Zinc-finger proteins contain DNA-binding domains and have a wide variety of functions, most of which encompass some form of transcriptional activation or repression. The majority of zinc-finger proteins contain a Krüppel-type DNA binding domain and a KRAB domain, which is thought to interact with KAP1, thereby recruiting histone modifying proteins. Belonging to the krueppel C2H2-type zinc-finger protein family, ZFP96 (Zinc finger protein 96 homolog), also known as ZSCAN12 (Zinc finger and SCAN domain-containing protein 12) and Zinc finger protein 305, is a 604 amino acid nuclear protein that contains one SCAN box domain and eleven C2H2-type zinc fingers. ZFP96 is upregulated by eight-fold from day 13 of pregnancy to day 1 post-partum, suggesting that ZFP96 functions as a transcription factor by switching off pro-survival genes and/or upregulating pro-apoptotic genes of the corpus luteum.