The LDL receptor can be described as a chimeric protein.

This enzyme from the proteobacterium Marichromatium gracile is a chimeric protein.

This allows CBD of the chimeric protein to bind to column.

These chimeric proteins are usually made of a modified antibody or antibody fragment, attached to a fragment of a toxin.

In some cases, the transcripts formed by CGs are translated to form chimeric or completely novel proteins.

A large number of transcript variations exist, encoding different isoforms or chimeric proteins.

Unlike duplicate genes, chimeric proteins are immediately distinct from their parental genes, and therefore are more likely to produce entirely new functions.

Because they are independently stable, domains can be "swapped" by genetic engineering between one protein and another to make chimeric proteins.

Protein engineering with homologous recombination develops chimeric proteins by swapping fragments between two parental proteins.

The purpose of creating fusion proteins in drug development is to impart properties from each of the "parent" proteins to the resulting chimeric protein.