A new set of monoclonal antibodies directed to proline-rich and central regions of p53

Hybrid Hybridomics. 2004 Oct;23(5):287-92. doi: 10.1089/hyb.2004.23.287.

Abstract

The p53 protein can adopt several conformations in cells--"latent," "active," or mutant--depending on cellular stress or mutations of the TP53 gene. Today, only a few antibodies discriminating these conformations are available. We produced three new anti-p53 monoclonal antibodies (MAbs) directed against epitopes of human p53. The H53C1 MAb recognizes an epitope located at the N-terminal part of the central region of p53 and can discriminate mutant from wild-type conformation. The H53C2 and H53C3 MAbs are against different epitopes within the proline-rich region of p53. Moreover, the H53C2 epitope is located in the second negative regulatory domain of p53 between residues 80 and 93. These MAbs can be used as new tools to study and modulate the cellular functions of p53.

MeSH terms

  • Animals
  • Antibodies, Monoclonal / immunology*
  • Antibody Specificity
  • Binding Sites / immunology
  • Epitopes / immunology*
  • Humans
  • Mice
  • Mice, Inbred BALB C
  • Mutation
  • Precipitin Tests
  • Proline / immunology
  • Protein Conformation
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / immunology
  • Tumor Suppressor Protein p53 / analysis*
  • Tumor Suppressor Protein p53 / chemistry
  • Tumor Suppressor Protein p53 / genetics
  • Tumor Suppressor Protein p53 / immunology*

Substances

  • Antibodies, Monoclonal
  • Epitopes
  • Recombinant Proteins
  • Tumor Suppressor Protein p53
  • Proline