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. As a member of the krueppel C2H2-type zinc-finger protein family, ZNF74 (Zinc finger protein 74) is a 643 amino acid nuclear protein that contains one KRAB domain and twelve C2H2-type zinc fingers. These internal features enable ZNF74 to bind tightly to the nuclear matrix and be involved in protein-protein interactions. Mapping to chromosome 22, the gene encoding ZNF74 is found to be consistently deleted in DiGeorge syndrome, a disease characterized by congenital heart defects, recurrent infections, palate abnormalities and learning disabilities. There are four isoforms of ZNF74 that are produced as a result of alternative splicing events.
Key Feature
Clonality
Polyclonal
Isotype
IgG
Host Species
Rabbit
Tested Applications
WBIPIFELISA
recommended for detection of ZNF74 of human origin by WB, IP, IF and ELISA non cross-reactive with other ZNF family members
Species Reactivity
HumanMouseRat
Concentration
1mg/ml
Purification
Affinity purified
Target Information
Alternative Names
epitope mapping at the C-terminus of ZNF74 of human origin
Tissue Specificity
epitope mapping at the C-terminus of ZNF74 of human origin