Use your antibodies-online credentials, if available.
No Products on your Comparison List.
Your basket is empty.
Find out more
Show all synonyms
Select your origin of interest
Human CD13 Protein expressed in Human Cells - ABIN3216379
Yeager, Ashmun, Williams, Cardellichio, Shapiro, Look, Holmes: Human aminopeptidase N is a receptor for human coronavirus 229E. in Nature 1992
Show all 6 Pubmed References
Crosslinking of CD13 by mAb C or E is required to inhibit adhesion, as monovalent Fab fragments are not sufficient. Thus, C and E antibodies recognize a distinct epitope on CD13, and binding to this epitope interferes with both CD13-mediated cell adhesion and enzymatic activity.
Data indicate the expression of aminopeptidase N (CD13) in small cell lung cancer (SCLC) tumor and suggest pre-therapeutic CD13 analysis for testing as investigational predictive biomarker for patient selection.
CD13 may be a marker for onychofibroblasts within nail matrix onychodermis
This is the first report presenting CD13 and FLI1 as important mediators of resistance to BRAF inhibition with potential as drug targets in BRAF inhibitors refractory melanoma.
CD13 enrichment was correlated with early recurrences, and poor prognosis in patients with hepatocellular carcinoma.
Patients with acute myeloid leukemia developing leukemia-specific acute hypoxic respiratory failure within 15 days had higher CD13 expression by leukemic cells.
Data suggest that CNGRC-GG-D(KLAKLAK)2 peptide actively participates in the downregulation of aminopeptidase N/CD13.
CGRP and IL-4 positively regulated APN/CD13 expression and activity in psoriatic fibroblasts.
this study shows that CD13 significantly contributes to tissue infiltration by monocytic myeloid-derived suppressor cells and monocytes, thereby contributing to the pathogenesis of hepatic inflammation
data reveal a novel role for CD13 in inducing homotypic aggregation in neutrophils, which results in a transmigration deficiency; this mechanism may be relevant to neutrophil micro-aggregation in vivo
CD13 expression is associated with hepatoblastoma invasiveness and could be a novel prognostic marker for hepatoblastoma.
Data indicate that fluorogenic substrates can be successfully used to identify aminopeptidase N and to measure their activity in cell lysates.
Data show that CD13 anntigen and receptor tyrosine kinase-like orphan receptor 2 (ROR2) identify a cardiac lineage precursor pool that is capable of successful engraftment into the porcine heart.
The substrate Angiotensin II, the enzymes aminopeptidases-A, B, M as well as IRAP 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 isoform and partially unraveled the molecular basis of LAP1 regulation.
Genetic ablation of APN expression had no effect on infectability by porcine epidemic diarrhea virus, demonstrating that APN is not essential for porcine epidemic diarrhea virus cell entry.
pAPN is not a functional receptor for porcine epidemic diarrhea virus, but promotes the infection of PEDV through its protease activity.
The C-terminal domain of the S1 domain of porcine epidemic diarrhea virus is bound to swine pAPN.
SPC 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.
Aminoeptidase N is the major for cell entry system of porcine epidemic diarrhea virus infection.
results demonstrate that aminopeptidase N reduces basolateral Na(+)-K(+)-ATPase levels via ANG IV/AGTRIV signaling. This novel pathway may be important in renal adaptation to high salt
we concluded that APN plays a significant role in the regulation of several sperm functions and early embryonic development. In addition, increased APN activity could potentially lead to several adverse consequences related to male fertility.
These studies identified CD13 as a novel negative regulator of mast cell activation in vitro and in vivo.
CD13 negatively regulates TLR4 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 and the neutral amino acid transporter B0AT1
cooperation in APN expression by both cancer cells and nonmalignant stromal cells within the tumor microenvironment promotes angiogenesis, tumor growth, and metastasis
expression of CD13 in normal and pathological human tissues
Data show that the majority of chondrocyte-like cells are of bone marrow origin, whereas CD34(+)/CD13(+) myeloid precursors appear to infiltrate the plaque actively and transdifferentiate into chondrocyte-like cells in the progression of atherosclerosis.
although CD13 is highly expressed on myeloid cells and is a reliable marker of the myeloid lineage of normal and leukemic cells, it is not a critical regulator of hematopoietic development, hemostasis, or myeloid cell function
CD13 expressed in microglia-derived exosomes is active in neuropeptide degradation and could have a distinct effect on local neuropeptide activity in the brain.
Results suggest that CD26 and CD13 play a role in T cell function in tissue-specific autoimmunity in the central nervous system.
In cardiac angiogenesis endothelial CD13/APN is upregulated. It can be targeted specifically with cNGR conjugates. In the heart cNGR binds its endothelial target only in angiogenic areas.
aminopeptidase N has a role in angiogenesis
APN activity is not responsible for betulinic acid-inhibited growth factor-induced angiogenesis in endothelial cells
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.
, alanyl aminopeptidase
, aminopeptidase M
, aminopeptidase N
, microsomal aminopeptidase
, myeloid plasma membrane glycoprotein CD13
, membrane alanine aminiopeptidase
, aminopeptidase n
, aminopeptidase N/CD13
, membrane protein p161
, cluster of differentiation antigen 13 (CD13)
, kidney Zn peptidase
, kidney aminopeptidase M
, leucine arylaminopeptidase 1
, membrane alanine aminopeptidase
, alanyl (membrane) aminopeptidase (aminopeptidase N, aminopeptidase M, microsomal aminopeptidase, CD13, p150)
, aminopeptidase Ey
, alanyl (membrane) aminopeptidase
, alanyl aminopeptidase, membrane L homeolog