CJC-1295 Ipamorelin Canada: Checking the 10mg Two-Peptide Blend
A two-peptide vial saves inventory lines, but it doubles the identity questions a QC lab has to answer. The CJC-1295 ipamorelin blend is a good example: one component is a 29-residue chain that folds into a helix, while its partner has just five residues, most of them non-standard. This article looks at the blend as it is supplied to research labs buying CJC-1295 ipamorelin in Canada, covering what the vial holds, how the two components behave in mass spectrometry and HPLC, and what a complete lot check should include.
Two very different peptides sharing a vial
The 10 mg blend contains 5 mg of each component, combined before freeze-drying.
| CJC-1295 without DAC (Mod GRF 1-29) | Ipamorelin | |
|---|---|---|
| Length | 29 residues | 5 residues |
| Sequence notation | [D-Ala2, Gln8, Ala15, Leu27]-GRF(1-29)-NH2 | Aib-His-D-2-Nal-D-Phe-Lys-NH2 |
| Formula | C152H252N44O42 | C38H49N9O5 |
| Average mass | 3367.9 g/mol | 711.9 g/mol |
| CAS | 863288-34-0 | 170851-70-4 |
| C-terminus | Amide | Amide |
The larger component is the form without the drug affinity complex. It should not be confused with the DAC conjugate, which carries an extra lysine and linker and is noticeably heavier; our note on the DAC and no-DAC forms explains the difference. Structurally the two components belong to separate families as well: one is a modified releasing-hormone fragment, the other a designed secretagogue, a distinction covered in GHRH analogues compared with secretagogues.
Equal milligrams, unequal molecule counts
A 1:1 split by weight is far from 1:1 by molecule count, because ipamorelin is less than a quarter the size of its partner. Working from the average masses:
- 5 mg of Mod GRF 1-29 is roughly 1.5 micromoles
- 5 mg of ipamorelin is roughly 7.0 micromoles
So each vial holds close to five ipamorelin molecules for every Mod GRF 1-29 molecule. For in-vitro designs that compare the blend against single-compound controls, molar amounts are usually the fairer basis for matching.
Reading the mass spectrum without mixing up ions
Under electrospray the two components ionise very differently. Ipamorelin mostly appears as a singly protonated ion near m/z 712.4. Mod GRF 1-29, at almost 3,370 Da, spreads across several charge states: roughly m/z 674.6 for the 5+ ion, 843.0 for 4+ and 1123.6 for 3+.
The ipamorelin ion therefore lands in the gap between the 5+ and 4+ signals of Mod GRF 1-29, and in a quick look at a narrow window it can be mistaken for part of the same envelope. The reliable way to tell them apart is the spacing of the isotope peaks. For a 1+ ion they sit about 1 m/z unit apart; for a 5+ ion they sit about 0.2 apart. Assign charge from that spacing, never from where a peak happens to land. A spectrum shown at too low a resolution to see the isotopes has left out exactly the information needed.
Two peaks, two wavelengths, no shortcut to the ratio
On reversed-phase HPLC the two components differ enough in size and hydrophobicity to separate as two clear main peaks. That is the first thing to confirm on any report.
This blend also allows a second detection channel. Mod GRF 1-29 has tyrosine at positions 1 and 10, and ipamorelin carries the naphthyl side chain of D-2-Nal, so both absorb in the 275 to 280 nm range. Recording 280 nm alongside the usual 214 nm gives each peak a characteristic area ratio between channels, a small but useful piece of identity evidence that many blends cannot provide because one component lacks any aromatic residue.
What neither wavelength gives is the mass ratio. Low-UV response depends largely on the number of peptide bonds, with aromatic side chains adding to it, and Mod GRF 1-29 has far more peptide bonds than ipamorelin. Equal milligrams will not produce equal peak areas. Converting areas to amounts needs a reference standard for each component; our article on purity and composition in multi-peptide vials covers the general problem.
Stereocentres a routine report leaves open
The blend contains three deliberate D-residues: D-alanine at position 2 of Mod GRF 1-29, and D-2-naphthylalanine and D-phenylalanine in ipamorelin. An L residue at any of those positions produces a diastereomer identical in formula and mass to the intended compound.
Mass spectrometry cannot see that, and standard amino acid analysis reports composition without configuration. Only a chiral method, or an HPLC method shown to separate the relevant diastereomers, answers the question. Few routine certificates include one, so it is worth recording as an open item. Our pieces on racemisation and chiral purity and on ipamorelin’s unusual residues go further.
Checking CJC-1295 ipamorelin in Canada: a lot checklist
For a lab receiving a batch of blend vials, a consistent checklist makes each lot comparable with the last:
- Confirm the label and certificate specify the no-DAC form and state both amidated sequences.
- Look for both masses on the report, with charge states assigned from isotope spacing.
- Confirm the chromatogram shows two identified main peaks, ideally at 214 and 280 nm.
- Check that composition is given per component in milligrams, not as one blended purity figure.
- Group vials by cap and crimp colour, pair each group with its certificate, and log lot, count and storage location on arrival.
Every product we list goes through third-party HPLC purity testing, and certificates for a selection of products are posted on our COA page.
Blend or single vials for volume work
A premixed vial fixes the ratio. If your design needs to vary it, or to run each component alone as a control, the single-compound CJC-1295 without DAC and ipamorelin vials give that flexibility. Volume pricing is mix-and-match, so blend and single vials in the same cart all count toward the same break.
Both peptides, blended or single, are sold strictly as in-vitro research material and must not be used in humans or animals.

