Scope and purposeAbout this handbook
This handbook is a practical companion for scientists who work with synthetic peptides at the bench. It brings together the chemistry, documentation and handling knowledge that sits behind a reliable experiment: what is actually in a vial of lyophilised peptide, how to read the paperwork that accompanies it, how to turn a few milligrams of powder into an accurate stock solution, and how to keep that material in good condition for as long as possible.
Who it is written for
The intended readers are laboratory researchers: postgraduate students and post-docs, research technicians, analytical chemists, and scientists in contract research organisations or industrial R&D teams. We assume familiarity with basic laboratory practice (calibrated pipettes, analytical balances, aseptic technique) but not specialist training in peptide chemistry.
What it covers – and what it deliberately does not
- Covered: peptide structure and nomenclature; how research peptides are synthesised and purified; purity, counter-ions and net peptide content; certificates of analysis; concentration and molarity calculations; solvent selection; sterile filtration for cell culture; aliquoting, storage and stability; troubleshooting; an overview of the Britpep catalogue organised by the research fields in which each compound appears in the published literature.
- Not covered: any use in people or animals. Britpep products are laboratory reagents supplied for in-vitro research. They are not medicines, food, food supplements or cosmetics, and this handbook contains no information on administration, quantities for living subjects, or effects on the body. Questions of that kind fall outside what we can answer.
How research information is presented
Where the handbook mentions a field of study, it describes what has been investigated in published work, together with the type of model used (cell culture, tissue, animal model or clinical study) and a numbered citation to the source. Two labels are used throughout the Britpep website and are kept here:
References were checked against PubMed or the official publisher at the time of writing. A citation describes what the source reports; it is not a claim about any Britpep product.
Chapter 1Peptide fundamentals
From amino acids to peptides
A peptide is a short polymer of amino acids. Each amino acid carries an amine group, a carboxylic acid group and a distinctive side chain. When the carboxyl group of one residue condenses with the amine of the next, water is lost and an amide link – the peptide bond – is formed. Repeating this produces a backbone with a free amine at one end (the N-terminus) and a free carboxyl at the other (the C-terminus). Sequences are always written from N to C.
There is no sharp boundary between a peptide and a protein, but chains of roughly two to fifty residues are conventionally called peptides. They are small enough to be made entirely by chemical synthesis, which is how almost every research peptide is produced today [1].
Reading a sequence
Residues are written either in three-letter code (Gly-His-Lys) or one-letter code (GHK). Prefixes and suffixes describe modifications that change the chemistry and, often, the stability of the molecule:
| Notation | Meaning | Example in the Britpep range |
|---|---|---|
| Ac- | N-terminal acetylation – removes the positive charge at the N-terminus | Thymosin Alpha-1, SNAP-8 |
| -NH₂ | C-terminal amide in place of the free acid | Ipamorelin, Kisspeptin-10, SS-31 |
| D-Xaa | A D-configured amino acid (the mirror image of the natural L form) | Ipamorelin, SS-31, CJC-1295 |
| Pal- | Palmitoyl (C16 fatty acyl) group, which makes the peptide markedly more lipophilic | Matrixyl (Pal-KTTKS) |
| ·Cu(II) | A metal complex: the peptide is supplied bound to copper | GHK-Cu, AHK-Cu |
| D-retro-inverso | Built from D-amino acids in reversed order, so side chains resemble the parent while the backbone resists proteases | FOXO4-DRI |
How research peptides are made
Most research peptides are produced by solid-phase peptide synthesis (SPPS). The C-terminal residue is anchored to an insoluble resin bead, and protected amino acids are then added one at a time through repeated rounds of deprotection, coupling and washing. In the widely used Fmoc strategy, the temporary protecting group on each new amine is removed with a mild base, while side-chain protecting groups stay in place until the end. The finished chain is cleaved from the resin, usually with a trifluoroacetic acid (TFA) cocktail that also strips the side-chain protection.
The crude product is a mixture. Alongside the target sequence it contains molecules that are one residue short (deletion sequences), chains that stopped early (truncations), species with protecting groups left on, and products of side reactions such as oxidation or aspartimide formation [2]. Preparative reversed-phase HPLC separates the target from most of these, and the pooled fractions are then freeze-dried.
Lyophilisation – why peptides arrive as a powder
Freeze-drying removes water by sublimation under vacuum after the solution has been frozen. The result is a light, often fluffy cake or a thin film on the vial wall. Removing water slows most chemical degradation pathways, which is why peptides are supplied and stored as solids and only dissolved shortly before use [3]. A small amount of residual moisture remains, and lyophilised material is hygroscopic: it will take up water from humid air if a cold vial is opened before it has warmed up.
Salt forms and counter-ions
Basic side chains (Lys, Arg, His) and a free N-terminus are protonated after cleavage and purification, so the peptide is isolated as a salt with an anion from the process – most commonly trifluoroacetate, sometimes exchanged to acetate or chloride. The counter-ion is part of the weighed mass but not part of the peptide. It can also matter biologically: residual trifluoroacetate has been reported to inhibit proliferation of osteoblasts and chondrocytes in culture at low concentrations [4]. For sensitive cell assays, note the salt form stated on the certificate and include a vehicle control prepared the same way.
Purity, peptide content and gross weight
Three different numbers describe the material in a vial, and they are often confused:
| Quantity | What it measures | How it is determined |
|---|---|---|
| Gross (fill) weight | Total solid in the vial: peptide plus counter-ions, residual water and any other non-peptide material | Weighing at fill; this is the figure on the label (e.g. 10 mg) |
| HPLC purity | The proportion of the UV-absorbing peptide material that is the target sequence, as a percentage of total peak area | Reversed-phase HPLC, typically detected at 214–220 nm |
| Net peptide content | The proportion of the gross weight that is peptide (of any sequence) rather than salt and water – often in the range 60–90% | Amino-acid analysis, elemental nitrogen analysis or quantitative NMR |
A peptide can be 98% pure by HPLC and still have a net peptide content of 75%: the impurities are few, but a quarter of the weighed mass is counter-ion and water. When an experiment depends on an exact molar concentration, the net peptide content – if it has been measured for that lot – should be used to correct the mass (see the worked example in Chapter 3) [5].
Molecular weight: average and monoisotopic
Two masses are quoted for peptides. The average molecular weight uses natural isotope abundances and is the one to use for weighing and molarity calculations. The monoisotopic mass counts only the most abundant isotope of each element (¹²C, ¹H, ¹⁴N, ¹⁶O) and is the one that a high-resolution mass spectrometer reports for the lightest peak in an isotope cluster. For BPC-157 (C₆₂H₉₈N₁₆O₂₂) the average molecular weight is about 1419.5 g/mol and the monoisotopic mass about 1418.7 Da. Unless a salt form is specified, catalogue molecular weights refer to the free peptide.
Chapter 2Reading a Britpep certificate of analysis
A certificate of analysis (COA) is a record of tests carried out on one specific lot of material. It is the main evidence a researcher has that the powder in the vial is what the label says it is. Learning to read one critically takes a few minutes and saves a great deal of uncertainty later.
Who performed the analysis
Every Britpep certificate states, near the top, who performed the testing and who issued the original report – for example the manufacturer's quality-control laboratory or a named analytical laboratory. Britpep transcribes the results onto Britpep headed paper exactly as they appear on the original, without rounding or alteration, and does not represent itself as the tester. The original manufacturer's certificate or laboratory report for any lot is available on request from [email protected].
The fields, one by one
| Field | What to check |
|---|---|
| Compound and batch (lot) number | The lot on the certificate must match the BATCH line on your vial label. A certificate for a different lot tells you nothing about your material. |
| Test date | When the analysis was carried out. Results describe the lot at that time. |
| Retest or expiry date | Where given, the date by which the lot should be re-analysed or no longer relied upon for its stated specification. Not every original report includes one. |
| Storage condition | The temperature at which the lot was held and should continue to be held. |
| Identity: formula, molecular weight, sequence | These should match the published structure of the compound. Some reports also state the salt form. |
| Appearance | Usually “white to off-white powder”. Copper complexes such as GHK-Cu are blue. |
| HPLC purity | The headline purity figure, with the acceptance criterion it was tested against. |
| Mass spectrum | Confirms that a species of the expected mass is present – the identity test. |
| Other tests | Some reports include water content, peptide content, residual solvents or related substances. Where a test was not performed the certificate says so. |
The HPLC result
Reversed-phase HPLC separates molecules by hydrophobicity on a C18 or similar column using a water/acetonitrile gradient, usually with a small amount of acid. Peptide bonds absorb strongly at 214–220 nm, so the chromatogram shows the target peptide as a main peak and related impurities as smaller peaks either side. Purity is the area of the main peak divided by the total area of all integrated peaks.
Three limitations are worth remembering. HPLC purity says nothing about counter-ions, water or other material that does not absorb in the UV; an impurity that co-elutes with the main peak is invisible; and the figure depends on the method, so numbers from different laboratories are not always directly comparable [2][5].
The mass spectrum
Electrospray mass spectrometry measures mass-to-charge ratio (m/z). Peptides pick up one or more protons, so a single compound can appear at several m/z values: [M+H]⁺, [M+2H]²⁺, [M+3H]³⁺ and so on. Larger peptides carry more charges.
Monoisotopic mass M ≈ 1418.70 Da; mass of a proton ≈ 1.007 Da.
[M+H]⁺ = (1418.70 + 1.007) / 1 ≈ 1419.7
[M+2H]²⁺ = (1418.70 + 2 × 1.007) / 2 ≈ 710.4
A spectrum showing ions near 1419.7 and 710.4 is consistent with the expected sequence. Sodium ([M+Na]⁺, +22 Da relative to [M+H]⁺) and potassium adducts are common and are not impurities in themselves.
Looking up a lot on britpep.co.uk
- Find the BATCH line on the vial label.
- Enter it in the COA checker at britpep.co.uk/coa-checker, or open the product page – each lists the lots with a published certificate.
- Download the Britpep certificate and confirm that the compound, lot number and vial size all match.
- If you need the manufacturer's or laboratory's original document for your records, email [email protected] quoting the lot number.
Questions to ask of any certificate
- Does the lot number match the vial in front of you?
- Is the organisation that carried out the analysis identified?
- Is there an identity test (mass spectrum), not just a purity number?
- Is the observed mass consistent with the expected molecular weight of the sequence?
- Is the purity reported against a stated acceptance criterion?
- Are dates present and plausible – test date before dispatch, retest date (if given) in the future?
- Are results reported as measured values rather than only “pass”?
Chapter 3Preparing solutions at the bench
Most problems with peptide experiments begin in the first ten minutes: the wrong solvent, an assumed molecular weight, or a stock solution that is never quite fully dissolved. This chapter sets out the calculations and the bench routine in order.
Before you open the vial
- Read the safety data sheet and complete your organisation's COSHH or equivalent risk assessment. Treat every research peptide as a material of unknown biological activity: wear a lab coat, gloves and eye protection, and weigh or handle open powders in a ventilated enclosure.
- Let the sealed vial reach room temperature – ideally inside a desiccator – before removing the cap. Opening a cold vial draws in condensation, and water on a hygroscopic powder accelerates hydrolysis and clumping [3].
- Tap or briefly centrifuge the vial so that loose powder collects at the bottom.
- Record the lot number, vial size, molecular weight and salt form (from the certificate) in your notebook before you start.
The three equations you need
| Mass concentration | c (mg/mL) = mass of peptide (mg) ÷ volume (mL) |
| Molar concentration | C (mol/L) = c (g/L) ÷ MW (g/mol) equivalently, C (mM) = c (mg/mL) ÷ MW (g/mol) × 1000 |
| Volume for a target molarity | V (mL) = mass (mg) ÷ [ MW (g/mol) × C (mM) ] × 1000 |
| Dilution | C₁ × V₁ = C₂ × V₂ |
Use the molecular weight from the certificate for your lot where one is given, since it reflects the exact structure supplied. Molecular weights in the catalogue are for the free peptide unless a salt form is stated.
Vial: 5 mg BPC-157. MW = 1419.5 g/mol. Target: 1 mM stock.
Amount = 5 mg ÷ 1419.5 g/mol = 3.522 µmol
Volume = 3.522 µmol ÷ 1 mM (1 µmol/mL) = 3.52 mL
Dissolving the whole vial in 3.52 mL of solvent gives 1.41 mg/mL, which is 1.00 mM.
From the 1 mM stock above, prepare 10 mL of 10 µM in assay buffer or culture medium.
V₁ = C₂ × V₂ ÷ C₁ = 10 µM × 10 mL ÷ 1000 µM = 0.100 mL
Add 100 µL of stock to 9.90 mL of buffer. For a dilution series, it is usually more accurate to make an intermediate (e.g. 100 µM) than to pipette very small volumes.
Vial: 10 mg KPV (Lys-Pro-Val). MW = 342.4 g/mol. Target: 10 mM.
Amount = 10 mg ÷ 342.4 g/mol = 29.21 µmol
Volume = 29.21 µmol ÷ 10 µmol/mL = 2.92 mL
Because KPV is small, a given mass contains many more molecules than the same mass of a larger peptide – a reminder that equal mg/mL concentrations of different peptides are not equimolar.
If a lot's measured net peptide content is 80%, a 5 mg vial contains about 5 × 0.80 = 4.0 mg of peptide. For BPC-157 that is 4.0 ÷ 1419.5 = 2.818 µmol, so 2.82 mL (not 3.52 mL) gives a true 1 mM solution. Where no peptide-content figure is reported, state in your methods that concentrations are based on gross weight.
Quick reference – mass concentration
| Peptide in vial | in 1.0 mL | in 2.0 mL | in 5.0 mL | in 10.0 mL |
|---|---|---|---|---|
| 2 mg | 2.0 mg/mL | 1.0 mg/mL | 0.40 mg/mL | 0.20 mg/mL |
| 5 mg | 5.0 mg/mL | 2.5 mg/mL | 1.0 mg/mL | 0.50 mg/mL |
| 10 mg | 10 mg/mL | 5.0 mg/mL | 2.0 mg/mL | 1.0 mg/mL |
| 20 mg | 20 mg/mL | 10 mg/mL | 4.0 mg/mL | 2.0 mg/mL |
| 50 mg | 50 mg/mL | 25 mg/mL | 10 mg/mL | 5.0 mg/mL |
Quick reference – molar stocks
Volumes of solvent that dissolve a whole vial to give 1 mM or 10 mM, based on the free-peptide molecular weight and the gross fill weight (correct for peptide content where it is known).
| Compound | MW (g/mol) | Vial | Amount | Volume for 1 mM | Volume for 10 mM |
|---|---|---|---|---|---|
| BPC-157 | 1,419.5 | 5 mg | 3.52 µmol | 3.52 mL | 0.352 mL |
| KPV | 342.4 | 10 mg | 29.21 µmol | 29.21 mL | 2.921 mL |
| Epitalon | 390.3 | 10 mg | 25.62 µmol | 25.62 mL | 2.562 mL |
| GHK-Cu | 401.9 | 50 mg | 124.41 µmol | 124.41 mL | 12.441 mL |
| Ipamorelin | 711.9 | 5 mg | 7.02 µmol | 7.02 mL | 0.702 mL |
| Kisspeptin-10 | 1,302.4 | 5 mg | 3.84 µmol | 3.84 mL | 0.384 mL |
| Thymosin Alpha-1 | 3,108.3 | 5 mg | 1.61 µmol | 1.61 mL | 0.161 mL |
Choosing a solvent
Solubility is governed mainly by a peptide's net charge at the working pH and by the proportion of hydrophobic residues. A quick estimate of net charge at pH 7 is a good starting point:
- Count +1 for each Lys (K) and Arg (R), and for a free N-terminus. His (H) is only partly protonated at pH 7; count it as +0.5 or ignore it.
- Count −1 for each Asp (D) and Glu (E), and for a free C-terminal acid (an amide C-terminus contributes nothing).
- Note how many residues are hydrophobic (Ala, Val, Leu, Ile, Met, Phe, Trp, Pro) and whether there are Cys or Met residues, which oxidise readily.
| Peptide character | First solvent to try | If it does not dissolve |
|---|---|---|
| Net positive (basic) | Sterile water | Add dilute acetic acid (around 10%) dropwise, then dilute with water or buffer |
| Net negative (acidic) | Sterile water or a near-neutral buffer | Add a small amount of dilute aqueous ammonia or ammonium bicarbonate, then dilute |
| Neutral or largely hydrophobic | A minimal volume of DMSO (or DMF), then add aqueous buffer slowly while mixing | Increase the organic fraction, or use acetonitrile/water for analytical work; avoid DMSO for peptides containing free Cys or Met, which it can oxidise |
| Lipidated (e.g. palmitoyl) | DMSO or ethanol | Warm gently; dilute into buffer containing carrier protein if the assay allows |
Sequence GEPPPGKPADDAGLV, free N- and C-termini. Positive: Lys (+1), N-terminus (+1) = +2. Negative: Glu, Asp, Asp (−3), C-terminus (−1) = −4. Net charge at pH 7 ≈ −2, so BPC-157 behaves as an acidic peptide: water or a neutral to slightly basic buffer is the logical first choice.
Always test solubility on a small portion first if you are unsure, so that a poor solvent choice does not compromise the whole vial. In cell assays, keep the final concentration of organic solvent low and consistent across conditions (for DMSO, commonly 0.1–0.5% or less, depending on the cell type), and include a solvent-only control.
Dissolving the peptide
- Add the calculated volume of solvent with a calibrated pipette, letting it run down the inside wall of the vial rather than jetting onto the powder.
- Replace the cap and roll or gently invert the vial until the solid has dissolved. Vigorous vortexing encourages foaming, and air–liquid interfaces promote aggregation of some peptides [6].
- If particles persist, allow a few minutes at room temperature, then try a brief burst in an ultrasonic bath, keeping the vial cool.
- Inspect against a dark and a light background. The solution should be clear; persistent haze or particles mean the peptide is not fully in solution, and the true concentration is unknown.
Sterile filtration for cell culture
Lyophilised research peptides are not supplied as sterile products. For cell-culture work, pass the dissolved stock through a 0.22 µm membrane filter with low protein binding (PES or PVDF are common choices) inside a biological safety cabinet. Filter membranes and housings retain a small hold-up volume and can adsorb some peptide, which matters for small volumes or very dilute solutions: filter the concentrated stock rather than the final dilution, pre-rinse with solvent if your protocol allows, and consider verifying the concentration of the filtrate for quantitative work. Filtration removes microorganisms but not endotoxin.
Aliquoting and labelling
Divide the stock into single-experiment volumes in low-binding polypropylene tubes as soon as it is made, so that each tube is thawed once and then used or discarded. Label every tube with the compound, Britpep lot number, concentration (with its unit, mg/mL or mM), solvent, date prepared and your initials, and record the same details in your notebook. Good aliquoting is the single most effective way to avoid freeze–thaw damage and to trace an unexpected result back to its source.
Chapter 4Storage and stability
Peptides degrade by a small number of well-understood chemical and physical routes. Knowing which ones apply to a given sequence makes it easier to choose storage conditions and to recognise when material may have changed [6].
| Degradation route | Residues or features at risk | How to limit it |
|---|---|---|
| Oxidation | Met, Cys, Trp; His to a lesser extent | Minimise headspace and light; use degassed solvents; avoid DMSO with Cys/Met; store frozen |
| Deamidation | Asn (especially Asn-Gly) and Gln | Keep solutions slightly acidic (around pH 5–6) and cold; avoid prolonged storage in solution |
| Hydrolysis and cleavage | Asp-Pro and Asp-Gly bonds; strongly acidic or basic conditions | Avoid extremes of pH; keep moisture out of solid material |
| Aggregation | Hydrophobic or amyloid-prone sequences; high concentration | Dissolve completely; avoid foaming and repeated freeze–thaw; store at a sensible concentration |
| Adsorption | Most peptides at low concentration, especially hydrophobic ones | Use low-binding plastics; keep stocks concentrated; add carrier protein to working solutions where compatible |
| Disulfide scrambling | Peptides with more than one Cys | Avoid basic pH and reducing/oxidising agents unless intended |
Recommended conditions
| Form | Recommended storage | Notes |
|---|---|---|
| Lyophilised, unopened | −20 °C or below, sealed, dark, dry | Follow the storage line on the product page and certificate. Short periods at ambient temperature (for example in transit) are generally tolerated by lyophilised solids. |
| Lyophilised, opened | −20 °C, tightly re-capped, in a desiccated container | Warm to room temperature before each opening. Consider dissolving and aliquoting the whole vial instead of repeated weighing. |
| Stock solution | Single-use aliquots at −20 °C; −80 °C for longer periods | Thaw once. Stability in solution is sequence-dependent and should be verified for long studies. |
| Working dilution | Prepare fresh on the day; keep on ice or at 2–8 °C | Discard at the end of the experiment rather than re-freezing. |
Why lyophilised material lasts longer
In the dry state, molecular mobility is low and water – a reactant in hydrolysis and deamidation and a medium for most other reactions – is largely absent [3]. Residual moisture and uneven distribution of components within the dried cake can still affect stability, which is one reason why an opened vial should be kept dry and re-sealed promptly [7]. Once a peptide is in solution, the clock runs much faster.
Retest dates and your own records
A retest or expiry date on a certificate applies to the lot stored under the stated condition in its original closure. Your own handling – opening, dissolving, freezing – starts a new history. For work that runs over months, it is good practice to record the date each vial was opened and each stock prepared, and to re-check identity or purity by HPLC–MS if results begin to drift.
Chapter 5Troubleshooting
The table below collects problems that laboratories commonly encounter with peptide reagents, with the usual causes and practical next steps.
| What you see | Likely cause | What to try |
|---|---|---|
| Vial appears empty | Small mass dried as a thin film on the glass | Check the label; add solvent and rinse the walls and stopper underside by gentle rolling |
| Powder will not dissolve | Solvent unsuited to the peptide's charge or hydrophobicity | Recalculate net charge; add dilute acid or base, or a small volume of DMSO, as in Chapter 3; test on a small portion |
| Clear stock turns cloudy when diluted into buffer | Buffer pH close to the isoelectric point; salting out; organic solvent too dilute | Dilute more slowly with mixing; change buffer pH; keep a little more co-solvent; lower the working concentration |
| Solution forms a gel | Self-association of aggregation-prone sequences at high concentration | Prepare a more dilute stock; use a chaotrope or organic co-solvent for analytical work if compatible |
| Foam or bubbles after mixing | Vortexing or forceful pipetting | Let it settle; briefly centrifuge; mix by gentle inversion next time |
| Response falls over the course of a study | Freeze–thaw damage, oxidation, adsorption to plastics, or stock older than its stability window | Use fresh single-use aliquots; switch to low-binding tubes; re-check by HPLC–MS |
| Unexpected toxicity in cell culture | Organic solvent concentration, residual TFA, endotoxin, or the peptide itself | Run solvent-only and counter-ion controls; reduce DMSO; consider an acetate or HCl salt form; test for endotoxin if relevant |
| Different lots give different results | Differences in net peptide content, salt form or impurity profile | Compare certificates; normalise by peptide content where measured; record the lot number with every dataset |
| Measured concentration lower than calculated | Calculation used gross weight; losses on filters or plastics | Correct for peptide content; quantify by UV (A280 if Trp/Tyr present, A205/A214 otherwise) or amino-acid analysis |
| Your MS shows extra peaks compared with the COA | Sodium or potassium adducts, different charge states, oxidation (+16 Da) | Assign peaks by mass difference before concluding the material is impure |
| GHK-Cu or AHK-Cu solution is blue | Normal – the colour comes from the copper(II) complex | No action needed. A colourless solution would suggest copper has been lost |
| Label is damaged or unreadable | Condensation or solvent splashes | Re-label secondary containers immediately; email us with your order number for the lot details |
If a problem persists and you suspect the material, contact [email protected] with the lot number, how the vial was stored and prepared, and any analytical data you have.
Chapter 6The Britpep catalogue by research area
Britpep products grouped by the research field in which each compound most often appears in the literature. For each entry we list up to two peer-reviewed research areas with the model type, citations, and the product page, where you will find structural data, storage information, lot certificates and a fuller literature summary – including, separately and clearly labelled, any emerging or unconfirmed lines of enquiry. Inclusion of a research area describes what has been studied; it is not a claim of any effect.
Evidence status labels are taken from the product pages and summarise the overall state of the published literature.
Cell signalling
Peptides and proteins used to probe intracellular signalling, growth-factor receptor pathways and cell migration in culture and tissue models.
Soluble activin receptor type IIB–Fc fusion protein (ActRIIB-Fc), studied in TGF-β superfamily signalling research.
- Skeletal muscle mass Mouse [8]
Synthetic 15-residue peptide corresponding to a partial sequence of a gastric protein, used in cell-signalling research.
- Tendon and ligament injury models Rodent; in vitro [9][10][11]
- Angiogenesis and vascular models In vitro; rodent [12]
5 mg · 10 mg · 20 mg britpep.co.uk/products/bpc-157/
Pre-mixed lyophilised combination of BPC-157 and TB-500 in a 1:1 ratio by mass (5 mg + 5 mg or 10 mg + 10 mg per vial).
- Pre-mixed research blend. Published research concerns the individual components (BPC-157, TB-500 (Thymosin β4)); no peer-reviewed studies of the blend itself were identified.
10 mg · 20 mg britpep.co.uk/products/bpc-157-tb-500/
Cytoskeleton & cell migration
Compounds studied in relation to actin dynamics, cell motility and tissue-repair models.
Synthetic thymosin β4-related peptide used in actin-cytoskeleton research.
5 mg · 10 mg britpep.co.uk/products/tb-500/
Extracellular matrix & fibroblast biology
Peptides examined in fibroblast culture and matrix-production studies, and multi-component blends built around them.
Copper(II) complex of the tripeptide Gly-His-Lys, used in fibroblast and extracellular-matrix research.
- Fibroblast and extracellular-matrix biology In vitro [15][16]
- Acute lung injury and fibrosis Mouse [17][18]
50 mg · 100 mg britpep.co.uk/products/ghk-cu/
Pre-mixed lyophilised combination of BPC-157, GHK-Cu, TB-500 and KPV (10 mg + 50 mg + 10 mg + 10 mg per vial).
- Pre-mixed research blend. Published research concerns the individual components (BPC-157, GHK-Cu, TB-500 (Thymosin β4), KPV); no peer-reviewed studies of the blend itself were identified.
Pre-mixed lyophilised combination of BPC-157, GHK-Cu and TB-500 (10 mg + 50 mg + 10 mg per vial).
- Pre-mixed research blend. Published research concerns the individual components (BPC-157, GHK-Cu, TB-500 (Thymosin β4)); no peer-reviewed studies of the blend itself were identified.
Cosmetic-science peptides
Short signal peptides that are characterised in cosmetic-science and formulation research.
Copper(II) complex of the tripeptide Ala-His-Lys, a GHK-Cu analogue used in cosmetic-science research.
- Hair follicle and dermal papilla cell biology Ex vivo / in vitro (human tissue) [19]
50 mg · 100 mg britpep.co.uk/products/ahk-cu/
Palmitoylated pentapeptide (Pal-KTTKS) used in cosmetic-science and extracellular-matrix research.
Acetylated octapeptide modelled on the N-terminus of SNAP-25, used in cosmetic-science research.
- SNARE complex and exocytosis (parent hexapeptide) In vitro [22]
Inflammatory signalling
Peptides investigated in models of inflammatory signalling.
11-residue peptide derived from erythropoietin helix B, used in EPOR/CD131 receptor-signalling research.
Immunology
Thymus-derived peptides and preparations studied in immunology research.
Polypeptide preparation extracted from bovine thymus, used in immunology research.
N-acetylated 28-residue thymic peptide, used in immunology research.
- Published research on this compound is mainly clinical. It is summarised, with citations, on the product page.
5 mg · 10 mg britpep.co.uk/products/thymosin-alpha-1/
Neuropeptide research
Neuropeptides and related compounds studied in neuronal cell culture, behavioural models and neuroscience research.
Synthetic, modified analogue of the heptapeptide Semax, used in neuropeptide research.
- Little peer-reviewed research is publicly available for this compound.
5 mg · 10 mg britpep.co.uk/products/adamax/
Mixture of low-molecular-weight peptides and amino acids derived from porcine brain protein, used in neurotrophic-signalling research.
Delta sleep-inducing peptide, a nonapeptide used in neuropeptide research.
5 mg · 10 mg · 15 mg britpep.co.uk/products/dsip/
Seven-residue peptide derived from spadin, used in TREK-1 channel research.
Synthetic tripeptide Glu-Asp-Arg used in neuronal cell-culture research.
Synthetic heptapeptide analogue of tuftsin extended with Pro-Gly-Pro, used in neuropeptide and immunomodulatory-signalling research.
5 mg · 10 mg britpep.co.uk/products/selank/
Synthetic heptapeptide analogue of the ACTH(4–7) fragment extended with Pro-Gly-Pro, used in neuropeptide research.
5 mg · 10 mg britpep.co.uk/products/semax/
Pre-mixed lyophilised combination of Semax and Selank (10 mg + 10 mg per vial), for comparative neuropeptide research.
28-residue neuropeptide of the secretin/glucagon family, used in VPAC receptor research.
- Immune regulation In vitro; rodent [47]
5 mg · 10 mg britpep.co.uk/products/vip/
Endocrine & receptor signalling
Ligands for growth-hormone-releasing hormone, ghrelin, kisspeptin and related receptors, plus IGF-1 analogues widely used in cell culture.
Modified C-terminal fragment (residues 176–191) of human growth hormone, studied in lipid-metabolism research.
- β3-AR dependence β3-AR knockout mice [48]
5 mg · 10 mg britpep.co.uk/products/aod9604/
GHRH(1–29) analogue carrying a Drug Affinity Complex (maleimido linker) for albumin conjugation, used in GHRH-receptor research.
- GRF receptor activation and albumin conjugation In vitro; rat [49]
2 mg · 5 mg · 10 mg britpep.co.uk/products/cjc-1295-dac/
Tetra-substituted GHRH(1–29) amide analogue (also called modified GRF 1–29), used in GHRH-receptor research.
- Published research on this compound is mainly clinical. It is summarised, with citations, on the product page.
5 mg · 10 mg britpep.co.uk/products/cjc-1295-no-dac/
Long-R3 analogue of insulin-like growth factor 1 with reduced IGF-binding-protein affinity, widely used in cell-culture research.
0.1 mg · 1 mg britpep.co.uk/products/igf-1-lr3/
Synthetic pentapeptide agonist of the ghrelin receptor (GHS-R1a), used in growth-hormone-secretagogue receptor research.
5 mg · 10 mg britpep.co.uk/products/ipamorelin/
C-terminal decapeptide of kisspeptin, used in KISS1R (GPR54) receptor research.
5 mg · 10 mg britpep.co.uk/products/kisspeptin-10/
N-terminally modified GHRH(1–44) amide analogue, used in GHRH-receptor research.
- Published research on this compound is mainly clinical. It is summarised, with citations, on the product page.
5 mg · 10 mg · 20 mg britpep.co.uk/products/tesamorelin/
Pre-mixed lyophilised combination of CJC-1295 without DAC and Ipamorelin (5 mg + 5 mg per vial).
- Pre-mixed research blend. Published research concerns the individual components (CJC-1295 (without DAC), Ipamorelin); no peer-reviewed studies of the blend itself were identified.
Mitochondrial & metabolic biochemistry
Mitochondrial-derived peptides, metabolic enzyme modulators and cofactors used in metabolic biochemistry.
Small-molecule methylquinolinium compound studied as an NNMT inhibitor in cell models.
5 mg · 10 mg · 20 mg · 50 mg britpep.co.uk/products/5-amino-1mq/
Adenosine analogue (AICA-riboside) widely used as an AMPK activator in cell-biology research.
- AMPK signalling In vitro (hepatocytes, adipocytes) [60]
- Endurance and metabolic gene expression Mouse [61]
50 mg · 100 mg britpep.co.uk/products/aicar/
16-residue mitochondrial-derived peptide encoded in the 12S rRNA region of mtDNA, used in metabolic biochemistry research.
- Diet-induced and age-related insulin resistance Mouse [62]
- Physical capacity in young, middle-aged and old animals Mouse [63]
10 mg · 20 mg · 40 mg britpep.co.uk/products/mots-c/
Nicotinamide adenine dinucleotide (oxidised form), an essential redox cofactor used in enzymology and metabolism research.
500 mg · 1000 mg britpep.co.uk/products/nad/
Small-molecule oestrogen-related receptor (ERR) agonist used in nuclear-receptor research.
Cell-permeable aromatic-cationic tetrapeptide that targets the inner mitochondrial membrane, used in mitochondrial research.
10 mg · 50 mg britpep.co.uk/products/ss-31/
Redox biochemistry
Reagents for redox and oxidative-stress biochemistry.
The tripeptide γ-Glu-Cys-Gly (GSH), a standard reagent in redox biochemistry.
600 mg · 1500 mg britpep.co.uk/products/glutathione/
Telomere & cellular senescence
Compounds investigated in telomere biology and cellular senescence.
Synthetic tetrapeptide (Ala-Glu-Asp-Gly) used in telomerase and cell-culture research.
- Telomere biology In vitro (human cells) [73][74]
- Spontaneous and transgenic tumour models Mouse [75][76]
10 mg · 50 mg britpep.co.uk/products/epitalon/
D-retro-inverso peptide designed to disrupt the FOXO4–p53 interaction, used in cellular-senescence research.
- Chemotoxicity and ageing models Mouse (fast-ageing XpdTTD/TTD and naturally aged) [77]
- Senescent Leydig cells In vitro; aged mice [78]
2 mg · 10 mg britpep.co.uk/products/foxo4-dri/
Oncology cell models
Peptides studied in cancer cell-line research.
Chimeric peptide (p53-derived HDM-2-binding domain + membrane-penetrating sequence) used in cancer cell-line research.
5 mg · 10 mg britpep.co.uk/products/pnc-27/
Chapter 7Ordering from Britpep
Made to order
Every order is prepared to order. Please allow approximately 7 days for preparation before dispatch.
UK delivery
Orders are sent by Royal Mail Tracked 24 at a flat £5.95. We deliver to UK addresses only and do not ship internationally.
Trade accounts
Universities, research institutes, CROs and R&D laboratories can apply for a trade account for quotations, purchase orders and invoice terms at britpep.co.uk/trade-account.
Certificates
Look up the certificate for any lot at britpep.co.uk/coa-checker. Originals are available on request from [email protected].
Who can buy
Britpep supplies research materials to purchasers aged 18 or over who confirm at checkout that the products will be used only for laboratory research. We may ask for further information about the intended research use, and we may refuse or cancel any order.
Contact
Email [email protected] for quotations, technical questions about certificates or handling, and queries about an order in preparation. The full catalogue, product pages and the Britpep research library are at britpep.co.uk.
SourcesReferences
Numbered in order of first citation. PubMed identifiers and DOIs were checked at the time of writing. Each summary in this handbook describes what the cited source reports; none is a claim about Britpep products.
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- The Human Medicines Regulations 2012, regulation 2: medicinal products. legislation.gov.uk. www.legislation.gov.uk/uksi/2012/1916/regulation/2
- Medicines and Healthcare products Regulatory Agency. Borderline products: how to tell if your product is a medicine. GOV.UK guidance. www.gov.uk/guidance/borderline-products-how-to-tell-if-your-product-is-a-medicine
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ImportantResearch use only – legal notice
All products supplied by Britpep are intended solely for in-vitro laboratory research and analytical use by suitably qualified persons. They are not medicinal products and have not been authorised as medicines by the Medicines and Healthcare products Regulatory Agency (MHRA) or any other regulator. They are not food, food supplements, cosmetics, veterinary medicines or medical devices, must not be administered to humans or animals in any way, and are not for consumption.
In the UK a product can be regulated as a medicine either because of what it does or because of how it is presented – including any claim, implied or explicit, that it treats or prevents disease [83][84]. Britpep does not make, and nothing in this handbook should be read as, any claim that a product treats, prevents, cures, diagnoses or alleviates any disease or condition, or that it is suitable for any use in people or animals. Descriptions of published research summarise what investigators have reported in the models stated; they are provided for scientific context only, are not statements of efficacy or safety, and have not been evaluated by the MHRA [85].
Purchasers are responsible for ensuring that they are competent to handle these materials; that they hold any approvals required for their work; that all handling, storage and disposal comply with applicable law, including the Control of Substances Hazardous to Health Regulations 2002 and local institutional rules; and that products are used only for lawful laboratory research. The toxicological properties of many research compounds have not been fully investigated.
The information in this handbook is general technical guidance for laboratory work, prepared with care and believed to be accurate at the time of publication. It is not medical, legal or regulatory advice, and it does not replace your own validation of methods or the professional judgement of your laboratory. Britpep's liability in respect of products is set out in its terms of sale at britpep.co.uk/legal/terms, and its research use policy is at britpep.co.uk/legal/research-use.
© 2026 Britpep. britpep.co.uk · [email protected]. Product names mentioned are used descriptively to identify research compounds. This handbook may be printed or shared in full for non-commercial laboratory use.