Table 1.

Antibodies used in this study

β-catenin, dephospho-specificMouseUpstate Biotechnology, 05-6651:400NY
β-catenin, pan (amino acids 571-781)MouseBD Transduction Laboratories, 6101531:400NY
β-catenin, pan (amino acids 768-781)RabbitSigma, C-22061:2000YN
β-catenin, pan (full length)GoatR&D Systems, AF13291:2000YY
Insulin (C-peptide)Guinea pigLinco, 4021-011:2500YY
GlucagonGuinea pigLinco, 4031-01F1:2500YY
GlucagonRabbitZymed, 18-00641:200YN
AmylaseRabbitSigma, A-82731:500YY
AmylaseSheepAbcam, ab89431:2000YN
Pdx1Guinea pigGift of Chris Wright, Vanderbilt University1:1000YY
Ptf1a/p48RabbitGift of Helena Edlund, University of Umea1:1000YN
BrdURatAbcam, ab63261:2000YY
E-cadherinRatZymed, 13-19001:2000YN
PlakoglobinGoatSanta Cruz, sc-14971:50YN
Cleaved caspase-3RabbitCell Signaling, 96611:100YY
  • Antibodies were used at the indicated dilutions, on frozen and/or paraffin sections. (In all cases, paraffin sections were subjected to high-temperature antigen retrieval — see Materials and methods for details.) Of the three pan-specific β-catenin antibodies used, two (Transduction Laboratories and Sigma) were raised specifically against epitopes outside of the floxed region of Catnblox [amino acid 1-312 (see Brault et al., 2001)]. Neither of these antibodies, nor a polyclonal antiserum against full-lengthβ -catenin (R&D Systems), stained pancreatic epithelial cells following Cre-mediated deletion of Catnblox, confirming the loss of β-catenin expression. In most cases, where antibodies are marked as not being used for frozen or paraffin wax sections (N), they were tested and failed to yield specific staining.

    N, no; Y, yes.