Molecular cloning and expression of a cDNA encoding a human Thioredoxin-like protein

Antonio Miranda-Vizuete, Jan Åke Gustafsson, Giannis Spyrou

Research output: Contribution to journalArticlepeer-review

51 Scopus citations


This report describes the cloning of a human cDNA that encodes a new protein (Txl, Thioredoxin-like) that belongs to the expanding family of thioredoxins based on sequence comparison of the deduced amino acid sequence. This cDNA, with a total length of 1278 bp, consists of 205 bp of 5'-untranslated sequence (including an in frame stop codon), an open reading frame of 870 bp and a 203 bp fragment of 3'-untranslated sequence. The coding sequence predicts a protein of 289 amino acids with two distinct domains: an N-terminal domain of 105 residues homologous to the rest of mammalian thioredoxins containing the conserved active site (CGPC) and a C-terminal domain of 184 residues with no homology with any other protein in the database. Northern blot analysis indicates that the txl probe hybridizes to a 1.3 Kb mRNA and is ubiquitously expressed in human tissues with the highest expression in stomach, testis and bone marrow.

Original languageEnglish (US)
Pages (from-to)284-288
Number of pages5
JournalBiochemical and Biophysical Research Communications
Issue number1
StatePublished - Feb 4 1998

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology


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