The invention relates to an isolated peptide of 12-20 amino acids in length comprising the amino acid sequence SEQ ID NO: 1, said peptide being characterised in that it contains a single phosphorylation on the serine residue at position 8 of SEQ ID NO:1. The invention further relates to a human monophosphorylated alpha-enolase isoform containing a single phosphorylation on the serine residue at position 419 of the human alpha-enolase amino acid sequence (SEQ ID NO:2) and optionally other post-translational modifications, as well as antibodies capable of specifically binding the peptide and/or the isoform of the invention. The peptide, the isoform and the antibodies of the invention are useful in the diagnosis and/or treatment of pancreatic adenocarcinoma.

AN ISOLATED MONOPHOSPHORYLATED PEPTIDE DERIVED FROM HUMAN ALPHA-ENOLASE USEFUL FOR DIAGNOSIS AND TREATMENT OF PANCREATIC ADENOCARCINOMA, ANTIBODIES DIRECTED AGAINST THE SAID MONOPHOSPHORYLATED PEPTIDE, AND USES THEREOF

NOVELLI, Francesco;TOMAINO, BARBARA;CAPPELLO, Paola
2011-01-01

Abstract

The invention relates to an isolated peptide of 12-20 amino acids in length comprising the amino acid sequence SEQ ID NO: 1, said peptide being characterised in that it contains a single phosphorylation on the serine residue at position 8 of SEQ ID NO:1. The invention further relates to a human monophosphorylated alpha-enolase isoform containing a single phosphorylation on the serine residue at position 419 of the human alpha-enolase amino acid sequence (SEQ ID NO:2) and optionally other post-translational modifications, as well as antibodies capable of specifically binding the peptide and/or the isoform of the invention. The peptide, the isoform and the antibodies of the invention are useful in the diagnosis and/or treatment of pancreatic adenocarcinoma.
2011
WO/2011/030302
F. Novelli, Natimab srl
Pancreatic Cancer; Diagnosis; alpha-enolase; autoantibodies
F. Novelli; B. Tomaino; P. Cappello
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/2318/84615
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