Guangzhou Boyuan Outdoor Products Co., Ltd. (hereinafter referred to as "Boyuan") is a specialized biotechnology and chemical trading enterprise based in Guangzhou, China, dedicated to the research, development, sourcing, and global distribution of high-purity peptide products and related biochemical reagents. Originally established with a focus on outdoor equipment and accessories, the company has strategically pivoted and expanded its core business to become a recognized supplier in the competitive peptide market, leveraging Guangzhou's robust logistics infrastructure and its proximity to major chemical and pharmaceutical manufacturing hubs in the Pearl River Delta. Boyuan's peptide product portfolio encompasses a wide array of bioactive peptides, including but not limited to research-grade SM, TR, RT, Selank, Semax, various GHRPs (Growth Hormone-Releasing Peptides) such as GHRP-2, GHRP-6, Ipamorelin, as well as NAD⁺ (Nicotinamide Adenine Dinucleotide), MGF (Mechano Growth Factor), and many other custom peptide sequences. Each product is meticulously manufactured in state-of-the-art, GMP-compliant facilities, and undergoes stringent quality control processes, including High-Performance Liquid Chromatography (HPLC) and Mass Spectrometry (MS) analysis, to ensure purity levels typically exceeding 98% or even 99%, with detailed Certificates of Analysis (CoA) readily available for customer verification. Boyuan offers peptides in various forms to meet diverse application needs, primarily as sterile lyophilized white powders or loose blocks, supplied in standard glass vials with precise dosages ranging from 1mg, 2mg, 5mg, 10mg to custom bulk quantities, all clearly labeled with product name, purity, net content, batch number, storage conditions (typically requiring -20°C or -80°C for long-term preservation), and the corresponding CAS numbers such as 53-84-9 for NAD⁺, 77591-33-4 for TB-500 (if applicable), or sample codes for SM, TR, RT. The company assigns unique model numbers to each specification — for instance, BY-SM-5MG for SM 5mg, BY-TR-10MG for TR 10mg, BY-RT-2MG for RT 2mg, BY-NAD-100MG for NAD⁺ 100mg — ensuring clear traceability and streamlined ordering for research institutions, pharmaceutical companies, and laboratory customers worldwide. Recognizing that peptides are typically intended for in vitro laboratory research, scientific studies, and preclinical development rather than human or veterinary use (unless explicitly authorized), Boyuan strictly adheres to international trade regulations and ethical sourcing guidelines. The company provides professional technical support, stable cold-chain logistics (including freeze packs and vacuum-insulated shipping containers) to maintain product integrity during transit, and responsive after-sales service. With a dedicated quality assurance team, Boyuan can also offer custom synthesis services for rare or modified peptide sequences, providing clients with tailored solutions and flexible lead times. The company's commitment to transparency is reflected in its practice of furnishing complete documentation, including MSDS (Material Safety Data Sheets), COA, HPLC chromatograms, and stability study reports upon request. Over the years, Boyuan has cultivated a reliable distribution network covering North America, Europe, Southeast Asia, and Australia, building long-term partnerships based on consistent product quality, competitive pricing, and professional communication. Despite its origins in outdoor products, Boyuan's successful transformation into a peptide supply specialist demonstrates its agility, technical competence, and customer-centric philosophy. The company continues to invest in refining its quality management systems, expanding its peptide library, and exploring new bioactive molecules to support cutting-edge scientific discovery. For any inquiries regarding pricing, bulk orders, custom synthesis, or technical specifications, Guangzhou Boyuan Outdoor Products Co., Ltd. welcomes clients to initiate direct correspondence through its official sales channels, where a knowledgeable representative will respond with detailed product information, current stock availability, and shipment quotations tailored to specific research requirements. Through unwavering dedication to excellence, Boyuan strives to be a trusted partner in the global peptide supply chain, empowering researchers and developers with premium biochemical tools for tomorrow's breakthroughs.
GHK-CU, systematically known as copper glycyl-L-histidyl-L-lysine complex and assigned CAS number 89030-95-5, is a synthetic tripeptide coordination compound supplied as a white to off-white lyophilized powder with a model designation of P-112 and a typical purity specification of ≥99% as determined by high-performance liquid chromatography. This material consists of the endogenous tripeptide sequence glycyl-histidyl-lysine associated with a divalent copper cation in a 1:1 molar ratio, forming a stable chelate structure in which the copper center is coordinated by the amino-terminal group of glycine, the imidazole side chain of histidine, and two deprotonated amide backbone nitrogens. The resulting complex exhibits a characteristic pale blue to violet tint when dissolved in neutral aqueous buffers, originating from electronic transitions of the metal center within a distorted coordination field, with a corresponding broad absorption maximum observed between 520 and 540 nanometers in UV-visible spectroscopy. From a physicochemical standpoint, GHK-CU demonstrates favorable solubility in deionized water and phosphate-buffered saline at pH 7.2–7.4, whereas its solubility in common organic media remains limited due to the polar nature of the peptide backbone and the coordination shell surrounding the metal ion. The molecular weight of the complex is calculated as approximately 403.9 grams per mole, and its molecular formula is written as C₁₄H₂₂N₆O₄Cu. When stored as a lyophilized solid at −20°C in a desiccated, light-protected container, GHK-CU retains full chromatographic purity and metal-binding integrity for a minimum of 24 months, as confirmed by real-time stability studies. Upon reconstitution in aqueous media, however, the stability profile becomes highly dependent on several experimental parameters including pH, temperature, buffer composition, ionic strength, and the presence of competing metal chelators. At neutral to mildly basic pH values ranging from 6.5 to 8.0, the copper-peptide complex remains intact for extended periods when maintained at 4°C, with less than 5 percent decomposition observed over 72 hours as measured by reversed-phase HPLC. Acidic conditions below pH 4.0 progressively disrupt the coordination environment, leading to partial dissociation of the metal ion, which can be detected by a shift in the visible absorption maximum and an increase in intrinsic fluorescence emission from free histidine side chains. Alkaline conditions above pH 9.0 promote the formation of insoluble metal hydroxides and subsequent precipitation, rendering the solution unsuitable for precise quantitative applications. Elevated temperatures exceeding 40°C accelerate oxidative side reactions, particularly at the histidine imidazole ring, resulting in minor byproducts that are analytically resolvable but generally undesirable for high-fidelity research. The coordination chemistry of GHK-CU has been extensively characterized using nuclear magnetic resonance spectroscopy and computational modeling, which collectively confirm that the tripeptide sequence provides three anchoring points for the metal ion: the amino-terminal group of the first residue, the imidazole side chain of the central histidine, and the first two amide backbone sites after deprotonation. This arrangement yields a nearly planar geometry with a fourth equatorial position occupied by either a water molecule or a buffer anion such as phosphate. The lysine side-chain amino group, although not directly bound to the metal in the predominant solution species under neutral conditions, participates in secondary electrostatic interactions that modulate the overall stability constant and redox behavior of the complex. Each production lot of GHK-CU is subjected to a comprehensive suite of analytical tests to ensure batch-to-batch consistency and research-grade quality. The primary purity assessment is performed using analytical HPLC with ultraviolet detection at both 220 and 280 nanometers, applying a gradient elution protocol on a C18 reversed-phase column with a typical particle size of 5 micrometers and dimensions of 4.6 by 250 millimeters. A purity threshold of not less than 99 percent is established by area normalization, with individual impurity peaks each not exceeding 0.2 percent of the total integrated area. Mass spectrometric confirmation employs electrospray ionization in positive ion mode or matrix-assisted laser desorption ionization time-of-flight mass spectrometry. The observed mass-to-charge ratio for the protonated molecular ion should fall within plus or minus 0.1 percent of the calculated monoisotopic mass of the complex. In electrospray ionization mass spectra, the isotopic distribution pattern of copper—featuring two major isotopes at mass 63 and mass 65 in approximately 69 and 31 percent natural abundance, respectively—serves as an intrinsic fingerprint confirming successful metal complexation. Residual processing solvents are quantified using gas chromatography to ensure levels remain below established thresholds for research-grade biochemicals. Metal profiling by inductively coupled plasma mass spectrometry ensures that extraneous metals such as iron, zinc, nickel, lead, and mercury remain below 5 parts per million each and below 20 parts per million total for non-target metals. For researchers preparing stock solutions, it is recommended to dissolve the lyophilized powder directly into the desired buffer without predilution, as intermediate water qualities may introduce trace metals that compete for copper binding. For most applications, a 10 millimolar stock solution in water or phosphate-buffered saline is convenient, which can be further diluted to working concentrations ranging from 100 nanomolar to 500 micromolar depending on the specific experimental design. Filtration through 0.22 micrometer polyethersulfone membranes is acceptable for preparation of solutions destined for cell-free biochemical assays; however, cellulose acetate or nylon membranes should be avoided due to their documented tendency to adsorb cationic peptides. Repeated freeze-thaw cycles should be avoided once the material is reconstituted, as thawing and refreezing promotes mechanical shearing of peptide aggregates and increases the risk of metal ion leaching, evidenced by elevated free metal levels in the supernatant following centrifugation. If extended storage of reconstituted solutions is necessary, aliquoting followed by flash-freezing and storage at −80°C is the preferred method, with each aliquot used exactly once and then discarded. The certificate of analysis provided with each shipment includes validated stability data under recommended conditions: for lyophilized solid stored at −20°C in the dark, purity remains at or above 99 percent for 24 months; at 4°C in the dark, purity remains at or above 98.5 percent for 12 months; at room temperature of approximately 25°C in the dark, purity remains at or above 97 percent for 6 months, although this is not recommended for long-term archiving. For reconstituted solutions stored at 4°C in water, purity remains at or above 98 percent for 7 days; in phosphate-buffered saline at 4°C, purity remains at or above 98 percent for 5 days; and at 37°C in phosphate-buffered saline, purity remains at or above 95 percent for 24 hours. Accelerated stability studies conducted at 40°C and 75 percent relative humidity over a 4-week period indicate that the primary degradation pathway involves deamidation of the bond between the first two amino acid residues, producing a related analog as the major degradant. Secondary pathways include metal dissociation followed by oxidation of the histidine residue. These degradation products are well resolved from the parent peak by HPLC and serve as useful markers for assessing sample handling history. Standard packaging sizes for research quantities include 10 milligrams, 25 milligrams, 50 milligrams, 100 milligrams, 500 milligrams, and 1 gram, with bulk quantities available upon request. Custom synthesis services are offered for GHK-CU analogs bearing isotopic labels such as stable isotopes including nitrogen-15 or carbon-13, fluorescent tags including FITC, FAM, and TAMRA, biotinylation at the lysine side chain, or replacement of the copper center with other divalent cations such as zinc, nickel, or cobalt for comparative metal-binding studies. For researchers requiring specific counterions or salt forms, lyophilization from various buffer systems can be arranged, with residual counterion content typically quantified by ion chromatography, and reduced counterion formulations available by specialty lyophilization protocols. GHK-CU is classified exclusively as a research-grade biochemical material intended for fundamental biochemical and biophysical investigations including metal-peptide binding studies using isothermal titration calorimetry or surface plasmon resonance, metal displacement assays employing chelators to measure conditional stability constants under various pH and ionic strength conditions, oxidation experiments in cell-free fully defined buffer systems containing oxidizable substrates, spectroscopic characterization as a reference compound for unknown metal coordination environments, and formulation studies investigating stability in various excipient matrices such as trehalose, mannitol, or polysorbate 20 for the development of reference standards or control materials. In summary, GHK-CU as defined by CAS number 89030-95-5, model designation P-112, white to off-white lyophilized powder appearance, and minimum 99 percent purity by HPLC represents a well-characterized, high-purity copper-peptide complex with defined coordination chemistry, favorable solubility properties, and excellent stability in its lyophilized form, making it a reliable reference standard for laboratories investigating metal-peptide recognition and biochemical stability in controlled non-cellular systems.
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