Phospho-C/EBPbeta (Thr235) Antibody detects endogenous levels of human LAP only when phosphorylated at Thr235, mouse and rat LAP only when phosphorylated at Thr188, and LIP only when phosphorylated at Thr37. This antibody does not cross-react with other phosphorylated C/EBPs.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding threonine 235 of human C/EBPbeta. Antibodies are purified by protein A and peptide affinity chromatography.
Background
CCAAT/enhancer-binding proteins (C/EBPs) are a family of transcription factors critical for cellular differentiation, terminal functions and inflammatory response (1). Six members of the family have been characterized (C/EBPα, -β, -γ, -δ, -ε and -ζ) and are distributed in a variety of tissues (1). There are two forms of C/EBPβ, the 38 kDa liver activating protein (LAP) and the 20 kDa liver inhibitory protein (LIP) which may be products of alternative translation. The 38 kDa LAP protein is a transcriptional activator while LIP may act as an inhibitor of C/EBPβ transcriptional activity (2). Phosphorylation of C/EBPβ at distinct sites stimulates its transcriptional activity (3-5). Phosphorylation at serine 105 of rat C/EBPβ, a unique site only present in the rat sequence, seems essential for rat C/EBPβ activation (6).