Anti-Zinc Fingers Linker (ZnFL) Antibody from rabbit, purified by affinity chromatography

C2H2 zinc finger (ZNF) proteins (ZFPs) represent the largest family of gene regulators in human. C2H2 ZFPs wrap around DNA via multiple zinc fingers to ensure a stable DNA interaction. Small linker peptides joining adjacent zinc finger modules are critical for the DNA-binding activity of C2H2 ZFPs. The vast majority of linker peptides contain a serine or threonine as their first amino acid residue, phosphorylation of which greatly reduces the DNA binding activity of C2H2 ZFPs. About half of ZFPs contain the highly conserved KRAB repression domain. KRAB family zinc finger proteins (KRAB-ZNF) adopt simple protein architecture where the conserved N-terminal KRAB domain is linked with the sequence-specific DNA-binding domain comprised of tandem arrays of the C2H2 type ZNFs. The KRAB domain directly binds KAP1 and is essential for KRAB-ZNF-mediated gene repression. Upon recruitment to chromatin by KRAB-ZNFs, KAP1 in turn functions as a scaffolding protein for histone- and DNA-modifying enzymes involved in target genes silencing.