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Phospho-C/EBPbeta (Ser105) Antibody (Rat Specific)
Primary Antibodies

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

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Citations (1)

Supporting Data

MW (kDa) 41

Application Key:

  • W-Western
  • IP-Immunoprecipitation
  • IHC-Immunohistochemistry
  • ChIP-Chromatin Immunoprecipitation
  • IF-Immunofluorescence
  • F-Flow Cytometry
  • E-P-ELISA-Peptide

Species Cross-Reactivity Key:

  • H-Human
  • M-Mouse
  • R-Rat
  • Hm-Hamster
  • Mk-Monkey
  • Mi-Mink
  • C-Chicken
  • Dm-D. melanogaster
  • X-Xenopus
  • Z-Zebrafish
  • B-Bovine
  • Dg-Dog
  • Pg-Pig
  • Sc-S. cerevisiae
  • Ce-C. elegans
  • Hr-Horse
  • All-All Species Expected


Supplied in 10 mM sodium HEPES (pH 7.5), 150 mM NaCl, 100 µg/ml BSA and 50% glycerol. Store at –20°C. Do not aliquot the antibody.

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 animals with a synthetic phosphopeptide corresponding to residues surrounding Ser105 of rat C/EBPbeta. Antibodies are purified by protein A and peptide affinity chromatography.


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).

  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.

Pathways & Proteins

Explore pathways + proteins related to this product.

For Research Use Only. Not For Use In Diagnostic Procedures.

Cell Signaling Technology is a trademark of Cell Signaling Technology, Inc.

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