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Rabbit polyclonal antibodies were raised against a proline rich, peptide sequence, comprising 13 amino acids, in the cytoplasmic domain of the CD3 epsilon chain. Immunoprecipitation experiments showed that this antibody preparation recognised the CD3 antigen on human T lymphoblasts. The antibody stained normal T cells strongly in tissue sections which had been fixed in formalin or Bouin's solution and embedded in paraffin wax. Its reactivity with T cell lymphoma, when evaluated on a series of 96 previously phenotyped cases, closely agreed with the results obtained on cryostat sections. These results indicate that the specific detection of T cells in routinely processed tissue biopsy specimens is now technically feasible on a wide scale in diagnostic laboratories using CD3 peptide antibodies, and they also suggest that in future the use of anti-peptide antibodies may detect other lineage specific antigenic markers in paraffin wax sections.

Original publication




Journal article


J Clin Pathol

Publication Date





1194 - 1200


Amino Acid Sequence, Antibodies, Antigens, Differentiation, T-Lymphocyte, Biomarkers, Tumor, CD3 Complex, Humans, Immunoenzyme Techniques, Lymphoma, Membrane Glycoproteins, Molecular Sequence Data, Paraffin, Peptide Fragments, Precipitin Tests, Receptors, Antigen, T-Cell, T-Lymphocytes, Tissue Preservation, Waxes