Human CEBP  alpha Alexa Fluor™ Plus 488-conjugated Antibody

CEBP alpha (CCAAT/Enhancer-Binding Protein; also C/EBP) is a 42-43 kDa member of the C/EBP subfamily, bZIP family of proteins. It is expressed in multiple cell types, particularly those that are fully differentiated, and includes hepatocytes, skeletal muscle cells, adipocytes, intestinal epithelium and proliferating macrophages. CEBP alpha acts as a transcriptional activator for a large and diverse number of genes, including glycogen synthase, GLUT4, and G-CSFR, and participates in both cell cycle progression and differentiation. Human CEBP alpha is 358 amino acids (aa) in length). It contains one transactivation domain (aa 1-96), poly-Gly segment (aa 99-104), a poly-Pro motif (aa 183-189), a bZIP dimerization region (aa 281-334), and an overlapping DNA-binding Leu-zipper domain (aa 317-345). CEBP alpha forms both homodimers, and heterodimers with other subfamily members. One alternative start site at Met120 generates a low activity 30-32 kDa isoform variant. There is also a utilized phosphorylation site at Ser21 that regulates activity. Over aa 1-124, human CEBP alpha shares 93% aa identity with mouse CEBP alpha.