Category: Peptide Profiles

Three of the most-searched growth-hormone research peptides — CJC-1295, Sermorelin and Ipamorelin — are constantly compared, and just as constantly confused. The confusion comes from lumping them into one bucket when in fact they split cleanly into two mechanistic families. This comparison lays out where each one sits and why it matters.

This concerns all three strictly as research materials. The peptides Solis supplies are for laboratory research use only — not for human or veterinary use — and nothing here is medical, dosing, or usage guidance.

The two families, three peptides

As covered in our primer on growth-hormone secretagogues, these peptides fall into two families defined by receptor:

• GHRH analogues (GHRH receptor): Sermorelin and CJC-1295.
• Ghrelin mimetic / GHRP (ghrelin receptor): Ipamorelin.

So two of the three act on one receptor, and the third acts on another.

Sermorelin vs CJC-1295

Both are GHRH analogues, so they engage the same receptor — the difference is stability and duration. Sermorelin corresponds to the short native GHRH(1–29) fragment and is the shortest-acting. CJC-1295 builds on that backbone with modifications; the DAC version in particular is engineered for a much longer duration of action. In short: same family, different half-life design.

Where Ipamorelin fits

Ipamorelin is the odd one out mechanistically — it is a ghrelin mimetic, acting on the GHS-R1a receptor rather than the GHRH receptor, and is noted in the literature for its selectivity. Because it reaches the growth-hormone axis by a different route, it is frequently studied in combination with a GHRH analogue such as CJC-1295, rather than as an alternative to it.

What to check when sourcing

For all three, the documentation is identical: ≥98% HPLC purity with the chromatogram, mass-spectrometry identity, and a lot-specific Certificate of Analysis. See our Quality & Analytics page.

Frequently asked questions

What’s the difference between CJC-1295 and Sermorelin?

Both are GHRH analogues acting on the same receptor; they differ mainly in stability and duration. Sermorelin is the short native fragment; CJC-1295 is engineered for longer action, especially in the DAC version.

How is Ipamorelin different from the other two?

Ipamorelin is a ghrelin mimetic acting on a different receptor (GHS-R1a), whereas CJC-1295 and Sermorelin are GHRH analogues. That’s why Ipamorelin is often studied alongside a GHRH analogue rather than instead of one.

Are any of them approved drugs?

No. All three are handled as research materials for laboratory use only and are not intended for human or veterinary use.

In summary

CJC-1295 and Sermorelin are GHRH analogues that differ in duration; Ipamorelin is a ghrelin mimetic on a different receptor, commonly paired with a GHRH analogue. Read the CJC-1295, Sermorelin and Ipamorelin profiles, and remember documentation — ≥98% HPLC, mass-spec identity, a lot-specific CoA — is what separates products. Browse the catalogue.

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Solis Peptides supplies research peptides for laboratory research use only — not for human or veterinary use, and not a medicine, supplement, or cosmetic. Nothing in this article is medical, dosing, or usage advice.

BPC-157 and TB-500 are the two most-discussed peptides in the tissue-repair research category, and they are almost always mentioned together. That pairing leads many buyers to assume they are interchangeable — but mechanistically they are quite distinct. This article explains why the two are studied side by side, how their research mechanisms differ, and what to check when sourcing either.

This concerns both peptides strictly as research materials. The peptides Solis supplies are for laboratory research use only — not for human or veterinary use — and nothing here is medical, dosing, or usage guidance.

Why they’re paired

BPC-157 and TB-500 are paired because they are the two flagship tool compounds in tissue-repair and angiogenesis research — the overlapping research contexts in which they appear make them natural companions in catalogues and literature reviews. But sharing a research area is not the same as sharing a mechanism.

How the mechanisms differ

The key concept is that the two peptides act through different pathways:

• BPC-157 — a synthetic pentadecapeptide whose research literature centres on the VEGFR2 and nitric-oxide pathways, i.e. vascular and angiogenic signalling.
• TB-500 — associated with the actin-binding region of thymosin β4, whose research literature centres on actin regulation and cell migration.

So one is studied primarily around vascular signalling, the other around the cytoskeleton and cell movement. They are different tools that happen to be studied in overlapping repair contexts.

Which one, and the naming trap

Because they are studied together, some suppliers offer them as a “blend.” As always, the meaningful information is the documentation, not the marketing. TB-500 carries an extra naming trap: “TB-500” and “thymosin β4” are used loosely, so mass-spec identity data is what tells you which molecule is actually in the vial.

What to check when sourcing either

The documentation set is identical for both: ≥98% HPLC purity with the chromatogram, mass-spectrometry identity, and a lot-specific Certificate of Analysis with net peptide content. See our Quality & Analytics page.

Frequently asked questions

Are BPC-157 and TB-500 the same?

No. They are both studied in tissue-repair research, but they act through different pathways — BPC-157 around VEGFR2/nitric-oxide signalling, TB-500 around actin regulation and cell migration.

Why are they sold together?

Because they are the two flagship tissue-repair research peptides and appear in overlapping literature, so catalogues commonly list them as a pair.

Are either of them approved drugs?

No. Neither is an approved medicine with the major regulators; both are handled as research materials for laboratory use only.

In summary

BPC-157 and TB-500 are the two flagship tissue-repair research peptides, paired by research context but distinct in mechanism — vascular/angiogenic signalling versus actin regulation. Read the full BPC-157 and TB-500 profiles, and note that documentation — ≥98% HPLC, mass-spec identity, a lot-specific CoA — is what separates products. Browse the catalogue.

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Solis Peptides supplies research peptides for laboratory research use only — not for human or veterinary use, and not a medicine, supplement, or cosmetic. Nothing in this article is medical, dosing, or usage advice.

KPV is a very short peptide with an outsized presence in inflammation-research literature. It is the C-terminal tripeptide fragment of alpha-melanocyte-stimulating hormone (α-MSH), and it is studied as a tool compound for probing inflammatory-signalling pathways. This profile explains what KPV is, what is studied, and what to check when sourcing it.

This concerns KPV strictly as a research material. The peptides Solis supplies are for laboratory research use only — not for human or veterinary use — and nothing here is medical, dosing, or usage guidance.

What is KPV?

KPV is a tripeptide — just three amino acids, Lysine-Proline-Valine — corresponding to the C-terminal fragment of α-MSH. Despite its small size, it retains research interest because that fragment is associated with the anti-inflammatory activity studied in the α-MSH literature. For the fundamentals of peptide fragments, see our primer on what peptides are.

Mechanisms explored in the literature

The KPV research literature centres on inflammation:

• Inflammatory-signalling pathways. KPV is studied for its reported influence on inflammatory-signalling cascades (such as NF-κB-related pathways) in preclinical models.
• Melanocortin-fragment activity. As an α-MSH fragment, KPV appears in research on the melanocortin system’s role in inflammation.

These are mechanisms studied in preclinical research, not approved clinical outcomes. KPV is not an approved therapeutic.

What’s on the market

KPV is typically sold as lyophilised powder in sealed vials. Research-grade material should be ≥98% HPLC with a batch Certificate of Analysis. Because it is a short, inexpensive peptide, documentation quality varies widely across suppliers.

Quality considerations when sourcing KPV

The standard documentation set applies: mass spectrometry for identity, HPLC purity of ≥98% shown as a chromatogram, and a lot-specific Certificate of Analysis with net peptide content. See our Quality & Analytics page, and current formats in the catalogue.

Frequently asked questions

What is KPV?

KPV is a tripeptide (Lys-Pro-Val) corresponding to the C-terminal fragment of alpha-MSH. In research it is studied as a tool compound for inflammatory-signalling pathways.

Is KPV an approved drug?

No. KPV is not an approved medicine with the major regulators. It is handled as a research material for laboratory use only.

What is KPV studied for?

In preclinical research it is examined for its reported influence on inflammatory-signalling pathways associated with the melanocortin system. These are research findings, not approved clinical uses.

In summary

KPV is a short α-MSH-derived tripeptide studied in preclinical research for inflammatory-signalling pathways. It is not an approved therapeutic, and documentation — ≥98% HPLC purity, mass-spec identity, a lot-specific CoA — is what separates products. See our Quality & Analytics page or browse the catalogue.

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Solis Peptides supplies research peptides for laboratory research use only — not for human or veterinary use, and not a medicine, supplement, or cosmetic. Nothing in this article is medical, dosing, or usage advice.

Selank is the companion peptide to Semax in the nootropic-research category — another synthetic regulatory peptide developed in Russia, but derived from a different natural molecule. Its research literature centres on anxiety-related and immunomodulatory pathways. This profile explains what Selank is, what is studied, and what to check when sourcing it.

This concerns Selank strictly as a research material. The peptides Solis supplies are for laboratory research use only — not for human or veterinary use — and nothing here is medical, dosing, or usage guidance.

What is Selank?

Selank is a synthetic heptapeptide based on tuftsin, a naturally occurring immune-active peptide fragment, with a stabilising tail added for research durability. Like Semax, it follows the “stabilised natural fragment” design pattern. For the fundamentals, see our primer on what peptides are.

Mechanisms explored in the literature

The Selank research literature has two main threads:

• GABAergic / anxiolytic pathways. The most-cited angle is Selank’s reported influence on GABAergic signalling in preclinical anxiety-related models.
• Immunomodulation. Because it derives from tuftsin, an immune-active peptide, Selank also appears in research on immune-signalling pathways.

These are mechanisms studied in preclinical research, not approved clinical outcomes. Selank is not an approved therapeutic in most jurisdictions.

What’s on the market

Selank is typically sold as lyophilised powder in sealed vials. Research-grade material should be ≥98% HPLC with a batch Certificate of Analysis. It is almost always discussed alongside Semax as the two flagship regulatory peptides in nootropic research.

Quality considerations when sourcing Selank

The documentation set is the standard one: mass spectrometry for identity, HPLC purity of ≥98% shown as a chromatogram, and a lot-specific Certificate of Analysis with net peptide content. See our Quality & Analytics page, and current formats in the catalogue.

Frequently asked questions

What is Selank?

Selank is a synthetic heptapeptide based on the immune-active peptide tuftsin, with a stabilising modification. In research it is studied for GABAergic/anxiolytic and immunomodulatory pathways.

Is Selank an approved drug?

In most jurisdictions Selank is not an approved medicine; it is handled as a research material for laboratory use only.

How is Selank related to Semax?

Both are stabilised Russian regulatory peptides used in nootropic research, but they derive from different natural molecules and are studied for different pathways — Selank for GABAergic/immune signalling, Semax for neurotrophic signalling.

In summary

Selank is a tuftsin-derived regulatory peptide studied in preclinical research for GABAergic and immunomodulatory pathways, and paired with Semax. It is not an approved therapeutic, and documentation — ≥98% HPLC purity, mass-spec identity, a lot-specific CoA — is what separates products. See our Quality & Analytics page or browse the catalogue.

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Solis Peptides supplies research peptides for laboratory research use only — not for human or veterinary use, and not a medicine, supplement, or cosmetic. Nothing in this article is medical, dosing, or usage advice.

Semax is one of the best-known peptides in the nootropic-research category. Originally developed in Russia, it is a synthetic analogue based on a fragment of adrenocorticotropic hormone (ACTH), and it appears frequently in preclinical literature on neurotrophic and neuroprotective pathways. This profile explains what Semax is, the mechanisms studied in research, and what to check when sourcing it.

This concerns Semax strictly as a research material. The peptides Solis supplies are for laboratory research use only — not for human or veterinary use — and nothing here is medical, dosing, or usage guidance.

What is Semax?

Semax is a synthetic peptide derived from the ACTH(4–10) fragment, with an added Pro-Gly-Pro tail that improves its stability. That structural tweak is characteristic of the “regulatory peptide” design approach: take a short active fragment of a natural hormone and stabilise it for research use. For the fundamentals of how such peptides are built, see our primer on what peptides are.

Mechanisms explored in the literature

The Semax research literature centres on the nervous system:

• BDNF and neurotrophic signalling. The most-cited angle is Semax’s reported influence on brain-derived neurotrophic factor (BDNF) and related neurotrophic pathways in research models.
• Neuroprotection models. Semax has been examined in preclinical models of neural stress and protection.

These are mechanisms studied in preclinical research, not approved clinical outcomes. Semax is not an approved therapeutic in most jurisdictions and is handled as a research compound.

What’s on the market

Semax is typically sold as lyophilised powder in sealed vials, and sometimes as a solution. Research-grade material should be ≥98% HPLC with a batch Certificate of Analysis. It is frequently grouped with Selank as the two flagship Russian regulatory peptides in the nootropic-research space.

Quality considerations when sourcing Semax

The documentation that separates credible Semax from an unknown powder is the standard set: mass spectrometry for identity, HPLC purity of ≥98% shown as a chromatogram, and a lot-specific Certificate of Analysis with net peptide content. We document all of this on our Quality & Analytics page, and current formats are in the catalogue.

Frequently asked questions

What is Semax?

Semax is a synthetic peptide based on the ACTH(4–10) fragment with a stabilising Pro-Gly-Pro tail. In research it is studied for neurotrophic and neuroprotective pathways, particularly BDNF.

Is Semax an approved drug?

In most jurisdictions Semax is not an approved medicine; it is handled as a research material for laboratory use only and is not intended for human or veterinary use.

What is Semax studied for?

In preclinical research it is examined for its reported influence on BDNF and neuroprotective pathways. These are research findings, not approved clinical uses.

In summary

Semax is a stabilised ACTH-fragment peptide studied in preclinical research for neurotrophic pathways such as BDNF, and commonly paired with Selank. It is not an approved therapeutic, and documentation — ≥98% HPLC purity, mass-spec identity, a lot-specific CoA — is what separates products. See our Quality & Analytics page or browse the catalogue.

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Solis Peptides supplies research peptides for laboratory research use only — not for human or veterinary use, and not a medicine, supplement, or cosmetic. Nothing in this article is medical, dosing, or usage advice.

MOTS-c belongs to a fascinating and relatively young category: the mitochondrial-derived peptides (MDPs). Unlike most research peptides, which correspond to fragments of proteins encoded in the cell nucleus, MOTS-c is encoded within the mitochondrial genome — the small, separate ring of DNA inside the cell’s energy organelles. That unusual origin, and its links to metabolic biology, are what make it a distinctive research tool.

As always, this concerns MOTS-c as a research material only. It is not an approved medicine, and the peptides Solis supplies are for laboratory research use only — not for human or veterinary use. Nothing here is medical, dosing, or usage guidance.

What is MOTS-c?

MOTS-c (Mitochondrial ORF of the 12S rRNA type-c) is a short peptide encoded in mitochondrial DNA. This is what sets it apart: the vast majority of peptides are products of nuclear genes, but MDPs like MOTS-c arise from the mitochondrial genome, which is why researchers describe them as “mitochondrial-derived.”

Its research profile is tied closely to cellular metabolism and energy homeostasis — appropriate for a peptide that comes from the cell’s power plants. For the general fundamentals, see our primer on what peptides are.

Mechanisms explored in the literature

The MOTS-c research literature centres on metabolic signalling:

• The AMPK pathway. MOTS-c is most often studied in relation to AMP-activated protein kinase (AMPK), a central sensor of cellular energy status. This is why MOTS-c is framed as a metabolic-regulation tool compound.
• Metabolic homeostasis. Research has examined MOTS-c in models of glucose handling, insulin sensitivity, and metabolic stress — as preclinical research, not clinical outcomes.
• Mitochondrial-nuclear communication. As an MDP, MOTS-c is studied in the broader question of how mitochondria signal to the rest of the cell.

These are mechanisms studied in research models, and MOTS-c is not an approved therapeutic.

What’s on the market

Across research-peptide suppliers, MOTS-c typically appears as:

• Lyophilised powder in sealed vials, reconstituted in the laboratory.
• Standalone listings, sometimes grouped with other longevity/metabolic research peptides such as Epitalon.
• Purity grades. Research-grade material should be ≥98% HPLC, with a batch Certificate of Analysis.

Quality considerations when sourcing MOTS-c

For a research buyer, the documentation that separates credible MOTS-c from an unknown powder is the standard set:

• Mass spectrometry confirming the molecular identity of the peptide for the specific lot.
• HPLC purity of ≥98%, shown as an actual chromatogram.
• A lot-specific Certificate of Analysis (CoA), plus clarity on net peptide content.

We document all of this on our Quality & Analytics page, and current MOTS-c formats are in the catalogue.

Frequently asked questions

What is MOTS-c?

MOTS-c is a mitochondrial-derived peptide — a short peptide encoded within mitochondrial DNA rather than the nuclear genome. In research it is studied mainly in the context of metabolic regulation and the AMPK energy-sensing pathway.

What makes MOTS-c unusual among peptides?

Its origin. Most peptides come from nuclear-encoded proteins, but MOTS-c is encoded in the mitochondrial genome, placing it in the distinct class of mitochondrial-derived peptides.

Is MOTS-c an approved drug?

No. MOTS-c is not an approved medicine with the major regulators. It is handled as a research material for laboratory use only.

In summary

MOTS-c is a mitochondrial-derived peptide whose research profile is built around metabolic regulation and the AMPK energy-sensing pathway, with a distinctive origin in the mitochondrial genome. It is commonly grouped with longevity/metabolic research peptides like Epitalon. It is not an approved therapeutic, and what separates products is documentation: ≥98% HPLC purity, mass-spec identity, and a lot-specific CoA. See our Quality & Analytics page or browse the catalogue.

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Solis Peptides supplies research peptides for laboratory research use only — not for human or veterinary use, and not a medicine, supplement, or cosmetic. Nothing in this article is medical, dosing, or usage advice.

Epitalon (also spelled Epithalon) is one of the most distinctive peptides in the longevity-research category. Where most research peptides are studied around tissue repair or the growth-hormone axis, Epitalon’s literature centres on the pineal gland and, most famously, on telomerase — the enzyme involved in maintaining the protective caps at the ends of chromosomes. This profile explains what Epitalon is, why it draws research interest, and what to check when sourcing it.

As with everything we publish, this concerns Epitalon as a research material only. It is not an approved medicine, and the peptides Solis supplies are for laboratory research use only — not for human or veterinary use. Nothing here is medical, dosing, or usage guidance.

What is Epitalon?

Epitalon is a synthetic tetrapeptide — a chain of just four amino acids (Ala-Glu-Asp-Gly). It was developed as a synthetic version of a peptide fraction originally associated with the pineal gland. Its very short length makes it straightforward to synthesise and characterise, which is part of why it became a widely available research compound.

Because it derives from pineal-associated material, Epitalon is often described in the literature in the context of the pineal axis and circadian regulation, alongside the telomerase angle it is best known for. For the basics of how short peptides like this are built, see our primer on what peptides are.

Mechanisms explored in the literature

Two threads dominate the Epitalon research literature:

• Telomerase activity. The most-cited research angle is Epitalon’s reported association with telomerase, the enzyme that adds repeats to telomeres. Because telomere length is a marker studied in the biology of cellular ageing, this is why Epitalon is grouped with “longevity” research peptides.
• Pineal and circadian context. As a pineal-derived sequence, Epitalon appears in research discussing melatonin regulation and circadian rhythm models.

It is worth stating the framing plainly: these are mechanisms examined in preclinical research, not approved clinical outcomes. Epitalon is not an approved therapeutic.

What’s on the market

Across research-peptide suppliers, Epitalon typically appears as:

• Lyophilised powder in sealed vials, reconstituted in the laboratory, commonly in small milligram sizes.
• “Epitalon” vs “Epithalon” labelling — the same compound, two spellings; documentation, not spelling, is what matters.
• Purity grades. Research-grade material should be ≥98% HPLC, with a batch Certificate of Analysis.

Quality considerations when sourcing Epitalon

Because Epitalon is short and inexpensive to make, the market carries a wide range of quality. The documentation that separates credible material from an unknown powder is the standard set:

• Mass spectrometry confirming the identity of the tetrapeptide for the specific lot.
• HPLC purity of ≥98%, shown as an actual chromatogram.
• A lot-specific Certificate of Analysis (CoA), plus clarity on net peptide content.

We document all of this on our Quality & Analytics page, and current Epitalon formats are in the catalogue.

Frequently asked questions

What is Epitalon?

Epitalon is a synthetic tetrapeptide (Ala-Glu-Asp-Gly) based on a peptide fraction associated with the pineal gland. In research it is studied for its reported links to telomerase activity and circadian/pineal biology.

Why is Epitalon associated with longevity research?

Because its most-cited research angle is telomerase — the enzyme that maintains telomeres, whose length is a marker studied in cellular-ageing biology.

Is Epitalon an approved drug?

No. Epitalon is not an approved medicine with the major regulators. It is handled as a research material for laboratory use only.

In summary

Epitalon is a short synthetic tetrapeptide from the pineal-peptide family, studied chiefly for its reported association with telomerase and circadian biology — the reason it sits in the longevity-research category alongside peptides like MOTS-c. It is not an approved therapeutic, and as with any research peptide, documentation is what separates products: ≥98% HPLC purity, mass-spec identity, and a lot-specific CoA. See our Quality & Analytics page or browse the catalogue.

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Solis Peptides supplies research peptides for laboratory research use only — not for human or veterinary use, and not a medicine, supplement, or cosmetic. Nothing in this article is medical, dosing, or usage advice.

Tesamorelin occupies a distinct place in the growth-hormone-secretagogue category, because unlike most of the research peptides discussed alongside it, it corresponds to a molecule that actually reached clinical approval for a specific medical indication. That history makes it one of the better-characterised peptides in the GHRH family, and a useful reference point for understanding how a growth-hormone-releasing-hormone analogue is engineered for stability. This profile explains what tesamorelin is, how it relates to the other GHRH-axis peptides, and what a research buyer should check when sourcing it.

As with everything we publish, this concerns tesamorelin strictly as a research material. The peptides Solis supplies are for laboratory research use only — not for human or veterinary use, and not a medicine, supplement, or cosmetic. Nothing here is medical, dosing, or usage guidance.

What is Tesamorelin?

Tesamorelin is a synthetic peptide analogue of growth-hormone-releasing hormone (GHRH). Natural GHRH is a 44-amino-acid hormone produced in the hypothalamus that signals the pituitary to release growth hormone. Tesamorelin is built on the biologically active fragment of that hormone, with a chemical modification — a trans-3-hexenoic acid group attached to the N-terminus — that makes the molecule more stable and resistant to rapid breakdown than the unmodified sequence.

That stabilising modification is the whole point of the molecule. Native GHRH and its shortest active fragments are fragile and short-lived; tesamorelin’s design keeps the GHRH-analogue structure intact for longer under experimental conditions. For the basics of how peptides like this are built, see our primer on what peptides are.

Mechanism explored in the literature

The mechanistic story of tesamorelin is that of a GHRH-receptor agonist:

• GHRH-receptor agonism. Tesamorelin binds the GHRH receptor on the pituitary — the same receptor engaged by the body’s own GHRH — and in research models stimulates the release of growth hormone. Because it mimics the natural hormone rather than acting through a separate pathway, it is described as a GHRH analogue.
• Engineered stability. The N-terminal modification is what differentiates tesamorelin mechanistically from unmodified GHRH fragments: it is designed to resist enzymatic degradation, giving a longer-lived interaction with the receptor system in study conditions.

As always, this is a description of mechanisms studied in research, not a claim of outcomes. In a research context, tesamorelin is handled as a tool compound for probing the GHRH axis, not as an approved therapeutic for laboratory use.

Tesamorelin vs Sermorelin vs CJC-1295

The most useful way to understand tesamorelin is to place it next to the other GHRH-axis peptides, because all three are GHRH analogues that differ mainly in how they are stabilised:

• Sermorelin corresponds to GHRH(1–29), the shortest fully active fragment. It is the closest to the “native” sequence and the shortest-acting of the three.
• CJC-1295 takes that GHRH(1–29) backbone and adds modifications, and in the DAC version a mechanism for a much longer duration of action.
• Tesamorelin takes the active GHRH fragment and stabilises it with its own N-terminal chemical group.

The key concept is that these are variations on one theme — the GHRH receptor — engineered for different stability profiles, rather than three unrelated compounds. This is distinct from the ghrelin-receptor peptides such as Ipamorelin, which reach the same growth-hormone axis through a different receptor entirely, and are therefore often studied in combination with GHRH analogues rather than as substitutes for them.

What’s on the market

Across research-peptide suppliers, tesamorelin typically appears as:

• Lyophilised powder in sealed vials, reconstituted in the laboratory, commonly in 5 mg and 10 mg sizes.
• Purity grades. Research-grade material should be ≥98% HPLC, with a batch Certificate of Analysis. Because tesamorelin is a longer and more elaborate molecule than a short peptide, synthesis quality and documentation matter a great deal.

Quality considerations when sourcing Tesamorelin

For a research buyer, the documentation that separates credible tesamorelin from an unknown powder is the same rigorous set that applies to every peptide:

• Mass spectrometry confirming the molecular identity of the analogue for the specific lot — important because the stabilising modification must actually be present and correct.
• HPLC purity of ≥98%, shown as an actual chromatogram rather than a bare claim.
• A lot-specific Certificate of Analysis (CoA), plus clarity on net peptide content.

We document all of this on our Quality & Analytics page, and current tesamorelin formats and pricing are in the catalogue.

Frequently asked questions

What is Tesamorelin?

Tesamorelin is a synthetic, stabilised analogue of growth-hormone-releasing hormone (GHRH), based on the active fragment of GHRH with an N-terminal modification that makes it more resistant to breakdown. In research it is studied as a GHRH-receptor agonist.

How is Tesamorelin different from Sermorelin?

Both are GHRH analogues. Sermorelin corresponds to the short native GHRH(1–29) fragment, while tesamorelin adds a stabilising N-terminal modification to the active fragment for greater stability.

Is Tesamorelin an approved drug?

Tesamorelin corresponds to a molecule that has received approval for a specific human medical indication in some jurisdictions. However, the material Solis supplies is sold strictly as a research chemical for laboratory use only, and is not offered as a medicine or for human or veterinary use.

In summary

Tesamorelin is a stabilised synthetic analogue of growth-hormone-releasing hormone, studied as a GHRH-receptor agonist and best understood as one of three related GHRH-axis peptides alongside Sermorelin and CJC-1295. As with any research peptide, what separates products is documentation: ≥98% HPLC purity, mass-spec identity, and a lot-specific CoA. See our Quality & Analytics page or browse the catalogue.

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Solis Peptides supplies research peptides for laboratory research use only — not for human or veterinary use, and not a medicine, supplement, or cosmetic. Nothing in this article is medical, dosing, or usage advice.

Sermorelin is, in a sense, the original of its family. Where peptides like CJC-1295 are engineered, stabilised variants, Sermorelin is the parent molecule they were built from — the shortest fragment of growth-hormone-releasing hormone that still does the job. This profile explains what Sermorelin is, how it works, how it relates to CJC-1295, and what to check when sourcing it.

As with everything we publish, this concerns Sermorelin as a research material only. It is not an approved medicine for these purposes, and the peptides Solis supplies are for laboratory research use only — not for human or veterinary use. Nothing here is medical, dosing, or usage guidance.

What is Sermorelin?

Sermorelin is a synthetic peptide corresponding to the first 29 amino acids of growth-hormone-releasing hormone (GHRH) — often written GRF (1-29). Native GHRH is a 44-amino-acid hormone, but researchers established long ago that the first 29 residues are the biologically active fragment: the shortest portion that retains full GHRH activity. Sermorelin is that fragment.

That makes it a GHRH analogue and a growth-hormone secretagogue — a compound studied for its ability to prompt the pituitary to release growth hormone. For the fundamentals of how peptides like this are built and characterised, see our primer on what peptides are.

Mechanism explored in the literature

Sermorelin’s mechanism is the cleanest in the GHRH family, precisely because it is the unmodified active fragment:

• GHRH-receptor agonism. Sermorelin binds the GHRH receptor on the pituitary and, in research models, stimulates the release of growth hormone. It engages the same receptor and pathway as native GHRH.
• Short-acting profile. Because it carries none of the stabilising substitutions or albumin-binding modifications found in engineered analogues, Sermorelin is comparatively short-acting in research systems — a pulsatile signal rather than a sustained one.

As always, these are mechanisms studied in preclinical research models, not approved clinical outcomes for the uses discussed here.

Sermorelin vs. CJC-1295

This is the comparison worth understanding. CJC-1295 is essentially a modified, stabilised version of the same GRF (1-29) backbone: it adds amino-acid substitutions (and, in the DAC form, an albumin-binding complex) to resist enzymatic breakdown and extend duration. Sermorelin is the unmodified parent — same active region, no stabilising changes, shorter action.

So the relationship is straightforward: Sermorelin is the original GRF (1-29); CJC-1295 is what you get when you engineer that fragment for longevity. Researchers choose between them depending on whether they want the native, short-acting signal or a longer-lasting one. Sermorelin is also frequently studied alongside ghrelin-receptor peptides such as Ipamorelin, which engage the growth-hormone axis through a complementary receptor.

What’s on the market

Across research-peptide suppliers, Sermorelin typically appears as:

• Lyophilised powder in sealed vials, reconstituted in the laboratory, commonly in 2 mg and 5 mg sizes.
• “Sermorelin” vs “GRF (1-29).” These names refer to the same molecule; a serious supplier’s documentation will make the sequence explicit.
• Purity grades. Research-grade material should be ≥98% HPLC, with a batch Certificate of Analysis. Undocumented material is a different product regardless of the label.

Quality considerations when sourcing Sermorelin

For a research buyer, the documentation that separates credible Sermorelin from an unknown powder is the same rigorous set:

• Mass spectrometry confirming the molecular identity of the peptide for the specific lot.
• HPLC purity of ≥98%, shown as an actual chromatogram.
• A lot-specific Certificate of Analysis (CoA), plus clarity on net peptide content.

We document all of this on our Quality & Analytics page, and current Sermorelin formats and pricing are in the catalogue.

Frequently asked questions

What is Sermorelin?

Sermorelin is a synthetic peptide corresponding to the first 29 amino acids of growth-hormone-releasing hormone — GRF (1-29) — the shortest fully active GHRH fragment. In research it is studied as a growth-hormone secretagogue.

Is Sermorelin the same as GRF (1-29)?

Yes. “Sermorelin” and “GRF (1-29)” refer to the same molecule: the biologically active first 29 amino acids of GHRH.

How is Sermorelin different from CJC-1295?

CJC-1295 is a modified, stabilised version of the same GRF (1-29) backbone, engineered to last longer (the DAC form binds albumin for a much longer duration). Sermorelin is the unmodified parent fragment and is shorter-acting.

Is Sermorelin an approved drug for these research uses?

The material Solis supplies is a research chemical for laboratory use only, not for human or veterinary use, and is not sold as a medicine.

In summary

Sermorelin is GRF (1-29) — the shortest fully active fragment of growth-hormone-releasing hormone, and the unmodified parent of engineered analogues like CJC-1295. Its mechanism is clean GHRH-receptor agonism with a short, pulsatile profile, and it is frequently studied alongside ghrelin-receptor peptides such as Ipamorelin. It is a research material, not a therapeutic, and what separates products is documentation: ≥98% HPLC purity, mass-spec identity, and a lot-specific CoA. See our Quality & Analytics page or browse the catalogue.

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Solis Peptides supplies research peptides for laboratory research use only — not for human or veterinary use, and not a medicine, supplement, or cosmetic. Nothing in this article is medical, dosing, or usage advice.

GHK-Cu is one of the most distinctive peptides in the research catalogue — you can often recognise it by sight, because its copper complex gives it a characteristic blue tint. It is also unusual in being a naturally occurring human peptide with a long history in the scientific literature. This profile explains what GHK-Cu is, the mechanisms studied around it, and what to check when sourcing it.

As with everything we publish, this concerns GHK-Cu as a research material only. The peptides Solis supplies are for laboratory research use only — not for human or veterinary use, and not a cosmetic. Nothing here is medical, dosing, or usage guidance.

What is GHK-Cu?

GHK-Cu is a copper-binding tripeptide — three amino acids (glycyl-L-histidyl-L-lysine, “GHK”) bound to a copper(II) ion. The GHK sequence occurs naturally in human plasma, where it has a well-documented ability to bind and carry copper. Its concentration in the body is reported in the literature to decline with age, which is part of why it has been so widely studied.

This makes GHK-Cu a textbook example of a carrier peptide — a peptide whose function is intimately tied to the metal ion it transports. The copper is not incidental; it is central to the molecule’s chemistry and to the research interest around it. For the broader distinction between carrier peptides and other classes, see our primer on what peptides are.

Mechanisms explored in the literature

The GHK-Cu research literature is unusually deep for such a small molecule, and it clusters around a few themes:

• Copper transport. As a copper-binding peptide, GHK-Cu is studied for how it delivers copper — a cofactor for many enzymes — into cellular systems in research models.
• Skin and tissue-remodelling research. A large body of work examines GHK-Cu in the context of skin, collagen, and extracellular-matrix research, which is why it appears so often in cosmetic-science literature. In a research setting this is about matrix and remodelling pathways, not a cosmetic claim.
• Gene-expression modulation. Some of the most-cited GHK-Cu papers report effects on the expression of large numbers of genes in cell models, positioning it as a tool for studying broad regulatory responses.
• Antioxidant and angiogenic pathways. As with several repair-associated peptides, vascular and antioxidant pathways feature in the literature.

The unifying thread is copper delivery and tissue-remodelling research. That combination — a specific carrier chemistry plus a wide-ranging regulatory footprint — is what has kept GHK-Cu in the literature for decades.

What’s on the market

Across research-peptide suppliers, GHK-Cu typically appears as:

• Lyophilised powder with the characteristic blue colour of the copper complex, in sealed vials, commonly in 10 mg and larger (e.g. 50 mg) sizes.
• GHK-Cu vs plain GHK. Some catalogues list the copper-complexed form (GHK-Cu) and the copper-free peptide (GHK) separately. They are chemically distinct; the copper is the defining feature of GHK-Cu.
• Purity grades. Research-grade material should be ≥98% HPLC, with a batch Certificate of Analysis. Undocumented material is a different product regardless of the label.

Quality considerations when sourcing GHK-Cu

Because the copper complex defines the molecule, documentation should confirm both the peptide and its complexation:

• Mass spectrometry confirming the molecular identity of the tripeptide for the specific lot.
• HPLC purity of ≥98%, shown as an actual chromatogram.
• A lot-specific Certificate of Analysis (CoA), plus clarity on net peptide content.

We document all of this on our Quality & Analytics page, and current GHK-Cu formats and pricing are in the catalogue.

Frequently asked questions

What is GHK-Cu?

GHK-Cu is a naturally occurring copper-binding tripeptide (glycyl-L-histidyl-L-lysine bound to a copper ion). In research it is studied as a carrier peptide for copper transport and in skin, collagen, and tissue-remodelling models.

Why is GHK-Cu blue?

The blue tint comes from the copper(II) ion bound to the GHK peptide. That copper complexation is the defining chemical feature of GHK-Cu, distinguishing it from the copper-free GHK peptide.

Is GHK-Cu a cosmetic?

No. Although GHK-Cu appears widely in cosmetic-science literature, the material Solis supplies is a research chemical for laboratory use only — not a cosmetic, medicine, or supplement, and not for human or veterinary use.

What purity should research-grade GHK-Cu be?

Research-grade material is typically characterised at ≥98% HPLC purity, with mass-spectrometry identity confirmation and a batch Certificate of Analysis.

In summary

GHK-Cu is a naturally occurring copper-binding tripeptide — a classic carrier peptide whose chemistry and research interest both centre on the copper ion it transports. Its literature spans copper delivery, skin and tissue-remodelling research, and broad gene-expression effects, making it one of the most-studied small peptides available. It is not a cosmetic or therapeutic; it is a research material. As always, what separates products is documentation: ≥98% HPLC purity, mass-spec identity, and a lot-specific CoA. See our Quality & Analytics page or browse the catalogue.

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Solis Peptides supplies research peptides for laboratory research use only — not for human or veterinary use, and not a medicine, supplement, or cosmetic. Nothing in this article is medical, dosing, or usage advice.