Render Target: STATIC
Render Timestamp: 2024-12-20T11:44:45.488Z
Commit: f2d32940205a64f990b886d724ccee2c9935daff
XML generation date: 2024-08-01 15:28:38.402
Product last modified at: 2024-09-16T20:45:08.478Z
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PDP - Template Name: Polyclonal Antibody
PDP - Template ID: *******59c6464

C/EBPβ Antibody #3082

Filter:
  • WB

    Supporting Data

    REACTIVITY R
    SENSITIVITY Endogenous
    MW (kDa) 38, 41
    SOURCE Rabbit
    Application Key:
    • WB-Western Blotting 
    Species Cross-Reactivity Key:
    • R-Rat 

    Product Information

    Product Usage Information

    Application Dilution
    Western Blotting 1:1000

    Storage

    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.

    Protocol

    Specificity / Sensitivity

    C/EBPbeta Antibody detects endogenous levels of rat C/EBPbeta protein. It does not cross-react with other C/EBP family members such as C/EBPalpha, -delta, -gamma, -epsilon or -zeta. It also does not recognize the p20 LIP rat C/EBPbeta isoform.

    Species Reactivity:

    Rat

    Source / Purification

    Polyclonal antibodies are produced by immunizing animals with a synthetic peptide corresponding to residues surrounding Ser105 of rat 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).
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