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C/EBP α regulates gene expression in a variety of tissues including liver, adipose, lung and intestine. C/EBP α uses a bipartite structural motif to bind DNA. Two protein chains dimerize through a set of amphipathic α helices termed the leucine zipper. Highly basic polypeptide regions emerge from the zipper to form a linked set of DNA contact surfaces. C/EBP α appears to function exclusively in terminally-differentiated, growth-arrested cells. Additional family members include C/EBP β, C/EBP γ, C/EBP δ and C/EBP ε, all of which exhibit similar DNA-binding specificities and affinities to C/EBP α. Furthermore, C/EBP β and C/EBP δ readily form heterodimers both with each other as well as with C/EBP α.
C EBP; C/EBP delta; c/EBP epsilon; C/EBPd; C/EBPdelta; C/EBP-delta; C/EBPe; C/EBPepsilon; C/EBP-epsilon; C/EBP-related protein 1; c/EBP-related protein 3; C/EPBe; CCAAT/enhancer binding protein (C/EBP), delta; CCAAT/enhancer binding protein (C/EBP), epsilon; CCAAT/enhancer binding protein , epsilon; CCAAT/enhancer binding protein delta; CCAAT/enhancer binding protein epsilon; CCAAT/enhancer-binding protein delta; CCAAT/enhancer-binding protein epsilon; CEBPD; Cebpe; Celf; CRP1; Crp3; Gm294; NF-IL6-beta; nuclear factor NF-IL6-beta; Transcription factor CELF
100 µL
100 µL
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