Human CHD1L Alexa Fluor™ Plus 405‑conjugated Antibody

CHD-1L (Chromohelicase/ATPase DNA-binding protein 1-Like; also ALC-1) is a 98-118 kDa member of the SNF2/RAD54 helicase family of proteins. It is expressed in hepatocytes, possesses ATPase activity, and likely promotes chromatin remodeling at sites of DNA damage. It also is considered an oncogene. CHD-1L upregulates ARHGEF9 trabscription, an action that promotes Cdc42 activity with accompanying filopodia formation and EMT. It also binds apoptosis-mediating Nur77, blocking its migration from nucleus-to-mitochondria. Human CHD-1L is 897 amino acids (aa) in length. It contains a helicase ATP-binding domain (aa 58-223), a C-terminal helicase domain (aa 351-513), a coiled-coil region (aa 38-675) and one Macro domain that binds poly-ADP-ribose and targets DNA damage sites (aa 704-897). There are at least two Ser/Thr phosphorylation sites. There are multiple potential splice variants. One isoform contains an alternative start site at Met114, a second isoform possesses a deletion of aa 43-246, a third isoform shows a three aa substitution for aa 363-897, and a fourth isoform combines a 16 aa insertion after Arg386 with a five aa substitution for aa 425-897. Over aa 759-879, human CHD-1L shares 94% aa identity with mouse CHD-1L.