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Protein-level stability is insufficient if proteoform-informative peptides disagree, so compare those peptide signals across normalization choices before interpreting RBOHC-associated or RBOHF-associated abundance changes.

Before comparing scaling schemes, the measured molecular species must be specified: total HEPACAM bait, a tagged construct, a processed form, or peptides shared across several proteoforms. Bait normalization can correct unequal recovery, but it cannot by itself distinguish altered binding from altered trafficking, processing, compartment access, or epitope availability. Input-protein scaling addresses a different quantity, while total-capture scaling may obscure a genuine change in the material available within the captured compartment. Missing prey signals are also ambiguous because absence may reflect reduced abundance, relocation, failed capture, or stochastic detection. The publication title supports discussing variant-associated localization and interactome changes, but the supplied metadata do not establish which HEPACAM species or normalization strategy was measured (PMID 42649352). Were the bait-defining peptides unique to a specific HEPACAM proteoform, and was bait recovery quantified independently in each relevant compartment?