| Field | Specification |
|---|---|
| Mfr No | |
| Alternative Names | Aminopeptidase N; AP-N; rAPN; Alanyl aminopeptidase; Aminopeptidase M; AP-M; Kidney Zn peptidase; KZP; Microsomal aminopeptidase; CD13; Anpep |
| Cellular Localization | |
| Clonality | |
| Concentration | |
| Gene ID | |
| Host | |
| Immunogen | E.coli-derived rat CD13/Anpep recombinant protein (Position: Q642-S965). |
| Isotype | |
| Molecular Weight | |
| Product Type | |
| Reactivity | |
| Reconstitution | |
| Target | |
| UniProt # |
Overview
Anti-CD13/Anpep Picoband® Antibody is an antibody for Anpep detection raised in Rabbit (Polyclonal, Rabbit IgG), with reported reactivity: Human,Mouse,Rat. Commonly used in WB, IHC, IF, Flow Cytometry, ELISA workflows.
Key elements and design rationale
- Target: Anpep (alanyl aminopeptidase, membrane); UniProt: P15684; NCBI Gene: 81641
- Antibody format: Rabbit, Polyclonal, Rabbit IgG
- Molecular weight: 150 kDa
- Applications: WB, IHC, IF, Flow Cytometry, ELISA
Vendor description (summary): Boster Bio Anti-CD13/Anpep Picoband® Antibody catalog # A02591-3.
Biological background
Biological context: Broad specificity aminopeptidase which plays a role in the final digestion of peptides generated from hydrolysis of proteins by gastric and pancreatic proteases. Also involved in the processing of various peptides including peptide hormones, such as angiotensin III and IV, neuropeptides, and chemokines. May also be involved the cleavage of peptides bound to major histocompatibility complex class II molecules of antigen presenting cells. May have a role in angiogenesis and promote cholesterol crystallization. May have a role in amino acid transport by acting as binding partner of amino acid transporter SLC6A19 and regulating its activity.
Expression and localization notes: cellular localization: Cell membrane. Single-pass type II membrane protein., tissue context: Expressed in epithelial cells of the kidney, intestine, and respiratory tract; granulocytes, monocytes, fibroblasts, endothelial cells, cerebral pericytes at the blood-brain barrier, synaptic membranes of cells in the CNS. Also expressed in endometrial stromal cells, but not in the endometrial glandular cells. Found in the vasculature of tissues that undergo angiogenesis and in malignant gliomas and lymph node metastases from multiple tumor types but not in blood vessels of normal tissues. A soluble form has been found in plasma. It is found to be elevated in plasma and effusions of cancer patients..
Common research applications
- Western blotting (WB): Compare Anpep levels across samples and conditions using appropriate loading and biological controls.
- Immunohistochemistry (IHC): Evaluate spatial distribution of Anpep in tissue sections, considering fixation and antigen retrieval effects.
- Immunofluorescence / ICC: Assess subcellular localization patterns and co-localization with compartment markers in cultured cells.
- Flow cytometry: Quantify Anpep-positive populations in single-cell suspensions with appropriate gating and controls.
- ELISA: Use antibody-based detection formats to assess antigen presence or binding in plate-based assays.
Notes for experimental interpretation
- Account for isoforms, post-translational modifications, and sample-specific processing that can shift apparent molecular weight or epitope accessibility.
- Use positive/negative biological controls where possible (e.g., known-expressing cells/tissues, knockdown/knockout models) and include appropriate secondary-only/isotype controls for imaging workflows.
Additional product notes (from provided fields)
- Specificity: No cross reactivity with other proteins.
- Background: Membrane alanyl aminopeptidase (EC 3.4.11.2) also known as alanyl aminopeptidase (AAP) or aminopeptidase N (AP-N) is an enzyme that in humans is encoded by the ANPEP gene. It is mapped to 1q31. 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.
- Cross reactivity: No cross-reactivity with other proteins.
- Cellular localization: Cell membrane. Single-pass type II membrane protein.
- Tissue details: Expressed in epithelial cells of the kidney, intestine, and respiratory tract; granulocytes, monocytes, fibroblasts, endothelial cells, cerebral pericytes at the blood-brain barrier, synaptic membranes of cells in the CNS. Also expressed in endometrial stromal cells, but not in the endometrial glandular cells. Found in the vasculature of tissues that undergo angiogenesis and in malignant gliomas and lymph node metastases from multiple tumor types but not in blood vessels of normal tissues. A soluble form has been found in plasma. It is found to be elevated in plasma and effusions of cancer patients.
- Research category: Adaptive Immunity,Autoimmune,B Cells,Cell Type Markers,Cytokines,Immune System Diseases,Immunology,Innate Immunity,T Cells,TNF Superfamily
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