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ANPEP Antibody (Center)
Purified Rabbit Polyclonal Antibody (Pab)
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB, E |
|---|---|
| Primary Accession | P15144 |
| Reactivity | Human |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | Rabbit IgG |
| Calculated MW | 109540 Da |
| Antigen Region | 615-641 aa |
| Gene ID | 290 |
|---|---|
| Other Names | Aminopeptidase N, AP-N, hAPN, Alanyl aminopeptidase, Aminopeptidase M, AP-M, Microsomal aminopeptidase, Myeloid plasma membrane glycoprotein CD13, gp150, CD13, ANPEP, APN, CD13, PEPN |
| Target/Specificity | This ANPEP antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 615-641 amino acids from the Central region of human ANPEP. |
| Dilution | WB~~1:1000 |
| Format | Purified polyclonal antibody supplied in PBS with 0.09% (W/V) sodium azide. This antibody is prepared by Saturated Ammonium Sulfate (SAS) precipitation followed by dialysis against PBS. |
| Storage | Maintain refrigerated at 2-8°C for up to 2 weeks. For long term storage store at -20°C in small aliquots to prevent freeze-thaw cycles. |
| Precautions | ANPEP Antibody (Center) is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | ANPEP |
|---|---|
| Synonyms | APN, CD13, PEPN |
| Function | 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 (By similarity). |
| Cellular Location | Cell membrane; Single-pass type II membrane protein. Note=Also found as a soluble form |
| Tissue Location | 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. |
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Provided below are standard protocols that you may find useful for product applications.
Background
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.
References
Watt,V.M., Willard,H.F. Hum. Genet. 85 (6), 651-654 (1990)
O'Connell,P.J., Gerkis,V. J. Biol. Chem. 266 (7), 4593-4597 (1991)
Shapiro,L.H., Ashmun,R.A. J. Biol. Chem. 266 (18), 11999-12007 (1991)
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