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Aminopeptidase N is located in the small-intestinal and renal microvillar membrane, and also in other plasma membranes. Additionally we are shipping CD13 Kits (22) and CD13 Proteins (13) and many more products for this protein.
Showing 10 out of 542 products:
Mouse (Murine) Monoclonal CD13 Primary Antibody for FACS - ABIN320066
Curnis, Gasparri, Sacchi, Cattaneo, Magni, Corti: Targeted delivery of IFNgamma to tumor vessels uncouples antitumor from counterregulatory mechanisms. in Cancer research 2005
Show all 11 references for ABIN320066
Human Monoclonal CD13 Primary Antibody for EIA, FACS - ABIN118525
Bradstock, Favaloro, Kabral, Kerr, Hughes, Musgrove: Myeloid progenitor surface antigen identified by monoclonal antibody. in British journal of haematology 1985
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Human Monoclonal CD13 Primary Antibody for FACS - ABIN118523
Favaloro, Bradstock, Kabral, Grimsley, Zowtyj, Zola et al.: Further characterization of human myeloid antigens (gp160,95; gp150; gp67): investigation of epitopic heterogeneity and non-haemopoietic distribution using panels of monoclonal antibodies belonging ... in British journal of haematology 1988
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Human Polyclonal CD13 Primary Antibody for WB - ABIN391875
Watt, Willard: The human aminopeptidase N gene: isolation, chromosome localization, and DNA polymorphism analysis. in Human genetics 1990
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Human Monoclonal CD13 Primary Antibody for IHC (p) - ABIN180516
Bonde, Meyer, Broe, Hokland, Turley, Hokland: Improved flow cytometric identification of myelopoiesis by the simultaneous labelling with CD13, CD14 and CD66 monoclonal antibodies. in British journal of haematology 1996
Show all 2 references for ABIN180516
Human Monoclonal CD13 Primary Antibody for FACS - ABIN319681
Bradstock, Favaloro, Kabral, Kerr, Hughes, Berndt, Musgrove: Human myeloid differentiation antigens identified by monoclonal antibodies: expression on leukemic cells. in Pathology 1986
Human Monoclonal CD13 Primary Antibody for FACS - ABIN1105839
Brok, Hornby, Griffiths, Scott, Hart: An extensive monoclonal antibody panel for the phenotyping of leukocyte subsets in the common marmoset and the cotton-top tamarin. in Cytometry 2001
Mouse (Murine) Monoclonal CD13 Primary Antibody for FACS, IP - ABIN1449277
Hayami, Sato, Wu, Nishikawa, Hiroi, Ohtani-Kaneko, Fukuda, Ohta: Down-regulation of BRCA1-BARD1 ubiquitin ligase by CDK2. in Cancer research 2005
Human Monoclonal CD13 Primary Antibody for FACS - ABIN1105840
Vermot-Desroches, Marchand, Roy, Wijdenes: Heterogeneity of antigen expression among human umbilical cord vascular endothelial cells: identification of cell subsets by co-expression of haemopoietic antigens. in Immunology letters 1996
The substrate Angiotensin II, the enzymes aminopeptidases-A, B, M as well as IRAP (show IL1RN Antibodies) were detected in the jejunal mucosa.
14-3-3epsilon might directly bind to CD13, which transmits its signal in chondrocytes to induce a catabolic phenotype similar to that observed in osteoarthritis.
Alanyl aminopeptidase expression is confined to mature zymogenic chief cells and its expression is lost en route to metaplasia.
Aminopeptidase N activity in tissue and plasma from colorectal cancer patients is an independent prognostic factor of 5-year survival.
Expression of APN/CD13 is a potential unfavorable factor to predict the efficacy and prognosis of post-operative chemotherapy in NSCLC patients, especially in lung adenocarcinoma patients.
We identified a unique HCC line, Li-7, which not only shows heterogeneity for a CD13(+) CSC hierarchy, but also undergoes a "population change" upon CSC differentiation
This study permitted the identification of the novel human LAP1C (show TOR1AIP1 Antibodies) isoform and partially unraveled the molecular basis of LAP1 regulation.
Together these experiments reveal potential enzymatic and signalling roles for APN in osteosarcoma and establish a starting point for an in-depth analysis of the role of APN in regulating invasiveness.
Postulate that the interaction of ADAM17 (show ADAM17 Antibodies) with CD13 and its downregulation following CD13 engagement has important implications in acute myeloid leukemia (show BCL11A Antibodies) cells.
CD13 could play an important role as a T cell chemoattractant, in a positive feedback loop that contributes to rheumatoid arthritis synovitis.
CD13 negatively regulates TLR4 (show TLR4 Antibodies) signaling, thereby balancing the innate response by maintaining the inflammatory equilibrium critical to innate immune regulation.
The impact of loss of CD13 on a model of ischemic skeletal muscle injury, was investigated.
Molecular mechanisms regulating CD13-mediated adhesion.
CD13 is essential for proper trafficking of the inflammatory cells necessary to prime and sustain the reparative response, thus promoting optimal post-infarction healing.
Tyrosine phosphorylation of CD13 regulates inflammatory cell-cell adhesion and monocyte trafficking.
This indicates that Anpep plays a critical role in the proteolytic remodelling of mammary tissue during adult mammary development.
the presence of digestive protein complexes in the intestinal brush-border containing the peptidases APN and ACE2 (show ACE2 Antibodies) and the neutral amino acid transporter B0AT1 (show SLC6A19 Antibodies)
cooperation in APN expression by both cancer cells and nonmalignant stromal cells within the tumor microenvironment promotes angiogenesis, tumor growth, and metastasis
APN activity is not responsible for betulinic acid-inhibited growth factor-induced angiogenesis in endothelial cells
SPC (show SFTPC Antibodies) subdomain of APN plays a key role in cell entry of PEDV and its expression permits PEDV growth
Porcine epidemic diarrhea virus recognizes protein receptor aminopeptidase N from pig and human and sugar coreceptor N-acetylneuraminic acid.
These data demonstrate that pAPN, the cellular receptor for porcine epidemic diarrhea virus, mediates polarized virus infection.
It was concluded that the difference in F4 binding to ANPEP is due to modifications in its carbohydrate moieties.
The region aa 673-722 of the C subunit of porcine aminopeptidase N is indicated to play a key role in swine transmissible gastroenteritis virus binding.
The binding ability of four truncated porcine aminopeptidase N proteins to transmissible gastroenteritis virus (TGEV), a porcine coronavirus, was analyzed by ELISA and immunoblotting.
results demonstrate that aminopeptidase N reduces basolateral Na(+)-K(+)-ATPase (show ATP1A1 Antibodies) levels via ANG (show ANG Antibodies) IV/AGTRIV signaling. This novel pathway may be important in renal adaptation to high salt
Aminopeptidase N is located in the small-intestinal and renal microvillar membrane, and also in other plasma membranes. In the small intestine aminopeptidase N plays a role in the final digestion of peptides generated from hydrolysis of proteins by gastric and pancreatic proteases. Its function in proximal tubular epithelial cells and other cell types is less clear. The large extracellular carboxyterminal domain contains a pentapeptide consensus sequence characteristic of members of the zinc-binding metalloproteinase superfamily. Sequence comparisons with known enzymes of this class showed that CD13 and aminopeptidase N are identical. The latter enzyme was thought to be involved in the metabolism of regulatory peptides by diverse cell types, including small intestinal and renal tubular epithelial cells, macrophages, granulocytes, and synaptic membranes from the CNS. Human aminopeptidase N is a receptor for one strain of human coronavirus that is an important cause of upper respiratory tract infections. Defects in this gene appear to be a cause of various types of leukemia or lymphoma.
, aminopeptidase n
, alanyl aminopeptidase
, aminopeptidase M
, microsomal aminopeptidase
, myeloid plasma membrane glycoprotein CD13
, aminopeptidase N/CD13
, membrane protein p161
, alanyl (membrane) aminopeptidase (aminopeptidase N, aminopeptidase M, microsomal aminopeptidase, CD13, p150)
, cluster of differentiation antigen 13 (CD13)
, kidney Zn peptidase
, kidney aminopeptidase M
, leucine arylaminopeptidase 1
, membrane alanine aminopeptidase
, membrane alanine aminiopeptidase
, aminopeptidase Ey