KLOW Blend Molecular Weight, Sequence & CAS Reference

Analytical Overview of Multi-Component Research Blends

In analytical chemistry and preclinical peptide research, composite formulations represent a specialized methodology for evaluating potential synergistic biochemical pathways. The KLOW research formulation combines four well-characterized peptide sequences into a single lyophilized matrix: Body Protection Compound 157 (BPC-157), Thymosin Beta-4 active fragment (TB-500), Glycyl-L-histidyl-L-lysine copper complex (GHK-Cu), and the alpha-MSH derivative tripeptide (KPV). Because this preparation is a multi-target combination rather than a single chemical entity, there is no single molecular weight, primary amino acid sequence, or Chemical Abstracts Service (CAS) registry number for the mixture as a whole.

Instead, researchers analyzing the KLOW Blend 80mg must evaluate each active pharmaceutical ingredient (API) individually based on its distinct molecular structure, empirical formula, net peptide content, and trifluoroacetate (TFA) or acetate salt ratios. Understanding these constituent parameters is critical when performing mass spectrometry assaying, reverse-phase high-performance liquid chromatography (RP-HPLC), or molar concentration calculations for cell culture systems. Explore our complete library of individual compounds within all peptides for baseline analytical data.

BPC-157 Structural Specifications and Sequence Data

BPC-157 is a 15-amino acid synthetic pentadecapeptide derived from human gastric juice protein BPC. In preclinical models, it has been widely investigated for its tissue-protective signaling properties, angiogenic modulation, and nitric oxide pathway interactions. When conducting quantitative analysis, researchers should reference the precise structural metrics of the isolated molecule.

The primary amino acid sequence for BPC-157 is Gly-Leu-Pro-Pro-Pro-Gly-Lys-Pro-Ala-Asp-Asp-Ala-Gly-Leu-Val (L-form amino acids). The empirical chemical formula of the free base is C62H98N16O22, yielding a theoretical monoisotopic mass of 1418.70 Da and an average molecular weight of 1419.56 g/mol. BPC-157 is typically synthesized as an acetate or TFA salt; the CAS registry number assigned to BPC-157 acetate is 137525-51-0. Additional detailed analytical profiles for single-entity pentadecapeptides can be reviewed in our BPC-157 sequence specifications document.

TB-500 (Thymosin Beta-4 Fragment) Molecular Parameters

TB-500 generally refers to the active heptapeptide core fragment of the naturally occurring 43-amino acid protein Thymosin Beta-4 (Tβ4). While full-length Tβ4 regulates actin polymerization and cell migration, the synthetic fragment Ac-LKKTETQ is frequently utilized in laboratory research to study localized cellular signaling and actin-binding domain dynamics.

The canonical sequence for the TB-500 active fragment is N-acetyl-Leu-Lys-Lys-Thr-Glu-Thr-Gln (Ac-LKKTETQ). Its chemical formula is C38H68N10O14 with an average molecular weight of approximately 889.01 g/mol. In contrast, full-length synthetic Thymosin Beta-4 possesses the formula C212H350N56O78S1 and a molecular weight of 4963.50 g/mol (CAS 77591-33-4). The fragment TB-500 is often assigned CAS reference 885340-86-7 depending on manufacturer specifications. For a deeper breakdown of structural variants, consult the TB-500 molecular weight technical hub.

GHK-Cu Copper Tripeptide Complex Characteristics

GHK-Cu is a naturally occurring copper-binding tripeptide consisting of glycyl-L-histidyl-L-lysine complexed with a divalent copper ion (Cu2+). In cellular assays, GHK-Cu is examined for its ability to regulate gene transcription involved in extracellular matrix remodeling, collagen synthesis, and antioxidant pathway expression.

The peptide backbone sequence is Gly-His-Lys. When complexed with copper(II), the theoretical chemical formula is represented as C14H23CuN6O4 (in its neutral coordinate form), with a formula mass of approximately 404.91 g/mol. The uncomplexed GHK tripeptide free base has a molecular weight of 340.38 g/mol (C14H24N6O4). The CAS reference number for GHK-Cu is 49557-75-7 (or 89030-95-5 for specific salt/complex forms). Researchers analyzing skin fibroblast assays or matrix metalloproteinase regulation can find expanded data via the GHK-Cu copper peptide mechanism guide.

KPV Tripeptide Sequence and Chemical Metrics

KPV is a C-terminal tripeptide fragment of alpha-melanocyte-stimulating hormone (alpha-MSH, amino acids 11–13). Preclinical in vitro studies focus on its nuclear factor-kappa B (NF-kB) inhibitory activity and cellular anti-inflammatory signaling cascades without inducing melanogenesis.

The amino acid sequence is Lys-Pro-Val (L-Lysine-L-Proline-L-Valine). The molecular formula of the free peptide base is C16H30N4O4, corresponding to a precise molecular weight of 342.44 g/mol. KPV is typically supplied as an acetate salt (CAS 67727-92-6) or TFA salt. Due to its low molecular weight, KPV demonstrates high solubility in aqueous buffer systems, making it an ideal candidate for comparative signaling assays alongside larger structural peptides.

Summary Matrix of KLOW Constituent Chemical Specifications

To assist laboratory personnel in establishing accurate HPLC calibration curves and mass spectrometry parent ion identification, the physical parameters of each KLOW constituent are summarized below:

• BPC-157: Sequence = Gly-Leu-Pro-Pro-Pro-Gly-Lys-Pro-Ala-Asp-Asp-Ala-Gly-Leu-Val | MW = 1419.56 g/mol | Formula = C62H98N16O22 | CAS = 137525-51-0 • TB-500 (Fragment): Sequence = Ac-Leu-Lys-Lys-Thr-Glu-Thr-Gln | MW = 889.01 g/mol | Formula = C38H68N10O14 | CAS = 885340-86-7 • GHK-Cu: Sequence = Gly-His-Lys (Cu2+ complex) | MW = 404.91 g/mol | Formula = C14H23CuN6O4 | CAS = 49557-75-7 • KPV: Sequence = Lys-Pro-Val | MW = 342.44 g/mol | Formula = C16H30N4O4 | CAS = 67727-92-6

Because the lyophilized KLOW Blend 80mg vial contains stoichiometric ratios of these four distinct entities, spectrophotometric quantification must account for individual molar extinction coefficients at 214 nm and 280 nm.

Impact of Salt Forms (TFA vs. Acetate) on Net Peptide Content

Synthetic peptides manufactured via Solid-Phase Peptide Synthesis (SPPS) inherently retain non-covalently bound counterions from cleavage and purification reagents. The most common counterions are trifluoroacetic acid (TFA, CF3COOH) and acetic acid (CH3COOH). Understanding counterion mass fraction is essential for accurate gravimetric preparation in laboratory experiments.

Gross lyophilized mass consists of net peptide mass, counterion mass, and residual moisture. For example, a peptide supplied as a TFA salt may exhibit a net peptide purity of 98% by HPLC, yet have a net peptide content (purity factor) of 75–85% by weight due to TFA mass contribution. When calculating molarity in culture media, researchers must refer to the lot-specific Certificate of Analysis. PX1 Research provides batch-specific documentation verified via nuclear magnetic resonance (NMR) or elemental analysis; access your documentation at our Certificate of Analysis (COA) repository.

Mass Spectrometry and RP-HPLC Verification Standards

Verifying the purity and identity of a multi-peptide formulation presents unique analytical challenges compared to single-peptide solutions. In reverse-phase high-performance liquid chromatography (RP-HPLC), a hydrophobic stationary phase (such as C18) combined with a gradient of water and acetonitrile (with 0.1% TFA) is utilized to resolve each constituent based on retention time.

Electrospray Ionization Mass Spectrometry (ESI-MS) or Matrix-Assisted Laser Desorption/Ionization (MALDI-TOF) is then employed to confirm parent ion mass-to-charge (m/z) ratios. In a compliant analytical standard for KLOW, four distinct peak retention times and four corresponding m/z signals must be resolved without co-eluting impurites or unidentified degradation fragments. PX1 Research conducts rigorous HPLC/MS identity testing and endotoxin screening on every batch through an independent, ISO 17025 accredited facility.

Comparative Analysis: KLOW vs. Related Regenerative Research Peptides

In cell biology and tissue modeling research, investigators frequently compare composite blends against individual isolated peptides or simpler two-component mixtures to isolate specific biological mechanisms. For instance, standalone BPC-157 5mg is regularly evaluated for localized cellular migration assays without the modulating influence of copper ions.

Similarly, targeted studies focusing primarily on cell migration speed and actin organization may utilize isolated TB-500 2mg, whereas studies isolating extracellular matrix cross-linking often isolate GHK-Cu 50mg. Multi-component matrices like the KLOW formulation allow researchers to analyze concurrent pathway activation—such as simultaneous VEGFR2 upregulation, actin filament binding, matrix metalloproteinase suppression, and NF-kB pathway inhibition—in unified in vitro models. Researchers seeking bulk quantities for comparative multi-plate studies can apply for institutional pricing through our wholesale lab portal.

Laboratory Reconstitution and Handling Parameters

Proper reconstitution protocols are required to maintain peptide stability and prevent physical aggregation of multi-component mixtures. Lyophilized peptide vials should be allowed to equilibrate to room temperature before reconstitution to minimize condensation inside the vial.

Reconstitution should be performed using Sterile Bacteriostatic Water (0.9% Benzyl Alcohol) or Sterile Normal Saline depending on assay requirements. Liquid should be directed slowly along the glass wall of the vial, followed by gentle swirling—never vigorous vortexing—to preserve secondary structural integrity. To calculate exact volumetric dilutions, stock concentrations, and aliquot distributions, utilize our interactive reconstitution calculator. Additional background on peptide handling and solubility dynamics can be found in our comprehensive research hub.