A portion of amino acids 50-250 from the human protein was used as the immunogen for the Aminopeptidase-N antibody.
Recognizes an integral membrane glycoprotein of 150kDa, identified as CD13 (also known as aminopeptidase-N). The antibody recognizes an extracellular epitope. The CD13 antigen is present on most cells of myeloid origin including granulocytes, monocytes, mast cells, and GM-progenitor cells. It is also expressed by the majority of AML, CML in myeloid blast crisis, and in a smaller fraction of lymphoid leukemias. CD13 is absent from normal lymphocytes, platelets and erythrocytes. CD13 is also present on fibroblasts, endothelial cells, epithelial cells from renal proximal tubules and intestinal brush border, bone marrow stromal cells, osteoclasts, and cells lining bile duct canaliculi. CD13 is identical to aminopeptidase N (APN), a prominent membrane-bound metalloprotease present on the surface of intestinal brush border and renal tubules. CD13 plays a role in metabolism of biologically active peptides, in phagocytosis, and in bactericidal / tumoricidal activities. It also serves as a receptor for human coronaviruses (HCV). The lineage-restricted pattern of expression of CD13 within the hemopoietic compartment suggests that it may be important in myeloid cell differentiation.
