S100A8 is a calcium-binding protein of the S100 protein family. It is one of the two different protein subunits of calprotectin, together with S100A9. The reviewed human reference sequence contains 93 amino acids; a gene symbol, the encoded protein and an assembled protein complex are related but different objects.[ref]
The distinction is useful when interpreting an assay. Suppose a stipulated preparation contains S100A8 chains and S100A9 chains. If only one-to-one heterodimers form, their concentration cannot exceed . Even at complete use of S100A9, S100A8 would remain outside those heterodimers. Measuring the amount of one subunit therefore does not by itself measure assembled calprotectin.
In a primary metal-binding study, changing binding-site residues contributed by both subunits impaired manganese/zinc binding and antimicrobial activity of the complex. Binding was measured with isothermal titration calorimetry and compared with functional assays. The experiment tests the assembled system; it does not establish that isolated S100A8 has every activity of calprotectin.[ref]
Nutrient metal sequestration by calprotectin inhibits bacterial superoxide defense, enhancing neutrophil killing of Staphylococcus aureus by Thomas E. Kehl-Fie and others. Figure2 and associated Results, metal-site variant and binding/activity comparisons
S100A8 consequently illustrates two levels of biological description: the properties of a particular polypeptide and the properties produced when that polypeptide assembles with a different partner.
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