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. 2012 May 21;287(27):22789–22798. doi: 10.1074/jbc.M112.378224

FIGURE 1.

FIGURE 1.

A truncated β-catenin species produced by post-translational cleavage of the N-terminal 95 amino acids is produced in developing liver during hepatoblast differentiation. A, an immunoblot analysis reveals a truncation of β-catenin from 97 to ∼75 kDa occurring as liver develops. B, a Northern blot on pooled mRNA from E12.5, E14.5, E16.5, E17.5, and E18.5 livers probed with a radiolabeled, full-length Ctnnb1 probe reveals only one β-catenin transcript at the expected size of ∼3565 bp. C, RT-PCR on cDNA from E14.5, E18.5, and adult using primers against the 5′-UTR and 3′-UTR of the Ctnnb1 transcript livers also indicates the presence of one mRNA species coding for β-catenin. D, immunoblots on liver lysates from E12.5, E14.5, E16.5, E17.5, and E18.5 using antibodies against different β-catenin epitopes shows that that antibodies targeting amino acids 571–781, phospho-Tyr-654, and phospho-Tyr-142 bind to the truncated β-catenin species, but those targeting amino acids 1–18 or 29–49 do not. E, tandem mass spectrometry on truncated β-catenin protein immunoprecipitated from pooled E18.5 liver lysate detected peptides comprising amino acids 96–125, 134–151, 159–170, 190–199, 486–495, 535–541, 550–564, 647–660, and 673–683.