C/EBPbeta (LAP) Antibody detects endogenous levels of total C/EBPbeta, the p38 and p36 LAPs, but not the p20 LIP. This antibody does not cross-react with C/EBPalpha, -delta, -gamma, -epsilon or -zeta.
Source / Purification
Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to the amino-terminal sequence 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).