Research Peptide≥99% HPLC StandardShips from Canada

Overview

Tesamorelin is a synthetic analog of growth-hormone-releasing hormone (GHRH 1-44) stabilised by an N-terminal trans-3-hexenoyl group that resists enzymatic degradation. It is supplied as a stable lyophilized peptide.

As a GHRH-receptor agonist it is studied for its ability to stimulate endogenous, pulsatile GH release and the downstream IGF-1 response, and much of its literature concerns effects on visceral-adipose tissue and related metabolic endpoints. It is offered strictly as a research material, and the studies cited below describe preclinical and clinical-pharmacology findings only.

Mechanisms of interest in research

GHRH-receptor agonism

Tesamorelin activates the GHRH receptor on pituitary somatotrophs to promote synthesis and pulsatile release of endogenous GH, distinguishing it from direct GH administration by preserving the body’s own feedback control in model systems.

Visceral-adipose and metabolic endpoints

A defining research focus is the effect of restored GH signalling on visceral (central) adipose tissue; tesamorelin has been studied for reductions in central fat accumulation and for related changes in muscle and lipid endpoints.

Specifications

Selected Research

The following peer-reviewed studies are provided for scientific context on this compound’s research background. They describe preclinical and in-vitro findings only and are not claims about this product.

This review reports that tesamorelin, a GHRH analog, was safe and effective at reducing central fat accumulation in HIV-infected patients in randomized trials, though the effect was transient.
Bedimo R. HIV AIDS (Auckl). PMID: 22096409

In a randomized-trial secondary analysis, tesamorelin increased trunk skeletal-muscle density and area compared with placebo over 26 weeks.
Adrian S, et al. J Frailty Aging. PMID: 31237318

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Research Peptide≥99% HPLC StandardShips from Canada

Overview

TB-500 is a synthetic peptide based on the actin-binding region of thymosin β-4 (Tβ4), a naturally occurring 43-amino-acid regenerative peptide found in most tissues and in high concentration in platelets and wound fluid. The fragment centres on the conserved actin-binding motif (LKKTETQ) that gives Tβ4 much of its activity, and it is supplied as a stable, water-soluble lyophilized peptide suited to laboratory handling.

In research, TB-500 and Tβ4 are studied for their role in cell motility and tissue regeneration. By binding monomeric G-actin, the peptide influences the assembly and disassembly of the actin cytoskeleton that underlies cell migration, and it is examined in preclinical and in-vitro models of angiogenesis, wound repair, and inflammation. It is offered strictly as a research material, and the studies cited below describe preclinical and in-vitro findings only.

Mechanisms of interest in research

G-actin sequestration and cytoskeletal dynamics

Thymosin β-4 is the major intracellular G-actin-sequestering peptide: it binds monomeric actin and buffers the pool available for filament formation. In cell models this regulation of actin polymerisation is associated with the changes in cell shape and motility required for migration, which is why the actin-binding motif carried by TB-500 is central to its study.

Cell migration and angiogenesis

Directed migration of endothelial cells is an early step in forming new vessels. In cultured cells and animal models, thymosin β-4 has been associated with increased endothelial and keratinocyte migration and with markers of angiogenesis, making it a frequent tool in vascular and wound-repair research.

Tissue repair and anti-inflammatory signalling

Beyond motility, thymosin β-4 has been studied for effects on cell survival, reduced scar formation, and lowered levels of inflammatory mediators in injury models. These observations underpin its use as a reference peptide in soft-tissue and cardiac repair research.

Specifications

Selected Research

The following peer-reviewed studies are provided for scientific context on this compound’s research background. They describe preclinical and in-vitro findings only and are not claims about this product.

In animal-model studies reviewed here, thymosin β-4 promoted cell migration, blood-vessel formation, cell survival and stem-cell maturation while reducing inflammatory mediators.
Philp D, et al. Ann N Y Acad Sci. PMID: 20536453

In an adult cardiac explant model, thymosin β-4 stimulated epicardial cell outgrowth and their differentiation into endothelial and smooth-muscle cells, promoting neovascularization.
Smart N, et al. Ann N Y Acad Sci. PMID: 17495252

This review describes thymosin β-4 as promoting cell migration and the mobilization and differentiation of stem/progenitor cells while reducing scar formation and fibrosis, with proposed applications in dermal, corneal, cardiac and neurological repair.
Goldstein AL, et al. Expert Opin Biol Ther. PMID: 22074294

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Research Peptide Blend≥99% HPLC StandardShips from Canada

Overview

This research blend co-lyophilizes two peptides in a single vial: BPC-157 (Body Protection Compound-157), a stable synthetic pentadecapeptide derived from a protein in gastric juice, and TB-500, a synthetic fragment based on the actin-binding region of thymosin β-4. It is intended for combined-exposure studies in which both peptides are examined together.

The two are frequently paired in tissue-repair research because they act through complementary mechanisms — BPC-157 through growth-factor and nitric-oxide signalling, and TB-500 through actin regulation and cell migration. No published study evaluates this specific blend; the references below concern the individual components. It is offered strictly as a research material, and the studies cited describe preclinical and in-vitro findings only.

Mechanisms of interest in research

BPC-157: angiogenesis and cytoprotection

BPC-157 is studied for effects on new blood-vessel formation and cell survival, associated in models with VEGFR2 and nitric-oxide signalling — the vascular component of tissue repair.

TB-500: actin regulation and cell migration

TB-500 carries the actin-binding motif of thymosin β-4 and is studied for sequestering monomeric actin and promoting the cell migration that underlies wound closure and angiogenesis.

Specifications

Selected Research

The following peer-reviewed studies are provided for scientific context on this compound’s research background. They describe preclinical and in-vitro findings only and are not claims about this product.

On BPC-157:

In cultured tendon explants and fibroblasts, BPC-157 increased fibroblast outgrowth, cell survival and migration via the FAK–paxillin pathway.
Chang CH, et al. J Appl Physiol. PMID: 21030672

A review describes BPC-157 as an angiomodulatory agent acting through nitric-oxide, VEGF and FAK-related pathways in injury models.
Seiwerth S, et al. Curr Pharm Des. PMID: 23782145

On TB-500 (thymosin β-4):

In animal-model studies, thymosin β-4 promoted cell migration, blood-vessel formation and cell survival while reducing inflammatory mediators.
Philp D, et al. Ann N Y Acad Sci. PMID: 20536453

In a cardiac explant model, thymosin β-4 stimulated epicardial cell outgrowth and differentiation into vascular cells, promoting neovascularization.
Smart N, et al. Ann N Y Acad Sci. PMID: 17495252

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Research Peptide≥99% HPLC StandardShips from Canada

Overview

AHK-Cu is the copper(II) complex of the synthetic tripeptide alanyl-L-histidyl-L-lysine (AHK), structurally related to the GHK-Cu family of copper-binding peptides. It is supplied as a stable lyophilized peptide.

In research it is studied mainly in the context of hair-follicle biology and the dermal papilla, where copper-peptide complexes have been associated with follicle cell proliferation and vascular support. Its literature is smaller than that of GHK-Cu. It is offered strictly as a research material, and the study cited below describes preclinical findings only.

Mechanisms of interest in research

Copper-peptide activity in the dermal papilla

As a copper-binding tripeptide, AHK-Cu is studied for effects on the dermal papilla cells at the base of the hair follicle, where copper peptides have been associated with proliferation, reduced apoptosis, and support of the follicle growth phase.

Vascular and follicular support

Copper peptides in this family are also examined for influence on local angiogenesis and growth-factor signalling around the follicle, relevant to hair-research models.

Specifications

Selected Research

The following peer-reviewed studies are provided for scientific context on this compound’s research background. They describe preclinical and in-vitro findings only and are not claims about this product.

In cultured human hair follicles, AHK-Cu stimulated follicle elongation and dermal-papilla cell proliferation while reducing apoptosis markers.
Pyo HK, et al. Arch Pharm Res. PMID: 17703734

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Research Compound≥99% HPLC StandardShips from Canada

Overview

Dihexa (N-hexanoic-Tyr-Ile-(6)-aminohexanoic amide) is a small-molecule analog of angiotensin IV, engineered as a metabolically stable peptidomimetic. Chemical modifications at both ends make it resistant to the peptidases that rapidly degrade natural peptides and allow it to cross biological membranes, so despite its peptide-like origin it behaves as a stable small-molecule compound.

In research it is studied for neurotrophic effects, particularly the formation of new synaptic connections, which it appears to drive by engaging the hepatocyte growth factor (HGF) / c-Met signalling system. It is offered strictly as a research material, and the studies cited below describe preclinical findings only.

Mechanisms of interest in research

HGF / c-Met system activation

Dihexa is studied as a positive modulator of hepatocyte growth factor and its receptor c-Met. By enhancing this signalling it is associated with dendritic arborization and the formation of new synapses in neuronal models.

Synaptogenesis and cognition models

The synapse-forming activity has made dihexa a subject of cognition and neurodegeneration research, where new functional synaptic connections are examined in animal models.

Metabolic stability as a peptidomimetic

Unlike native angiotensin IV, dihexa resists peptidase degradation and penetrates tissues, properties central to its use as a research tool for probing HGF/c-Met-dependent neurotrophic effects.

Specifications

Selected Research

The following peer-reviewed studies are provided for scientific context on this compound’s research background. They describe preclinical and in-vitro findings only and are not claims about this product.

This study reports that dihexa induces dendritic arborization and synaptogenesis by activating the HGF/c-Met system, facilitating new functional synaptic connections and memory consolidation in Alzheimer-disease animal models.
Wright JW, et al. J Alzheimers Dis. PMID: 25649658

In zebrafish lateral-line cells, the HGF mimetic dihexa protected sensory hair cells against aminoglycoside toxicity through an HGF-mediated mechanism.
Uribe PM, et al. Front Cell Neurosci. PMID: 25674052

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Research Peptide≥99% HPLC StandardShips from Canada

Overview

IGF-1 LR3 (Long-R3-IGF-1) is an 83-amino-acid recombinant analog of insulin-like growth factor 1. It carries an arginine substitution at position 3 and a 13-residue N-terminal extension; together these lower its affinity for the IGF-binding proteins that normally sequester IGF-1, so more of the analog remains free and active. It is supplied as a stable lyophilized peptide.

In research it is widely used as a potent, binding-protein-resistant tool for activating the IGF-1 / type-1 IGF receptor pathway in cell culture, where it drives proliferation, differentiation and survival signalling. It is offered strictly as a research material, and the study cited below describes preclinical findings only.

Mechanisms of interest in research

Type-1 IGF receptor signalling

IGF-1 LR3 activates the type-1 IGF receptor, engaging the downstream PI3K–Akt and MAPK pathways that promote cell growth, proliferation and survival. Its reduced binding-protein affinity gives a stronger, more sustained signal than native IGF-1 in culture.

Binding-protein resistance as a research tool

Because IGF-binding proteins normally modulate IGF-1 availability, the low-affinity design of LR3 is used to study IGF-receptor effects with minimal interference, and to distinguish receptor-mediated from binding-protein-mediated actions.

Specifications

Selected Research

The following peer-reviewed studies are provided for scientific context on this compound’s research background. They describe preclinical and in-vitro findings only and are not claims about this product.

In porcine embryonic myogenic cells, Long-R3-IGF-1 stimulated proliferation, and the study used its low binding-protein affinity to show that IGFBP-5 can suppress that proliferation through an IGF-independent mechanism.
Pampusch MS, et al. J Endocrinol. PMID: 15817840

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Research Peptide≥99% HPLC StandardShips from Canada

Overview

KPV is a synthetic tripeptide corresponding to the C-terminal three residues (lysine-proline-valine) of the hormone α-melanocyte-stimulating hormone (α-MSH). Despite its small size it retains much of the anti-inflammatory activity of the parent hormone. It is supplied as a stable lyophilized peptide.

In research it is studied mainly for anti-inflammatory signalling, notably in models of gut and mucosal inflammation, where it appears to act partly through pathways independent of the classical melanocortin receptors. It is offered strictly as a research material, and the study cited below describes preclinical findings only.

Mechanisms of interest in research

Anti-inflammatory signalling and NF-κB

KPV is studied for dampening pro-inflammatory signalling, including interference with the NF-κB pathway that drives cytokine production. This activity is examined as a mechanism for reduced inflammation in cell and animal models.

Melanocortin-receptor-independent action

Unlike the full α-MSH hormone, the effects of KPV have been observed even where melanocortin-receptor signalling is limited, suggesting it can act through receptor-independent routes — a distinctive feature of its research profile.

Mucosal and gut-inflammation models

Much of the KPV literature concerns intestinal inflammation, where it is studied for effects on mucosal immune cells and epithelial transport.

Specifications

Selected Research

The following peer-reviewed studies are provided for scientific context on this compound’s research background. They describe preclinical and in-vitro findings only and are not claims about this product.

KPV showed significant anti-inflammatory effects in two murine models of colitis that appeared at least partly independent of MC1R signalling.
Kannengiesser K, et al. Inflamm Bowel Dis. PMID: 18092346

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Research Peptide≥99% HPLC StandardShips from Canada

Overview

MOTS-c (mitochondrial ORF of the twelve-S rRNA type-c) is a 16-amino-acid peptide encoded within the mitochondrial genome rather than the nucleus. It is one of a small group of mitochondrial-derived peptides and is supplied as a stable lyophilized peptide.

In research it is studied as a mitochondrial signal that regulates whole-body metabolism, notably through activation of the energy sensor AMP-activated protein kinase (AMPK) and translocation to the nucleus under metabolic stress. It is offered strictly as a research material, and the study cited below describes preclinical findings only.

Mechanisms of interest in research

Folate cycle, purine biosynthesis and AMPK activation

MOTS-c has been shown to act on the folate cycle and its linked de-novo purine biosynthesis, raising AICAR and activating AMPK — the cellular energy sensor that shifts metabolism toward glucose uptake and fatty-acid oxidation.

Metabolic homeostasis and insulin sensitivity

Through AMPK signalling, MOTS-c is studied for effects on insulin sensitivity and protection against diet-induced metabolic dysfunction in animal models.

Nuclear translocation and stress-adaptive gene expression

Under metabolic stress MOTS-c can move to the nucleus and influence antioxidant and metabolic gene programs, a mechanism examined as a mitochondrial-to-nuclear signal.

Specifications

Selected Research

The following peer-reviewed studies are provided for scientific context on this compound’s research background. They describe preclinical and in-vitro findings only and are not claims about this product.

This study identified MOTS-c as a mitochondrial-derived peptide that inhibits the folate cycle and de-novo purine biosynthesis, activating AMPK and preventing insulin resistance and diet-induced obesity in mice.
Lee C, et al. Cell Metab. PMID: 25738459

In mice, regular moderate-intensity running raised hypothalamic MOTS-c expression and induced a mitochondrial unfolded-protein response and thermogenesis in adipose tissue.
Kang GM, et al. Cell Metab. PMID: 33535098

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Research Peptide≥99% HPLC StandardShips from Canada

Overview

Retatrutide is a synthetic single-peptide (unimolecular) agonist of three receptors at once — the GIP, GLP-1, and glucagon receptors. It is engineered with a fatty-acid modification for an extended half-life and is supplied as a stable lyophilized peptide.

Its research interest is the addition of glucagon-receptor agonism to dual-incretin activity: glucagon-receptor signalling can raise energy expenditure, so the triple combination is studied for effects on metabolic rate, lipid handling, and body weight beyond incretin action alone. It is offered strictly as a research material, and the study cited below describes clinical-pharmacology findings only.

Mechanisms of interest in research

Triple GIP/GLP-1/glucagon receptor agonism

Retatrutide activates the two incretin receptors (GIP and GLP-1) together with the glucagon receptor from one molecule. Balancing these three signals is the central research question, since incretin and glucagon actions have distinct and partly opposing metabolic effects.

Energy expenditure and lipid metabolism

Glucagon-receptor activation is associated with increased energy expenditure and hepatic lipid mobilisation. Retatrutide is studied for how this component adds to incretin-driven appetite and insulin effects.

Body-weight and metabolic endpoints

The triple-agonist design is examined for larger effects on body weight and metabolic endpoints than dual- or single-receptor agonists in model systems.

Specifications

Selected Research

The following peer-reviewed studies are provided for scientific context on this compound’s research background. They describe preclinical and in-vitro findings only and are not claims about this product.

In a phase-2 randomized trial in adults with obesity, retatrutide (a triple GIP/GLP-1/glucagon agonist) produced dose-dependent body-weight reductions of up to about 24% over 48 weeks, compared with about 2% on placebo.
Jastreboff AM, et al. N Engl J Med. PMID: 37366315

In a phase-2 trial in adults with type 2 diabetes, retatrutide produced dose-dependent reductions in HbA1c and body weight that exceeded placebo and were comparable to or greater than dulaglutide at higher doses.
Rosenstock J, et al. Lancet. PMID: 37385280

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Research Peptide≥99% HPLC StandardShips from Canada

Overview

Retatrutide is a synthetic single-peptide (unimolecular) agonist of three receptors at once — the GIP, GLP-1, and glucagon receptors. It is engineered with a fatty-acid modification for an extended half-life and is supplied as a stable lyophilized peptide.

Its research interest is the addition of glucagon-receptor agonism to dual-incretin activity: glucagon-receptor signalling can raise energy expenditure, so the triple combination is studied for effects on metabolic rate, lipid handling, and body weight beyond incretin action alone. It is offered strictly as a research material, and the study cited below describes clinical-pharmacology findings only.

Mechanisms of interest in research

Triple GIP/GLP-1/glucagon receptor agonism

Retatrutide activates the two incretin receptors (GIP and GLP-1) together with the glucagon receptor from one molecule. Balancing these three signals is the central research question, since incretin and glucagon actions have distinct and partly opposing metabolic effects.

Energy expenditure and lipid metabolism

Glucagon-receptor activation is associated with increased energy expenditure and hepatic lipid mobilisation. Retatrutide is studied for how this component adds to incretin-driven appetite and insulin effects.

Body-weight and metabolic endpoints

The triple-agonist design is examined for larger effects on body weight and metabolic endpoints than dual- or single-receptor agonists in model systems.

Specifications

Selected Research

The following peer-reviewed studies are provided for scientific context on this compound’s research background. They describe preclinical and in-vitro findings only and are not claims about this product.

In a phase-2 randomized trial in adults with obesity, retatrutide (a triple GIP/GLP-1/glucagon agonist) produced dose-dependent body-weight reductions of up to about 24% over 48 weeks, compared with about 2% on placebo.
Jastreboff AM, et al. N Engl J Med. PMID: 37366315

In a phase-2 trial in adults with type 2 diabetes, retatrutide produced dose-dependent reductions in HbA1c and body weight that exceeded placebo and were comparable to or greater than dulaglutide at higher doses.
Rosenstock J, et al. Lancet. PMID: 37385280

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