Cell Signaling Technology

Product Pathways - Glucose Metabolism

Phospho-C/EBPbeta (Ser105) Antibody (Rat Specific) #3081

Applications Reactivity MW (kDa) Source
W R 41 Rabbit

Applications Key:  W=Western Blotting
Reactivity Key:  R=Rat
Species enclosed in parentheses are predicted to react based on 100% sequence homology. Species cross-reactivity is determined by Western blot.

Specificity / Sensitivity

Phospho-C/EBPbeta (Ser105) Antibody (Rat Specific) detects endogenous levels of rat C/EBPbeta only when phosphorylated at serine 105. It does not cross-react with phosphorylated rat C/EBP family members alpha, delta, gamma, epsilon or zeta. It also does not recognize the p20 LIP rat C/EBPbeta isoform.

Source / Purification

Polyclonal antibodies are produced by immunizing rabbits with a synthetic phospho-peptide (KLH coupled) corresponding to residues surrounding Ser105 of rat C/EBPbeta. Antibodies are purified by protein A and peptide affinity chromatography.

Western Blotting

Western Blotting

Western blot analysis of extracts from untreated or serum stimulated PC12 cells, using Phospho-C/EBPbeta (Ser105) Antibody (Rat Specific) (A, B) or C/EBPbeta Antibody #3082 (C, D). Nitrocellulose membranes B and D were treated with alkaline phosphatase (CIP) to show the phospho-specificity of Phospho-C/EBPbeta (Ser105) Antibody.

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/EBPalpha, -beta, -delta, -gamma, -epsilon and -zeta) and are distributed in a variety of tissues (1). There are two forms of C/EBPbeta, 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/EBPbeta transcriptional activity (2). Phosphorylation of C/EBPbeta at distinct sites stimulates its transcriptional activity (3-5). Phosphorylation at serine 105 of rat C/EBPbeta, a unique site only present in the rat sequence, seems essential for rat C/EBPbeta activation (6).

  1. Lekstrom-Himes, J. and Xanthopoulos, K.G. (1998) J. Biol. Chem. 273, 28545-28548.
  2. Calkhoven, C.F. et al. (2000) Genes Dev. 14, 1920-1932.
  3. Wegner, M. et al. (1992) Science 256, 370-373.
  4. Trautwein, C. et al. (1993) Nature 364, 544-547.
  5. Nakajima, T. et al. (1993) Proc. Natl. Acad. Sci. USA 90, 2207-2211.
  6. Buck, M. et al. (1999) Mol. Cell 4, 1087-1092.

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