Chromatin assembly factor 1 (CAF1) is the only histone chaperone known to assemble histones H3 and H4 onto newly synthesized DNA both in vitro and in vivo . The 938 amino acid multidomain p150 (CHAF1A) binds via its C-terminal third to p60, which is an essential step for nucleosome assembly because knocking down either subunit disrupts the activity . In addition, CAF1 facilitates DNA synthesis depending on the binding of the N-terminal 31 residues of p150 to the proliferating cell nuclear antigen (PCNA), which acts as a sliding clamp to stimulate the processivity of DNA polymerase . CHAF1A regulates the formation of heterochromatin in mammalian cells during replication and in plants it maintains the transcription of certain subsets of genes. Furthermore, CHAF1A exists in a chromatin-remodeling complex WINAC, which coactivates ligand-induced transactivation function of the vitamin D receptor .
Western Blot:Jurkat Cells, 1:500-1:5000; IHC: Human cervix Tissue, 1:20-1:200
Type: Primary
Antigen: CHAF1A
Clonality: Polyclonal
Clone: 0
Conjugation: Unconjugated
Epitope:
Host: Rabbit
Isotype: IgG
Reactivity: