The plasma proteome spans thousands of proteins whose levels are dynamic and vary by orders of magnitude, are diverse in origin, and play a wide range of biological roles.1 This scope and variation present challenges for analysis and quantitation, leaving this rich domain for biomedical discovery relatively underexplored in nephrology research. However, this has begun to change with the advent of various affinity-based proteomic methods. For example, aptamer-based methods use short oligonucleotides that (1) fold into diverse shapes to bind target proteins with high specificity and (2) can be quantified via hybridization to complementary DNA probes on microarrays.