A recombinant antibody is an antibody produced from a defined genetic sequence rather than directly from hybridoma or serum-derived material. Recombinant antibodies support greater consistency, long-term reproducibility, and sequence-level control.

Learn more: Advantages of Recombinant Antibodies

Antibody avidity refers to the combined binding strength created when multiple antibody binding sites interact with one or more target molecules. While affinity describes a single interaction, avidity reflects the overall stability of multivalent binding. 

Antibody affinity describes the strength of binding between a single antibody binding site and its target epitope. Higher affinity can support stronger target recognition, but assay performance also depends on specificity, epitope accessibility, matrix behavior, and antibody pairing.

High-throughput surface plasmon resonance, or high-throughput SPR, is a label-free technology used to measure antibody binding kinetics and epitope relationships across many candidates in parallel. It helps researchers compare affinity, off-rate, and epitope diversity earlier in antibody discovery and assay development. 

Epitope binning is a method used to group antibodies based on whether they bind the same, overlapping, or distinct regions of a target protein. It is especially useful for identifying compatible antibody pairs for sandwich ELISA and other paired-antibody assay formats.

Epitope mapping identifies the specific region or amino acid sequence of a target protein that an antibody recognizes. This information can help researchers understand specificity, cross-reactivity risk, and whether an antibody is likely to work in a given assay format. 

Antibody pair selection is the process of identifying two antibodies that can bind the same target at the same time without interfering with each other. Strong antibody pairs are essential for sandwich ELISAs and many biomarker detection workflows.