Details up front: Medutest · 98.8%.
I have a result I cannot explain, and I would rather diagnose it than guess.
I have checked the obvious explanations and eliminated the two easiest ones.
What would you check first, and what would you conclude from each outcome?
A 98.8 per cent result against a higher certificate figure is usually a method difference, not a disagreement about the vial. Inter-laboratory spread on identical peptide material runs half a per cent to a full per cent by RP-HPLC. Gradient slope, detection wavelength and integration convention each move the number, and a gentler gradient resolves impurities that a steeper one hides under the main peak — so the better method reports the worse figure. Get the column, the gradient and the wavelength from both Medutest and the supplier before treating 98.8 per cent as a contradiction.
Understanding purity requires separating the chemistry from the method from the reporting convention, and the three are not independent.
Tailing factor measures peak shape, and a badly tailing peak spreads into the region where small impurities live, forcing tangent-skim integration that assigns tail area to the main peak.
Sample solvent strength affects peak shape — if you inject in strong solvent on a gradient starting in weak solvent, the solvent peak can distort your main peak or create a false shoulder.
The Arrhenius relationship for peptide degradation is the basis of accelerated stability testing and also governs how quickly methods drift with temperature.
The practical summary: ask for the chromatogram and the method, and ignore the headline number until you have both.
Analytical standards and reagents with traceable certificates. Every quantitative result you read inherits the accuracy of the standard behind it.
Shop standardsThe single most important distinction is between what purity measures — the fraction of detected material that is your target — and what you actually want to know — how much of the material in the vial is your target.
Column pore size affects mass transfer — a 100 Angstrom packing on a 5 kDa peptide restricts diffusion, broadening the peak and potentially hiding small impurities in the shoulders.
Mobile phase additive choice affects ionisation and peak shape — TFA gives sharp peaks but suppresses mass spectrometry signal, formic acid gives worse peaks but preserves signal.
Compare purity within a single laboratory on the same method, never across laboratories.
Identity and purity are orthogonal, and a high purity says almost nothing about whether the peak is actually what you think it is.
Retention time is sequence-specific and method-specific, so comparing your result to a supplier value using a different method is meaningless without method documentation.
To be exact about it, buffer versus acid in the mobile phase changes the ionisation state of basic and acidic residues, shifting retention and selectivity — same vial, potentially different separation.
If you are ranking vendors, specify a method and have all samples tested at the same place.
edited 21 Aug 2026 by s_kalniete — reworded for clarity after a comment
Ask PeptideStack is a static archive. Posting is closed, but the norms are worth stating: answer the question that was asked, show your working, cite the trial or the certificate, and say plainly where the evidence runs out.