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. ZFP106 (Zinc finger protein 106), also known as zinc finger protein 474, is a 1883 amino acid human homolog of the mouse Zfp106 protein and is a member of the Krüppel C2H2-type zinc-finger family. Localized to the nucleus, ZFP106 contains two C2H2-type zinc fingers and is thought to be involved in transcriptional regulation.
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIPELISA
recommended for detection of ZFP106 of mouse and human origin by WB, IP and ELISA: