S100A9 is a calcium-binding protein of the S100 protein family that partners with S100A8 in calprotectin. The reviewed human reference sequence contains 114 amino acids. Its sequence and interactions distinguish it from S100A8 even though the two proteins can act within one heterodimer.[ref]
A complex contains contributions from both partners. In metal-binding experiments on calprotectin, substitutions in the predicted interfacial sites reduced measurable manganese/zinc binding. Comparing the variant with the ordinary protein complex linked binding to antimicrobial function. Those observations concern a defined molecular preparation, rather than every biological situation in which S100A9 is detected.[ref]
An original counting example makes the measurement limit explicit. A sample containing 100 S100A9 chains might contain 50 one-to-one S100A8/S100A9 heterodimers plus 50 unpaired S100A9 chains, or 100 heterodimers if enough S100A8 is present. Both samples have the same total S100A9 count. An assay detecting that subunit alone cannot distinguish the two stipulated assemblies.
This is why sequence identity, subunit abundance and complex activity should be recorded separately. A change in a protein subunit's measured abundance is not automatically a proportional change in the activity of the assembled calprotectin.

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