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. Zinc finger protein 398 (ZNF398), also known as Zinc finger DNA-binding protein p52/p71 or ZER6, is a 642 amino acid member of the Krüppel C2H2-type zinc-finger protein family. Localized to the nucleus, ZNF627 contains nine C2H2-type zinc fingers and one KRAB domain through which it is thought to be involved in DNA-binding and transcriptional regulation. Existing as two isoforms produced by alternative splicing, ZNF398 is induced by ERå.
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIPELISA
recommended for detection of ZNF398 of human origin by WB, IP and ELISA