GLP-2 is secreted as a 33-amino acid peptide, but is rapidly degraded at an N-terminus site to GLP-2(3-33) in circulation, in large part, by dipeptidylpeptidase IV (DPPIV). GLP-2 (3-33) acts as a partial agonist with potential competitive antagonistic properties on the GLP-2 receptor. In the GLP-2 receptor-binding assay, the binding IC50 for GLP-2 1–33 was 3.1 nM, and it was 41 nM for GLP-2 3-33. Thus, GLP-2 3–33 had 7.5% binding affinity compared to GLP-2 1-33.