Detection of Mouse Aminopeptidase N/CD13 by Western Blot. Western blot shows lysates of mouse kidney tissue and mouse uterus tissue. PVDF membrane was probed with 1 µg/mL of Rat Anti-Mouse Aminopeptidase N/CD13 Monoclonal Antibody (Catalog # MAB2335) followed by HRP-conjugated Anti-Rat IgG Secondary Antibody (Catalog # HAF005). A specific band was detected for Aminopeptidase N/CD13 at approximately 150 kDa (as indicated). This experiment was conducted under reducing conditions and using Immunoblot Buffer Group 1.
Detection of Mouse Aminopeptidase N/CD13 by Simple WesternTM. Simple Western lane view shows lysates of mouse kidney tissue, loaded at 0.2 mg/mL. A specific band was detected for Aminopeptidase N/CD13 at approximately 204 kDa (as indicated) using 10 µg/mL of Rat Anti-Mouse Aminopeptidase N/CD13 Monoclonal Antibody (Catalog # MAB2335) followed by 1:50 dilution of HRP-conjugated Anti-Rat IgG Secondary Antibody (Catalog # HAF005). This experiment was conducted under reducing conditions and using the 12-230 kDa separation system.
Preparation and Storage
Reconstitute at 0.5 mg/mL in sterile PBS.
The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. *Small pack size (SP) is shipped with polar packs. Upon receipt, store it immediately at -20 to -70 °C
Stability & Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
6 months, -20 to -70 °C under sterile conditions after reconstitution.
Background: Aminopeptidase N/CD13
The mouse Anpep gene encodes Aminopeptidase N (APN), which is also known as microsomal aminopeptiase, alanyl aminopeptidase, Aminopeptidase M, CD13, or membrane protein p161 (1‑3). The deduced amino acid sequence of mouse APN consists of a short cytoplasmic tail (residues 2 to 8), a transmembrane region (residue 9 to 32), a Ser/Thr rich region and a zinc metalloprotease domain (residues 69 to 966). Widely expressed in many cells, tissues and species, APN cleaves the N-terminal amino acids from bioactive peptides, leading to their inactivation or degradation. The roles of APN in many fields, such as neuroscience, hematopoeitic cells, immune system, angiogenesis, cancer and viral infection, have been reviewed (4).
Chen, H. et al. (1996) J. Immunol. 157:2593.
Larsen, S.L. et al. (1996) J. Exp. Med. 184:183.
Hansen, A.S. et al. (1993) Eur. J. Immunol. 23:2358.
Turner, A.J. (2004) in Handbook of Proteolytic Enzymes (ed. Barrett, et al.) p. 289 Academic Press, San Diego.
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