fragment (TB-500); Body Protection Compound-157 (BPC-157); L-Lysyl-L-Prolyl-L-Valine (KPV)
GHK-Cu Sequence Gly-His-Lys + Cu²⁺
TB-500 Sequence 43-amino acid thymosin beta-4 peptide analog
BPC-157 Sequence Gly-Glu-Pro-Pro-Pro-Gly-Lys-Pro-Ala-Asp-Asp-Ala-Gly-Leu-Val
KPV Sequence H-Lys-Pro-Val-OH
Molecular Formula GHK-Cu: C₁₄H₂₂CuN₆O₄ / TB-500: C₃₈H₆₈N₁₀O₁₄ / BPC-157: C₆₂H₉₈N₁₆O₂₂ / KPV: C₁₆H₃₀N₄O₄
Molecular Weight GHK-Cu: 401.91 g/mol; TB-500: 889.01 g/mol; BPC-157: 1,419.54 g/mol; KPV: 342.43 g/mol
PubChem CID GHK-Cu: 378611; TB-500: 62707662; BPC-157: 9941957; KPV: 125672
Format Blue-purple lyophilized powder in sterile research vials
Total Blend Amount 80mg (combined peptide formulation)
Purity ≥99% per component, verified by third-party testing (Janoshik & Finnrick Analytics); lot-specific COAs available
Solubility Highly soluble in sterile water, bacteriostatic water, or saline; reconstitute gently to preserve peptide integrity
Storage (Lyophilized) 2–8°C (36–46°F); extended storage beyond 6 months at –20°C (–4°F); protect from light and moisture
Storage (Reconstituted) 2–8°C (36–46°F) for up to 30 days; aliquot into single-use volumes and store at –20°C to –80°C for extended use
Handling Notes Avoid repeated freeze–thaw cycles; use sterile low-binding microcentrifuge tubes for aliquoting; label with peptide identity, concentration, and preparation date
Research Designation For research use only — not approved for human or veterinary use, clinical administration, or therapeutic application
Supplier Spark Peptide

 

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