|Phospho-C/EBPα (Ser21) Antibody 2841||20 µl||
|Phospho-C/EBPα (Thr222/226) Antibody 2844||20 µl||
||H M||30, 42, 45||Rabbit|
|C/EBPα (D56F10) XP® Rabbit mAb 8178||20 µl||
||H M||42, 28||Rabbit IgG|
|Phospho-C/EBPβ (Thr235) Antibody 3084||20 µl||
||H M||19 LIP. 36 LAP. 38 LAP.||Rabbit|
|C/EBPβ (LAP) Antibody 3087||20 µl||
||H M||35 to 38 mouse LAP. 45 to 49 human LAP.||Rabbit|
|C/EBPδ Antibody 2318||20 µl||
|CHOP (D46F1) Rabbit mAb 5554||20 µl||
|Anti-rabbit IgG, HRP-linked Antibody 7074||100 µl||
Polyclonal antibodies are produced by immunizing animals with a synthetic phosphopeptide corresponding to residues surrounding Ser21 of human C/EBPα, Thr222/226 of mouse C/EBPα, or Thr235 of human C/EBPβ. Polyclonal antibodies are also produced by immunizing animals with a synthetic peptide corresponding to the amino-terminal sequence of human C/EBPβ or the sequence of mouse C/EBPδ. Polyclonal antibodies are purified by protein A and peptide affinity chromatography. Monoclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Ala176 of human C/EBPα protein or to residues surrounding Leu159 of human CHOP protein.
CCAAT/enhancer-binding proteins (C/EBPs) are transcription factors critical for cellular differentiation, terminal function, and inflammatory response. Six characterized family members (C/EBPα, β, δ, γ, ε, and ζ) are distributed in a variety of tissues (1). Translation from alternative start codons results in two C/EBPα isoforms (p42 and p30) that are strong transcriptional activators (2). Research studies indicate that insulin and insulin-like growth factor-I stimulate C/EBPα dephosphorylation, which may play a key role in insulin-induced repression of GLUT4 transcription (3). Phosphorylation of C/EBPα at Thr222, Thr226, and Ser230 by GSK-3 may be required for adipogenesis (4). The two forms of C/EBPβ, 38 kDa liver activating protein (LAP) and the 20 kDa liver inhibitory protein (LIP), may result from alternative translation. The 38 kDa LAP protein is a transcriptional activator while LIP may inhibit C/EBPβ transcriptional activity (5). Phosphorylation of C/EBPβ at distinct sites stimulates its transcriptional activity (6-8). Phosphorylation at the rat-specific site Ser105 in C/EBPβ appears essential for C/EBPβ activation in rat (9). C/EBPδ protein is highly expressed in adipose tissue, lung, and intestine (10). Increased expression of C/EBPδ mRNA levels during adipogenesis suggests that C/EBPδ plays an important role in positively regulating adipogenesis (10,11). C/EBPδ is expressed in the mammalian nervous system and plays an important role in long-term memory (10,12). CHOP is a C/EBP-homologous protein that inhibits C/EBP and LAP in a dominant-negative manner (13). CHOP expression is induced by cellular stresses, including starvation; induced CHOP suppresses cell cycle progression from G1 to S phase (14). During ER stress, the level of CHOP expression is elevated and CHOP functions to mediate programmed cell death (15).
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