Compounds shaping the frontier of neuroscience — from anxiolytic peptides to neurotrophic complexes.
Developed at Moscow's Institute of Molecular Genetics, Selank represents a rational design approach to neuropeptide therapeutics—a synthetic heptapeptide built upon the immune peptide tuftsin's structural scaffold. This derivative demonstrates the rare capacity to simultaneously modulate IL-6 expression and influence monoaminergic neurotransmitter systems, bridging neuroimmune signaling in ways few compounds can. Its dual action on GABA and serotonin pathways has positioned it as a cornerstone tool in anxiety neurobiology research.
Researchers investigating the intersection of immune signaling and behavioral neuroscience find Selank indispensable. Over two decades of Russian neurochemical research have characterized its mechanism across multiple systems, making it one of the most comprehensively studied synthetic anxiolytics in contemporary neuropharmacology.
Store lyophilized at -20°C in sealed vial. Upon reconstitution with bacteriostatic water, maintain at 2-8°C and utilize within 30 days. Avoid freeze-thaw cycles to preserve peptide integrity.
Developed at Moscow's Institute of Molecular Genetics, Selank represents a rational design approach to neuropeptide therapeutics—a synthetic heptapeptide built upon the immune peptide tuftsin's structural scaffold. This derivative demonstrates the rare capacity to simultaneously modulate IL-6 expression and influence monoaminergic neurotransmitter systems, bridging neuroimmune signaling in ways few compounds can. Its dual action on GABA and serotonin pathways has positioned it as a cornerstone tool in anxiety neurobiology research.
Researchers investigating the intersection of immune signaling and behavioral neuroscience find Selank indispensable. Over two decades of Russian neurochemical research have characterized its mechanism across multiple systems, making it one of the most comprehensively studied synthetic anxiolytics in contemporary neuropharmacology.
Store lyophilized at -20°C in sealed vial. Upon reconstitution with bacteriostatic water, maintain at 2-8°C and utilize within 30 days. Avoid freeze-thaw cycles to preserve peptide integrity.
Semax emerged from the same Moscow laboratory that produced Selank, but with an entirely different objective: augmenting cognitive capacity through neurotrophic upregulation. This heptapeptide analogue of the ACTH(4-10) fragment demonstrates a mechanism rare among small peptides—it crosses the blood-brain barrier intact and directly increases brain-derived neurotrophic factor expression in cortical and hippocampal regions. The result: enhanced neuroplasticity, improved dopaminergic and serotonergic tone, and measurable effects on memory consolidation in experimental models.
Where most nootropics rely on neurotransmitter modulation alone, Semax operates upstream—influencing the very production of proteins that govern synaptic remodeling. Its effects on cerebrovascular function have made it a staple in stroke recovery research, while cognitive neuroscientists value its ability to enhance working memory without stimulant-like side effects.
Store lyophilized at -20°C protected from light. Reconstitute with bacteriostatic or sterile water; maintain at 2-8°C and use within 30 days. This peptide exhibits enhanced stability compared to unmodified ACTH fragments.
Delta Sleep-Inducing Peptide represents a landmark discovery in chronobiology. Isolated from the cerebral venous blood of sleeping rabbits in 1977 by Swiss researchers Schoenenberger and Monnier, DSIP opened scientific inquiry into endogenous sleep architecture modulation. Unlike sedatives that suppress neural activity, this nonapeptide appears to facilitate natural sleep-wake transitions through circadian rhythm entrainment and stress hormone regulation.
The peptide's mechanism extends beyond simple sleep induction: it modulates stress response systems, exhibits analgesic properties in pain perception studies, and demonstrates cortisol-regulating effects that have made it valuable in neuroendocrine research. Decades of investigation have revealed DSIP's subtle, multi-system influence—acting more as a biological rhythm optimizer than a traditional sleep agent.
Store lyophilized at -20°C in amber vial to protect from light degradation. Upon reconstitution, store refrigerated (2-8°C) and utilize within 30 days for optimal peptide stability.
Sleep architecture involves layered neurochemical systems—GABAergic inhibition, serotonergic tone, melatonergic timing, and neuropeptide signaling all converge to orchestrate restorative sleep. This proprietary blend recognizes that complexity, combining DSIP with complementary peptides that target distinct but overlapping pathways in sleep-wake regulation. The formulation enables researchers to investigate multi-system sleep modulation in ways single-agent studies cannot capture.
Unlike crude sedative approaches, this blend mirrors the brain's endogenous sleep-promoting cascade—facilitating rather than forcing the transition to restorative sleep states. Chronobiology researchers studying circadian misalignment, sleep disorder pathophysiology, or the molecular architecture of sleep cycles find this combination invaluable for modeling natural sleep regulation.
Store lyophilized at -20°C protected from light and moisture. Reconstituted solution remains stable at 2-8°C for up to 30 days when stored properly. Single-use aliquoting recommended for repeated experiments.
Cerebrolysin stands apart in neuroprotection research: where most compounds target a single pathway, this pharmaceutical-grade preparation contains a complex mixture of low-molecular-weight neuropeptides and amino acids derived from porcine brain tissue. The result is a biological profile that simultaneously activates multiple neurotrophic signaling cascades—mimicking BDNF, NGF, CNTF, and GDNF pathways that govern neuroplasticity, cell survival, and synaptic remodeling.
Developed in Austria and extensively studied across European and Asian research institutions, Cerebrolysin has accumulated over 300 published studies in neurodegenerative disease models, stroke recovery, and traumatic brain injury research. Its mechanism—providing exogenous neurotrophic support when endogenous systems fail—makes it irreplaceable in neuroprotection studies where single-target interventions prove insufficient.
Store refrigerated at 2-8°C in original sealed ampules. Do not freeze. Protect from direct light. Use immediately upon opening; this product does not contain preservatives. Stable unopened for 24 months under proper conditions.
The molecules redefining metabolic research — single, dual, and triple receptor agonists.
Semaglutide represents the culmination of decades of incretin biology research. Novo Nordisk's scientists engineered this glucagon-like peptide-1 analogue with a strategic fatty acid modification that enables albumin binding, dramatically extending its half-life from minutes to days. This single molecular modification transformed GLP-1 from a rapidly degraded hormone into a sustained metabolic signaling tool, enabling researchers to study prolonged GLP-1 receptor activation without the confounding variables of pulsatile dosing.
The compound's potency at GLP-1 receptors—combined with its resistance to DPP-4 degradation—has made it the gold standard in metabolic research models. Studies investigating glucose homeostasis, pancreatic beta-cell function, appetite regulation via hypothalamic pathways, and incretin receptor pharmacology consistently rely on semaglutide as the reference GLP-1 agonist.
Store lyophilized at -20°C protected from light. Upon reconstitution with bacteriostatic water, store at 2-8°C and use within 30 days. The acylated structure provides enhanced stability compared to native GLP-1.
Tirzepatide represents a paradigm shift in incretin biology. Where previous research focused on single-receptor agonism, Eli Lilly scientists engineered this novel peptide to activate both glucose-dependent insulinotropic polypeptide (GIP) and glucagon-like peptide-1 (GLP-1) receptors with balanced potency. The compound's structure—based on the native GIP sequence with modifications that confer GLP-1 activity—creates a dual agonist profile impossible to achieve with natural hormones.
This dual incretin activation reveals synergistic metabolic effects: GIP enhances insulin secretion and may support beta-cell health, while GLP-1 provides appetite suppression and delays gastric emptying. Researchers studying incretin receptor cross-talk, synergistic metabolic signaling, or the distinct contributions of GIP versus GLP-1 pathways find tirzepatide indispensable for dissecting complex incretin physiology.
Store lyophilized at -20°C in sealed container. Reconstitute with bacteriostatic water; maintain at 2-8°C for up to 30 days. The fatty acid modification provides proteolytic resistance and extended stability.
Tirzepatide represents a paradigm shift in incretin biology. Where previous research focused on single-receptor agonism, Eli Lilly scientists engineered this novel peptide to activate both glucose-dependent insulinotropic polypeptide (GIP) and glucagon-like peptide-1 (GLP-1) receptors with balanced potency. The compound's structure—based on the native GIP sequence with modifications that confer GLP-1 activity—creates a dual agonist profile impossible to achieve with natural hormones.
This dual incretin activation reveals synergistic metabolic effects: GIP enhances insulin secretion and may support beta-cell health, while GLP-1 provides appetite suppression and delays gastric emptying. Researchers studying incretin receptor cross-talk, synergistic metabolic signaling, or the distinct contributions of GIP versus GLP-1 pathways find tirzepatide indispensable for dissecting complex incretin physiology.
Store lyophilized at -20°C in sealed container. Reconstitute with bacteriostatic water; maintain at 2-8°C for up to 30 days. The fatty acid modification provides proteolytic resistance and extended stability.
Retatrutide represents the frontier of incretin research. Building on tirzepatide's dual-agonist success, Eli Lilly scientists engineered this peptide with an unprecedented pharmacological profile: balanced activation of three distinct hormone receptors—GLP-1, GIP, and glucagon. This triple agonism creates a metabolic phenotype unattainable through any combination of existing compounds: incretin-mediated glucose regulation and appetite suppression, plus glucagon-driven energy expenditure.
The addition of glucagon receptor activity—traditionally avoided in metabolic therapies due to hyperglycemic concerns—proves synergistic when balanced with GLP-1 and GIP signaling. Researchers investigating energy balance, thermogenesis, complex metabolic pathway interactions, or next-generation incretin pharmacology find retatrutide essential for exploring multi-receptor agonism strategies.
Store lyophilized at -20°C protected from moisture. Reconstitute with bacteriostatic water; stable at 2-8°C for 30 days. Handle with care—this represents one of the most complex peptide agonists in metabolic research.
Cagrilintide reimagines amylin pharmacology. While the first-generation amylin analogue pramlintide required frequent dosing and suffered from limited stability, Novo Nordisk's structural modifications created a compound with dramatically extended receptor residence time and proteolytic resistance. This long-acting analogue enables researchers to study sustained amylin receptor activation—revealing roles for this often-overlooked hormone in metabolic regulation that short-acting compounds cannot illuminate.
Amylin, co-secreted with insulin from pancreatic beta cells, serves as a critical satiety signal and gastric motility regulator. Cagrilintide's enhanced pharmacokinetics make it ideal for investigating amylin receptor biology, the interplay between amylin and incretin pathways, and the therapeutic potential of sustained amylin agonism in metabolic disease models.
Store lyophilized at -20°C in sealed vial. Upon reconstitution, maintain refrigerated at 2-8°C and use within 30 days. The acylated structure provides exceptional stability compared to native amylin.
Precision tools for studying the GH axis — from GHRH analogues to ghrelin receptor agonists.
Sermorelin represents elegant peptide design: by identifying the minimal bioactive sequence within full-length GHRH(1-44), researchers created a compound with identical receptor activity but enhanced stability and reduced immunogenicity. This 29-amino acid fragment contains the entire receptor-binding domain, making it indispensable for studying GHRH receptor pharmacology without the complications of the full 44-residue hormone.
The peptide binds selectively to GHRH receptors on pituitary somatotrophs, triggering endogenous growth hormone release through natural pulsatile mechanisms. Unlike exogenous growth hormone administration, sermorelin preserves the physiological feedback loops governing GH secretion, making it the preferred tool for studying growth hormone axis regulation, pituitary function, and the upstream control of IGF-1 production.
Store lyophilized at -20°C protected from light. Reconstitute with bacteriostatic water; maintain at 2-8°C and use within 30 days. The truncated structure provides improved stability versus full-length GHRH.
Ipamorelin solved a critical problem in growth hormone secretagogue research: earlier ghrelin mimetics like GHRP-6 and GHRP-2 stimulated GH release but also elevated prolactin and cortisol through off-target receptor activation. Novo Nordisk's Ipamorelin, a carefully designed pentapeptide, demonstrates near-exclusive selectivity for the ghrelin receptor (GHS-R1a) on somatotrophs, triggering GH secretion without the hormonal side effects that confound experimental interpretation.
This selectivity makes ipamorelin the gold standard for dissecting ghrelin receptor pharmacology and GH secretion mechanisms. Researchers studying the distinction between GHRH-mediated and ghrelin-mediated GH release, or investigating selective GH secretagogue approaches, find this peptide essential for clean, interpretable results.
Store lyophilized at -20°C. Upon reconstitution with bacteriostatic water, refrigerate at 2-8°C and utilize within 30 days. Ipamorelin demonstrates excellent stability in solution compared to earlier secretagogues.
CJC-1295 without Drug Affinity Complex (commonly called Modified GRF 1-29 or Mod GRF) represents refined GHRH analogue design. Through targeted amino acid substitutions at positions vulnerable to enzymatic cleavage, researchers created a peptide significantly more stable than natural GHRH yet without the week-long half-life of DAC-conjugated CJC-1295. This intermediate stability profile proves ideal for studying pulsatile GH release—the natural physiological pattern that continuous GHRH exposure would obscure.
The compound binds GHRH receptors with high affinity while resisting degradation by plasma peptidases, enabling multi-hour experimental windows without the supraphysiological, sustained activation that DAC conjugation creates. Researchers investigating natural GH pulse architecture, GHRH receptor desensitization, or physiological GH secretion patterns prefer this version for its balance of stability and pulsatility.
Store lyophilized at -20°C protected from light and moisture. Reconstitute with bacteriostatic water; stable at 2-8°C for 30 days. The structural modifications provide significant proteolytic resistance.
Growth hormone release is governed by two parallel pathways: GHRH signaling through pituitary GHRH receptors, and ghrelin acting via GHS-R1a receptors. This combination recognizes that dual-pathway activation produces supra-additive effects—the GH pulse amplitude from combined GHRH/ghrelin agonism exceeds the sum of individual stimulation. The mechanism involves distinct intracellular signaling cascades that converge on GH granule release, with ghrelin potentially amplifying GHRH's effects through calcium mobilization.
Researchers studying GH secretion physiology, investigating secretagogue synergy, or modeling maximal endogenous GH release find this pre-optimized ratio invaluable. The combination eliminates dosing variables, ensuring consistent GHRH:ghrelin pathway stimulation across experiments—a critical factor in reproducible GH research.
Store lyophilized at -20°C in sealed dual-chamber vial. Reconstitute both components simultaneously; maintain at 2-8°C and use within 30 days. Both peptides exhibit excellent co-stability in solution.
This represents human somatotropin in its native form: 191 amino acids in the precise sequence and tertiary structure found in pituitary-derived growth hormone. Produced through recombinant DNA technology in E. coli expression systems, this rHGH is structurally indistinguishable from endogenous GH, making it the unambiguous choice for studying growth hormone receptor binding, GH-mediated signal transduction, and the direct effects of somatotropin on target tissues.
Where secretagogues provide indirect GH elevation through endogenous release, direct GH administration enables precise dose-response studies, receptor saturation experiments, and investigation of GH signaling independent of pituitary function. With over four decades of research characterizing GH's effects on IGF-1 production, lipolysis, protein synthesis, and tissue remodeling, this molecule remains central to endocrine and metabolic research.
Store lyophilized at -20°C protected from light. Upon reconstitution with bacteriostatic water, maintain at 2-8°C and use within 14 days—shorter than peptide secretagogues due to protein aggregation susceptibility. Avoid agitation; gently swirl to dissolve.
The repair toolkit — peptides that drive angiogenesis, cell migration, and tissue remodeling.
Tissue repair requires coordinated processes: inflammatory resolution, angiogenesis, cell migration, extracellular matrix remodeling, and cytoprotection. This combination targets multiple phases simultaneously. BPC-157, a pentadecapeptide partial sequence of the body protection compound isolated from gastric juice, demonstrates remarkable cytoprotective properties in mucosal tissue while promoting angiogenesis through VEGF modulation. TB-500 (Thymosin Beta-4 fragment) facilitates actin polymerization and cytoskeletal reorganization, driving cell migration to injury sites and promoting extracellular matrix formation.
Their mechanisms complement: BPC-157 protects existing tissue and stimulates new vessel formation, while TB-500 mobilizes repair cells and promotes structural regeneration. With hundreds of published studies investigating each peptide individually, researchers increasingly combine them to model multi-phase tissue healing—from acute injury response through complete structural restoration.
Store lyophilized at -20°C protected from moisture. Both peptides remain stable when co-reconstituted; maintain at 2-8°C and use within 30 days. Compatible in the same solution without interaction.
KPV (Lysine-Proline-Valine) represents molecular dissection of anti-inflammatory signaling. As the C-terminal tripeptide of alpha-melanocyte stimulating hormone, KPV retains the parent molecule's remarkable anti-inflammatory properties while eliminating melanocortin receptor-mediated effects like pigmentation. This separation of functions makes KPV uniquely valuable: it modulates inflammatory gene transcription through NF-κB pathway inhibition and reduces pro-inflammatory cytokine production without the broader melanocortin system effects.
Research has demonstrated KPV's effectiveness in inflammatory bowel disease models, dermal inflammation studies, and wound healing research where inflammation must be controlled without suppressing the entire immune response. Its ability to penetrate epithelial barriers and concentrate in inflamed tissues makes it particularly relevant for mucosal inflammation research.
Store lyophilized at -20°C. Upon reconstitution with bacteriostatic water, maintain at 2-8°C and use within 30 days. This small peptide demonstrates excellent stability in solution.
Glycyl-L-Histidyl-L-Lysine bound to copper represents one of nature's elegant metal-mediated signaling systems. First isolated from human plasma in the 1970s by Dr. Loren Pickart, GHK-Cu demonstrates the biological importance of copper-peptide coordination chemistry. The copper ion, precisely positioned by the peptide's histidine and terminal amine, activates the complex's biological functions: stimulating collagen and glycosaminoglycan synthesis, modulating metalloproteinase activity for balanced extracellular matrix remodeling, and providing localized antioxidant effects.
GHK-Cu's plasma concentration declines with age, correlating with diminished tissue repair capacity—a relationship that has driven extensive research into its role in wound healing, dermal remodeling, and tissue regeneration. The peptide's ability to simultaneously promote matrix synthesis and regulate degradation makes it irreplaceable in studies of balanced tissue remodeling.
Store lyophilized at -20°C protected from light (copper complexes are photosensitive). Reconstitute with sterile water; the copper complex remains stable at 2-8°C for 30 days. Avoid oxidizing agents.
LL-37 occupies a unique position in human immunology: it is the only antimicrobial peptide produced by the human cathelicidin family, unlike other species that express multiple cathelicidin variants. Cleaved from the C-terminus of the hCAP18 precursor protein, this amphipathic alpha-helical peptide demonstrates broad-spectrum antimicrobial activity against bacteria, fungi, and enveloped viruses through membrane disruption. Beyond direct antimicrobial action, LL-37 exhibits immunomodulatory functions—recruiting immune cells, modulating inflammatory responses, and promoting wound closure.
Expression of LL-37 is induced by vitamin D, linking nutritional status to innate immune capacity—a relationship that has made this peptide central to research on vitamin D-dependent immunity. Its multi-functional profile (antimicrobial, chemotactic, angiogenic, and wound-healing) makes LL-37 essential for studying the complex roles of antimicrobial peptides beyond simple pathogen killing.
Store lyophilized at -20°C. Upon reconstitution, maintain at 2-8°C and use within 30 days. The amphipathic structure requires gentle handling to prevent aggregation at higher concentrations.
Thymalin belongs to a unique category of biological compounds developed in the Soviet Union: bioregulators—short peptides (typically 2-4 amino acids) extracted from specific organs that demonstrate tissue-specific regulatory effects. Isolated from thymus tissue, Thymalin contains peptides that appear to modulate T-cell differentiation and thymic function through mechanisms still being elucidated, possibly involving chromatin remodeling and gene expression regulation.
The bioregulator hypothesis suggests these short peptides bind to DNA regulatory regions, influencing cell differentiation and function in their tissue of origin. While mechanistic details continue to emerge, decades of research in Russia and Eastern Europe have characterized Thymalin's effects on immune function, T-cell populations, and adaptive immunity—making it valuable for thymic biology research and immunosenescence studies.
Store lyophilized at -20°C protected from moisture. Reconstitute with sterile or bacteriostatic water; maintain at 2-8°C and use within 30 days. As a biological extract, handle with standard peptide precautions.
Laennec represents the biological complexity that single-molecule research cannot capture. This pharmaceutical-grade extract, derived from healthy human placenta and manufactured under strict Japanese pharmaceutical standards, contains a remarkably diverse array of bioactive molecules: multiple growth factor families (FGF, EGF, VEGF, HGF), cytokines, amino acids, vitamins, and minerals that collectively drive tissue regeneration. The placenta—nature's most rapidly growing temporary organ—concentrates factors that promote cell proliferation, angiogenesis, and tissue remodeling.
Unlike recombinant single-factor preparations, Laennec provides the factor combinations and ratios that occur naturally during development and healing. Researchers studying complex tissue regeneration, investigating growth factor synergies, or modeling multi-factor biological environments find this extract invaluable for capturing biological complexity that simplified systems miss.
Store refrigerated at 2-8°C in sealed ampules. Do not freeze—freezing damages the biological factor profile. Protect from direct light. Use immediately upon opening; no preservatives present. Stable 24 months unopened under proper refrigeration.
From mitochondrial-derived peptides to lipotropic blends — every metabolic pathway covered.
Cellular defense compounds — NAD+ cofactors, glutathione systems, and mitochondrial protectors.
Nicotinamide adenine dinucleotide occupies a position of unparalleled importance in cellular biochemistry. This dinucleotide serves simultaneously as an electron carrier in redox reactions (the NAD+/NADH couple drives glycolysis, the TCA cycle, and oxidative phosphorylation), a substrate for sirtuins (deacetylases that regulate metabolism and longevity pathways), a substrate for PARPs (DNA repair enzymes), and a precursor for calcium signaling molecules. Without adequate NAD+, cellular energy production, gene expression regulation, and DNA maintenance all collapse.
NAD+ levels decline with age across tissues, correlating with metabolic dysfunction and cellular senescence—a relationship that has positioned NAD+ at the center of aging research. Studies investigating sirtuins, researching cellular energy metabolism, exploring DNA repair mechanisms, or modeling age-related NAD+ decline require direct NAD+ administration or measurement.
Store lyophilized at -20°C protected from light (NAD+ is photosensitive). Upon reconstitution with sterile water, use immediately or store at 2-8°C for up to 30 days. Avoid repeated freeze-thaw cycles which degrade the dinucleotide.
Nicotinamide adenine dinucleotide occupies a position of unparalleled importance in cellular biochemistry. This dinucleotide serves simultaneously as an electron carrier in redox reactions (the NAD+/NADH couple drives glycolysis, the TCA cycle, and oxidative phosphorylation), a substrate for sirtuins (deacetylases that regulate metabolism and longevity pathways), a substrate for PARPs (DNA repair enzymes), and a precursor for calcium signaling molecules. Without adequate NAD+, cellular energy production, gene expression regulation, and DNA maintenance all collapse.
NAD+ levels decline with age across tissues, correlating with metabolic dysfunction and cellular senescence—a relationship that has positioned NAD+ at the center of aging research. Studies investigating sirtuins, researching cellular energy metabolism, exploring DNA repair mechanisms, or modeling age-related NAD+ decline require direct NAD+ administration or measurement.
Store lyophilized at -20°C protected from light (NAD+ is photosensitive). Upon reconstitution with sterile water, use immediately or store at 2-8°C for up to 30 days. Avoid repeated freeze-thaw cycles which degrade the dinucleotide.
Glutathione (γ-L-glutamyl-L-cysteinyl-glycine) represents the first line of antioxidant defense. This tripeptide, present in millimolar concentrations in cells, functions as the primary reducing agent that neutralizes reactive oxygen species before they damage proteins, lipids, or DNA. The peptide's cysteine thiol group (-SH) provides the reducing power—glutathione oscillates between reduced (GSH) and oxidized (GSSG) forms, with the GSH/GSSG ratio serving as a key indicator of cellular redox status.
Beyond direct antioxidant action, glutathione serves as a cofactor for glutathione peroxidases (which reduce hydrogen peroxide) and glutathione S-transferases (which detoxify electrophilic compounds and xenobiotics). Manufactured in Korea to pharmaceutical standards, this preparation provides research-grade glutathione for oxidative stress studies, redox biology research, and investigation of the glutathione system's central role in cellular protection.
Store refrigerated at 2-8°C in sealed pharmaceutical vials. After opening, use immediately or maintain at 2-8°C for up to 7 days. This pharmaceutical preparation is formulated for immediate research use.
Glutathione (γ-L-glutamyl-L-cysteinyl-glycine) represents the first line of antioxidant defense. This tripeptide, present in millimolar concentrations in cells, functions as the primary reducing agent that neutralizes reactive oxygen species before they damage proteins, lipids, or DNA. The peptide's cysteine thiol group (-SH) provides the reducing power—glutathione oscillates between reduced (GSH) and oxidized (GSSG) forms, with the GSH/GSSG ratio serving as a key indicator of cellular redox status.
Beyond direct antioxidant action, glutathione serves as a cofactor for glutathione peroxidases (which reduce hydrogen peroxide) and glutathione S-transferases (which detoxify electrophilic compounds and xenobiotics). This higher-dose preparation enables concentration-dependent studies and research requiring substantial glutathione supplementation in experimental models.
Store lyophilized at -20°C protected from light and oxidizing conditions. Upon reconstitution with sterile water, use promptly or store at 2-8°C for up to 30 days. Glutathione oxidizes over time; fresh solutions provide optimal reducing capacity.
Alpha-lipoic acid (1,2-dithiolane-3-pentanoic acid) occupies a unique position in antioxidant biology: its amphipathic structure allows it to scavenge reactive species in both water-soluble compartments (cytoplasm) and lipid-rich environments (membranes)—a property no other antioxidant possesses. Beyond direct free radical neutralization, lipoic acid serves as an essential cofactor for mitochondrial α-ketoacid dehydrogenase complexes (pyruvate dehydrogenase, α-ketoglutarate dehydrogenase), linking its antioxidant function directly to energy metabolism.
The reduced form (dihydrolipoic acid) demonstrates remarkable antioxidant activity, directly scavenging reactive oxygen and nitrogen species while regenerating other antioxidants—reducing oxidized vitamin C, vitamin E, and glutathione back to their active forms. This antioxidant network amplification makes lipoic acid a force multiplier in cellular antioxidant defense.
Store refrigerated at 2-8°C protected from light (light-sensitive). Supplied in solution for immediate use. Maintain sealed until use; utilize within 30 days after opening. Protect from oxidizing conditions.
L-Ascorbic acid (vitamin C) serves multiple critical biochemical roles beyond its well-known antioxidant function. As a cofactor for prolyl and lysyl hydroxylases, ascorbate is absolutely required for collagen triple helix stability—without adequate vitamin C, collagen synthesis fails, manifesting as scurvy. The vitamin also serves as cofactor for dopamine β-hydroxylase (converting dopamine to norepinephrine) and other copper-containing monooxygenases essential for neurotransmitter synthesis.
As an antioxidant, ascorbate directly reduces reactive oxygen species and serves as the first line of defense in aqueous environments. It functions synergistically with vitamin E by reducing tocopheroxyl radicals back to active tocopherol, linking water-soluble and lipid-soluble antioxidant systems. This pharmaceutical-grade Liquid Reagent preparation enables precise dosing in controlled research applications.
Store refrigerated at 2-8°C protected from light (photosensitive). Use within 14 days after opening. Ascorbic acid oxidizes in solution over time; fresh preparations provide optimal activity. Do not freeze.
SS-31 (Szeto-Schiller peptide 31, D-Arg-Dmt-Lys-Phe-NH2) represents a breakthrough in mitochondria-targeted therapeutics. This cell-permeable tetrapeptide contains alternating cationic and aromatic residues that enable it to penetrate cells and selectively accumulate at the inner mitochondrial membrane, where it binds with high affinity to cardiolipin—the signature phospholipid of mitochondrial membranes. This cardiolipin interaction stabilizes cristae architecture, the elaborately folded inner membrane structures that house the electron transport chain.
Unlike broad antioxidants, SS-31 concentrates precisely where mitochondrial ROS are generated—at the electron transport chain. By optimizing cristae structure and reducing electron leak, SS-31 decreases reactive oxygen species production at the source while preserving mitochondrial membrane potential and ATP synthesis. This mechanism has made SS-31 invaluable in ischemia-reperfusion research, neurodegenerative disease models, and studies of mitochondrial dysfunction.
Store lyophilized at -20°C protected from light. Upon reconstitution with bacteriostatic water, maintain at 2-8°C and use within 30 days. The aromatic-cationic structure provides excellent peptide stability.
The longevity frontier — senescent cell clearance, telomerase modulation, and neuroprotection.
FOXO4-DRI represents molecular precision in anti-aging research. Senescent cells—aged cells that cease dividing but resist apoptosis—accumulate with age and secrete inflammatory factors (the senescence-associated secretory phenotype, SASP) that damage surrounding tissues. Dutch researchers discovered that in senescent cells, FOXO4 protein binds and sequesters p53, preventing p53-mediated apoptosis. FOXO4-DRI, a peptide mimicking the p53-binding domain of FOXO4, competitively disrupts this interaction—freeing p53 to trigger apoptosis specifically in senescent cells.
The D-retro-inverso modification—constructing the peptide from D-amino acids in reverse sequence—creates a molecule with identical binding surface topology but dramatically enhanced proteolytic stability. This senolytic approach—selectively eliminating senescent cells while sparing healthy ones—represents a targeted strategy for addressing cellular aging.
Store lyophilized at -20°C protected from moisture. Upon reconstitution, maintain at 2-8°C and use within 30 days. D-amino acid peptides demonstrate exceptional proteolytic stability.
Epithalon (Epitalon, Ala-Glu-Asp-Gly) emerged from decades of Russian gerontology research led by Professor Vladimir Khavinson. This tetrapeptide, designed to replicate bioactive sequences from the pineal peptide epithalamin, demonstrates two remarkable properties in experimental models: activation of telomerase (the enzyme that maintains telomere length) and modulation of circadian rhythms through melatonin regulation. These dual mechanisms position Epithalon at the intersection of cellular aging and chronobiology research.
Telomeres—the protective caps on chromosome ends—shorten with each cell division, eventually triggering senescence. Telomerase can extend telomeres, but most somatic cells suppress this enzyme. Epithalon's apparent ability to transiently activate telomerase in adult tissues has driven extensive research into its mechanism and potential for studying telomere biology and cellular aging interventions.
Store lyophilized at -20°C. Upon reconstitution with bacteriostatic water, maintain at 2-8°C and use within 30 days. This short peptide demonstrates good stability in solution.
PE 22-28 represents targeted neuroplasticity research. This heptapeptide, corresponding to amino acids 22-28 of the propeptide region of sortilin (a protein involved in neurotrophin sorting), was identified through research into spadin—an endogenous peptide with neuroprotective properties. PE 22-28 interacts with TREK-1 (TWIK-related potassium channel), a background potassium channel involved in neuronal excitability, synaptic plasticity, and stress response.
By modulating TREK-1 channel activity, PE 22-28 influences neuronal membrane potential and excitability, with downstream effects on neurotrophic signaling and synaptic remodeling. Research suggests this peptide may enhance neuroplasticity—the brain's capacity to reorganize synaptic connections—making it valuable for studying neuroadaptation, neuroprotection mechanisms, and the role of potassium channels in cognitive function.
Store lyophilized at -20°C. Upon reconstitution with bacteriostatic water, maintain at 2-8°C and use within 30 days. Standard peptide handling precautions apply.
Melanocortin receptor pharmacology — MC3R, MC4R, and opioid receptor research tools.
PT-141 emerged from structure-activity relationship studies of Melanotan II, a synthetic α-MSH analogue. While Melanotan II activates multiple melanocortin receptor subtypes (MC1R through MC5R), its metabolite PT-141 demonstrates preferential activity at MC3R and MC4R with reduced MC1R activation—eliminating much of the pigmentation effect while retaining central melanocortin activity. This selectivity makes PT-141 invaluable for dissecting the distinct roles of melanocortin receptor subtypes.
MC3R and MC4R, expressed primarily in the hypothalamus, regulate energy balance, autonomic function, and motivated behaviors through melanocortin signaling. PT-141 enables researchers to study these central melanocortin pathways without the confounding peripheral effects of broader melanocortin activation, making it the preferred tool for investigating hypothalamic melanocortin biology.
Store lyophilized at -20°C. Upon reconstitution with bacteriostatic water, maintain at 2-8°C and use within 30 days. The cyclic structure provides enhanced proteolytic stability.
Dermorphin stands as one of pharmacology's most intriguing discoveries. Isolated from the skin secretions of South American Phyllomedusa frogs, this heptapeptide contains an unusual D-alanine in position 2—one of the rare instances of D-amino acids in biologically active peptides. This structural quirk contributes to dermorphin's exceptional properties: nanomolar μ-opioid receptor affinity, selectivity ratios exceeding 1000:1 for μ over δ and κ receptors, and resistance to peptidase degradation.
The peptide's extraordinary selectivity and potency have made it an essential tool in opioid receptor biology—enabling precise study of μ-opioid receptor pharmacology, structure-activity relationships, and receptor-ligand interactions. Researchers investigating opioid signaling mechanisms, studying receptor binding kinetics, or exploring the structural determinants of receptor selectivity consistently rely on dermorphin as a reference μ-selective agonist.
Store lyophilized at -20°C protected from moisture and light. Upon reconstitution with sterile or bacteriostatic water, maintain at 2-8°C and use within 30 days. The D-amino acid provides proteolytic resistance.
Neurotoxins and dermatological research compounds for neuromuscular and skin biology.
Botulinum neurotoxin type A represents the gold standard for studying exocytosis. This large protein complex, produced by Clostridium botulinum, consists of a heavy chain (responsible for binding and internalization) and a light chain (the zinc-dependent endopeptidase that cleaves SNAP-25). By specifically cleaving SNAP-25—a protein essential for SNARE complex formation—BoNT/A prevents synaptic vesicles from fusing with the presynaptic membrane, completely blocking neurotransmitter release.
This exquisite molecular specificity makes botulinum toxin invaluable beyond its clinical applications. Researchers studying SNARE protein biology, investigating synaptic vesicle fusion mechanisms, exploring neuromuscular junction physiology, or dissecting the molecular machinery of exocytosis rely on BoNT/A's specific, irreversible SNAP-25 cleavage. The toxin serves as a molecular scalpel that precisely disrupts a single step in neurotransmitter release.
Store lyophilized at -20°C. Upon reconstitution, use immediately or store at 2-8°C for a maximum of 4 hours—this protein loses activity rapidly in solution. Handle with extreme care following institutional biosafety protocols.
Botulinum neurotoxin type A represents the gold standard for studying exocytosis. This large protein complex, produced by Clostridium botulinum, consists of a heavy chain (responsible for binding and internalization) and a light chain (the zinc-dependent endopeptidase that cleaves SNAP-25). By specifically cleaving SNAP-25—a protein essential for SNARE complex formation—BoNT/A prevents synaptic vesicles from fusing with the presynaptic membrane, completely blocking neurotransmitter release.
This exquisite molecular specificity makes botulinum toxin invaluable beyond its clinical applications. Researchers studying SNARE protein biology, investigating synaptic vesicle fusion mechanisms, exploring neuromuscular junction physiology, or dissecting the molecular machinery of exocytosis rely on BoNT/A's specific, irreversible SNAP-25 cleavage. The toxin serves as a molecular scalpel that precisely disrupts a single step in neurotransmitter release.
Store lyophilized at -20°C. Upon reconstitution, use immediately or store at 2-8°C for a maximum of 4 hours—this protein loses activity rapidly in solution. Handle with extreme care following institutional biosafety protocols.
Next-generation tissue protection — innate repair receptor agonists and targeted therapeutics.
ARA-290 represents molecular refinement of erythropoietin's tissue-protective properties. While full-length EPO stimulates red blood cell production through the classical EPO receptor, it also activates a distinct receptor complex called the innate repair receptor (IRR or tissue-protective receptor)—a heteromeric complex that triggers cell protection, reduces inflammation, and promotes tissue repair. ARA-290, an 11-amino acid EPO-derived peptide, selectively activates the IRR without engaging the erythropoietic EPO receptor.
This separation of functions enables clean investigation of EPO's tissue-protective mechanisms without the confounding hematological effects. Research has demonstrated ARA-290's effects in neuropathy models, ischemia-reperfusion injury, and inflammatory conditions—all mediated through IRR signaling pathways distinct from classical EPO effects. The peptide provides a unique tool for studying tissue protection mechanisms and innate repair receptor biology.
Store lyophilized at -20°C. Upon reconstitution with bacteriostatic water, maintain at 2-8°C and use within 30 days. This peptide demonstrates good stability in solution.