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Aminopeptidase N, also known as cluster of differentiation 13 (CD13), is a zinc-dependent and membrane-bound ectopeptidase and type II membrane glycoprotein encoded by ANPEP in humans.1,2 It is composed of a short N-terminal cytosolic domain, a membrane-spanning domain, and five extracellular domains, including a C-terminal catalytic domain.2,3 It is ubiquitously expressed on cell membranes where it functions as a dimer to degrade peptides and proteins containing N-terminal neutral amino acids.2 Plasma levels of soluble aminopeptidase N are increased and positively correlated with tumor progression in patients with non-small cell lung cancer (NSCLC).1 ANPEP is overexpressed in psoriatic skin lesions, synovial fibroblasts isolated from patients with rheumatoid arthritis, and lymphocytes and peripheral blood mononuclear cells (PBMCs) isolated from patients with multiple sclerosis during acute exacerbation and chronic progression.2 Cayman’s Aminopeptidase N/CD13 (C-Term) Rabbit Monoclonal Antibody (RM403) can be used for immunohistochemistry (IHC) and Western blot (WB) applications.
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1. Aminopeptidase N (CD13) as a target for cancer chemotherapy. Cancer Sci. 102(3), 501-508 (2011).
2. CD13/Aminopeptidase N Is a potential therapeutic target for inflammatory disorders. J. Immunol. 204(1), 3-11 (2020).
3. Structure and function of aminopeptidase N. Adv. Exp. Med. Biol. 477, 25-34 (2000).