|Detection of Human CDP/CUTL1 by Western Blot. Western blot shows lysates of K562 human chronic myelogenous leukemia cell line. PVDF membrane was probed with 1 µg/mL of Goat Anti-Human CDP/CUTL1 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF4756) followed by HRP-conjugated Anti-Goat IgG Secondary Antibody (Catalog # HAF019). Specific bands were detected for CDP/CUTL1 at approximately 190 kDa and 110 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.|
CDP (CCAAT Displacement Protein; also CUX-1 and CUTL-1) is a 180-190 kDa member of the CUT homeobox family of proteins. It is found in multiple cell types, and appears to act as a negative regulator of transcription for genes as diverse as c-myc, CD8 and TGF-beta RII. Repression is assumed to occur either by direct DNA interaction, which interferes with transcriptional activator binding to gene promoters, or through the recruitment of active HDACs to target gene promoter sequences. Human CDP is 1505 amino acids (aa) in length. It contains three consecutive DNA-binding CUT domains (aa 542-629; 934-1007; 1125-1202) plus one C-terminal homeobox domain (aa 1244-1303). CDP undergoes phosphorylation, resulting in its inactivation, and reportedly also homodimerizes. There are multiple splice variants (termed CASP), ranging from 75-85 kDa in size. Most are characterized by the presence of a unique 260 aa substitution for aa 410-1505 that contains a Golgi transmembrane domain. CDP also undergoes extensive proteolytic processing, creating functional DNA binding C-terminal fragments that range from 75-110 kDa in size. Over aa 64-268, human CDP shares 97% aa identity with mouse CDP.
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