Human Aminopeptidase N/CD13 Antibody Summary
Lys69-Lys967
Accession # P15144
Applications
Please Note: Optimal dilutions should be determined by each laboratory for each application. General Protocols are available in the Technical Information section on our website.
Scientific Data
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Detection of Human Aminopeptidase N/CD13 by Western Blot. Western blot shows lysates of human kidney tissue and human prostate tissue. PVDF membrane was probed with 0.5 µg/mL of Sheep Anti-Human Aminopeptidase N/CD13 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF3815) followed by HRP-conjugated Anti-Sheep IgG Secondary Antibody (Catalog # HAF016). 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.
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Detection of Aminopeptidase N/CD13 in U937 Human Cell Line by Flow Cytometry. U937 human histiocytic lymphoma cell line was stained with Sheep Anti-Human Aminopeptidase N/CD13 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF3815, filled histogram) or isotype control antibody (Catalog # 5-001-A, open histogram), followed by APC-conjugated Anti-Sheep IgG Secondary Antibody (Catalog # F0127). View our protocol for Staining Membrane-associated Proteins.
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Aminopeptidase N/CD13 in Human Kidney. Aminopeptidase N/CD13 was detected in immersion fixed paraffin-embedded sections of human kidney using Sheep Anti-Human Aminopeptidase N/CD13 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF3815) at 0.3 µg/mL overnight at 4 °C. Tissue was stained using the Anti-Sheep HRP-DAB Cell & Tissue Staining Kit (brown; Catalog # CTS019) and counterstained with hematoxylin (blue). Specific staining was localized to convoluted tubules. View our protocol for Chromogenic IHC Staining of Paraffin-embedded Tissue Sections.
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Detection of Human Aminopeptidase N/CD13 by Simple WesternTM. Simple Western lane view shows lysates of human small intestine tissue and human prostate tissue, loaded at 0.5 mg/mL. A specific band was detected for Aminopeptidase N/CD13 at approximately 177-198 kDa (as indicated) using 10 µg/mL of Sheep Anti-Human Aminopeptidase N/CD13 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF3815) followed by 1:50 dilution of HRP-conjugated Anti-Sheep IgG Secondary Antibody (Catalog # HAF016). This experiment was conducted under reducing conditions and using the 12-230 kDa separation system.
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Western Blot Shows Human Aminopeptidase N/CD13 Specificity by Using Knockout Cell Line. Western blot shows lysates of U937 human histiocytic lymphoma cell line and human APN knockout U937 human histiocytic lymphoma cell line (KO). PVDF membrane was probed with 0.5 µg/mL of Sheep Anti-Human Aminopeptidase N/CD13 Antigen Affinity-purified Polyclonal Antibody (Catalog # AF3815) followed by HRP-conjugated Anti-Sheep IgG Secondary Antibody (HAF016). A specific band was detected for Aminopeptidase N/CD13 at approximately 150 kDa (as indicated) in the parental U937 human histiocytic lymphoma cell line, but is not detectable in knockout U937 human histiocytic lymphoma cell line. GAPDH (AF5718) is shown as a loading control. This experiment was conducted under reducing conditions and using Western Blot Buffer Group 1.
Reconstitution Calculator
Preparation and Storage
- 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 human 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 human 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 (3).
- Olsen, J. et al. (1988) FEBS Lett. 238:307.
- Look, A.T. et al. (1989) J. Clin. Invest. 83:1299.
- Turner, A.J. (2004) in Handbook of Proteolytic Enzymes (ed. Barrett, et al.) pp. 289, Academic Press, San Diego.
Product Datasheets
Citations for Human Aminopeptidase N/CD13 Antibody
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
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Citations: Showing 1 - 5
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Characterization of CCoV-HuPn-2018 spike protein-mediated viral entry
Authors: Yongmei Liu, Danying Chen, Yuanyuan Wang, Xinglin Li, Yaruo Qiu, Mei Zheng et al.
J Virol
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Cell-surface tethered promiscuous biotinylators enable comparative small-scale surface proteomic analysis of human extracellular vesicles and cells
Authors: Lisa L Kirkemo, Susanna K Elledge, Jiuling Yang, James R Byrnes, Jeff E Glasgow, Robert Blelloch et al.
eLife
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TMPRSS2 activates the human coronavirus 229E for cathepsin-independent host cell entry and is expressed in viral target cells in the respiratory epithelium.
Authors: Bertram S, Dijkman R, Habjan M, Heurich A, Gierer S, Glowacka I, Welsch K, Winkler M, Schneider H, Hofmann-Winkler H, Thiel V, Pohlmann S
J Virol, 2013-03-27;87(11):6150-60.
Species: Human
Sample Types: Whole Cells, Whole Tissue
Applications: IHC, IHC-Fr -
Isolation and characterization of current human coronavirus strains in primary human epithelial cell cultures reveal differences in target cell tropism.
Authors: Dijkman R, Jebbink M, Koekkoek S, Deijs M, Jonsdottir H, Molenkamp R, Ieven M, Goossens H, Thiel V, van der Hoek L
J Virol, 2013-02-20;87(11):6081-90.
Species: Human
Sample Types: Whole Tissue
Applications: IHC -
Comparative site-specific N-glycoproteome analysis reveals aberrant N-glycosylation and gives insights into mannose-6-phosphate pathway in cancer
Authors: Minyong Chen, Diego M. Assis, Matthieu Benet, Colleen M. McClung, Elizabeth A. Gordon, Shourjo Ghose et al.
Communications Biology
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