CD13 Antibody (YA4651)
(Synonyms: ANPEP; APN; CD13; PEPN; Aminopeptidase N; AP-N; hAPN; Alanyl aminopeptidase; Aminopeptidase M; AP-M; Microsomal aminopeptidase; Myeloid plasma membrane glycoprotein CD13; gp150; CD13)CD13 Antibody (YA4651) is a non-conjugated antibody, targeting to CD13. Camel, chimeric fusion of Nanobody (VHH) and mouse IgG1 Fc domain , recombinantly produced from 293F cell。
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Host:
Mouse
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Application:
FC, ELISA
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Formulation:
Supplied in Phosphate-buffered solution.
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Conjugation:
Non-conjugated
To place orders, for customer services and technical support, please contact: MedChemExpress USA
Tel: 609-228-6898 E-mail: [email protected] [email protected]
Applications
| Application |
ELISA
ELISA: Enzyme Linked Immunosorbent Assay
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FC
FC: Flow Cytometry
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|---|---|---|
| Dilution Ratio | 1:5000-100000 | 1-2μg/Test |
Product Details
CD13 Antibody (YA4651) is a non-conjugated antibody, targeting to CD13. Camel, chimeric fusion of Nanobody (VHH) and mouse IgG1 Fc domain , recombinantly produced from 293F cell。
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Host Mouse
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Clonality Monoclonal,Recombinant
affinity purified.
Non-conjugated
Unmodified
Product Properties
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Appearance
Solution
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Formulation
Supplied in Phosphate-buffered solution.
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Storage & Stability
Stored at -20°C for 1 year. Avoid repeated freeze / thaw cycles.
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Shipping
Shipping with blue ice.
Background
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Function
CD13/aminopeptidase N (APN) is a widely expressed transmembrane ectoenzyme in endothelial, epithelial, fibroblast, and leukocyte populations[1]. Mechanistically, CD13 regulates cytokine activity by N-terminal cleavage, participates in MHC class II peptide trimming, and also mediates signal transduction, receptor recycling, FcγR-mediated phagocytosis, and cytokine-receptor functions independent of enzymatic activity[2]. In inflammatory models, IFN-γ regulated CD13/APN mRNA, membrane CD13, and enzyme activity in HL-60 myelo-monocytic cells, supporting cytokine-dependent control during inflammation[3]. In cancer research, CD13 is a Zn2+-dependent membrane ectopeptidase associated with growth of different human cancers and evaluated as a target for inhibitors and APN-targeted carrier constructs[4]. Compared with related aminopeptidase isoforms, CD13/APN is specifically framed as a \"moonlighting\" enzyme because its receptor and signaling roles do not always depend on catalytic activity[5]. This distinction is experimentally important because lung cancer cell migration increased even with catalytically inactive CD13, whereas anti-CD13 antibodies reduced migration and invasion[6]. For applications, natural and synthetic APN inhibitors help analyze peptide-response modulation, immune functions, proliferation, secretion, invasion, and angiogenesis[1].
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Subcellular Localization
Cell membrane; Single-pass type II membrane protein
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Expression
Tissue_specificity:This protein is expressed in the epithelial cells, granulocytes, monocytes, fibroblasts, endothelial cells, pericytes at the blood-brain barrier, and synaptic membranes of cells in the kidneys, intestines, and respiratory tract. It is also expressed in endometrial stromal cells but not in endometrial glandular cells. It has been found in the vascular system of angiogenic tissues, as well as in malignant gliomas and lymph node metastases of various tumor types, but not in the blood vessels of normal tissues. A soluble form has been found in plasma. The protein is present at elevated levels in the plasma and exudate of cancerous cells.
Induction:Estradiol and IL8/interleukin-8 decrease enzymatic activity in vitro in endometrial stromal cells by 40% and 30%, respectively -
Subunit
Homodimer. Interacts with SLC6A19 (By similarity)
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SwissProt ID
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Synonyms
ANPEP; APN; CD13; PEPN; Aminopeptidase N; AP-N; hAPN; Alanyl aminopeptidase; Aminopeptidase M; AP-M; Microsomal aminopeptidase; Myeloid plasma membrane glycoprotein CD13; gp150; CD13
Documentation
[1]. Bauvois B, et al. Aminopeptidase-N/CD13 (EC 3.4.11.2) inhibitors: chemistry, biological evaluations, and therapeutic prospects. Med Res Rev. 2006 Jan;26(1):88-130. [Content Brief]
[2]. Lu C, et al. CD13/Aminopeptidase N Is a Potential Therapeutic Target for Inflammatory Disorders. J Immunol. 2020 Jan 1;204(1):3-11. [Content Brief]
[3]. Gabrilovac J, et al. Regulation of aminopeptidase N (EC 3.4.11.2; APN; CD13) by interferon-gamma on the HL-60 cell line. Life Sci. 2005 Apr 22;76(23):2681-97. [Content Brief]
[4]. Wickström M, et al. Aminopeptidase N (CD13) as a target for cancer chemotherapy. Cancer Sci. 2011 Mar;102(3):501-8. [Content Brief]
[5]. Mina-Osorio P. The moonlighting enzyme CD13: old and new functions to target. Trends Mol Med. 2008 Aug;14(8):361-71. doi: 10.1016/j.molmed.2008.06.003. Epub 2008 Jul 5. PMID: 18603472; PMCID: PMC7106361. et al. The moonlighting enzyme CD13: old and new functions to target. Trends Mol Med. 2008 Aug;14(8):361-71. [Content Brief]
[6]. Chang YW, et al. CD13 (aminopeptidase N) can associate with tumor-associated antigen L6 and enhance the motility of human lung cancer cells. Int J Cancer. 2005 Aug 20;116(2):243-52. [Content Brief]
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