CD13 Antibody (YA1253)
(Synonyms: ANPEP; APN; CD13; PEPN; Aminopeptidase N; AP-N; hAPN; Alanyl aminopeptidase; Aminopeptidase M; AP-M; Microsomal aminopeptidase; Myeloid plasma membrane glycoprotein CD13; gp150; CD antigen CD13)Based on 1 Customer Validation
CD13 Antibody (YA1253) is a Rabbit-derived and non-conjugated IgG monoclonal antibody, targeting to CD13.
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Host:
Rabbit
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Isotype:
IgG
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Application:
IHC-P
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Reactivity :
Human
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Formulation:
Supplied in 50mM Tris-Glycine(pH 7.4), 0.15M NaCl, 40%Glycerol, 0.01% sodium azide and 0.05% BSA.
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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 |
IHC-P
IHC-P: Immunohistochemistry-Paraffin
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|---|---|
| Dilution Ratio | 1:100-1:200 |
Product Details
CD13 Antibody (YA1253) is a Rabbit-derived and non-conjugated IgG monoclonal antibody, targeting to CD13.
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Host Rabbit
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Clonality Recombinant,Monoclonal
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Species ReactivityHuman
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Observed Molecular WeightObserved band size: 110 kDa
Note: Due to possible protein modifications or aggregation, the molecular weight should be confirmed by actual measurement, and the predicted value is for reference only.
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Calculated Molecular Weight Predicted band size: 110 kDa
A synthesized peptide derived from human CD13
Endogenous
Affinity Purified
Non-conjugated
Unmodified
IgG
Product Properties
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Appearance
Solution
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Formulation
Supplied in 50mM Tris-Glycine(pH 7.4), 0.15M NaCl, 40%Glycerol, 0.01% sodium azide and 0.05% BSA.
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Concentration
Batch-dependent, Please check the COA for the concentration of each lot. Check Lot Concentration
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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.
Verification Images
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Immunohistochemical analysis of paraffin-embedded human pancreas using CD13 antibody. The section was pre-treated using heat mediated antigen retrieval with EDTA (pH 9.0) for 14 minutes. The tissues were blocked in 5% BSA for 30 minutes at room temperature, washed with TBST, and then probed with the primary antibody (HY-P81508, 1/200) for 30 minutes at room temperature. The detection was performed using Polymer HRP-conjugated Goat Anti-Mouse/Rabbit lgG(H&L) secondary antibody (HY-P83652). DAB was used as the chromogen. Tissues were counterstained with hematoxylin and mounted with DPX. -
Immunohistochemical analysis of paraffin-embedded human liver cancer using CD13 antibody. The section was pre-treated using heat mediated antigen retrieval with EDTA (pH 9.0) for 14 minutes. The tissues were blocked in 5% BSA for 30 minutes at room temperature, washed with TBST, and then probed with the primary antibody (HY-P81508, 1/200) for 30 minutes at room temperature. The detection was performed using Polymer HRP-conjugated Goat Anti-Mouse/Rabbit lgG(H&L) secondary antibody (HY-P83652). DAB was used as the chromogen. Tissues were counterstained with hematoxylin and mounted with DPX. -
Immunohistochemical analysis of paraffin-embedded human lung cancer using CD13 antibody. The section was pre-treated using heat mediated antigen retrieval with EDTA (pH 9.0) for 14 minutes. The tissues were blocked in 5% BSA for 30 minutes at room temperature, washed with TBST, and then probed with the primary antibody (HY-P81508, 1/200) for 30 minutes at room temperature. The detection was performed using Polymer HRP-conjugated Goat Anti-Mouse/Rabbit lgG(H&L) secondary antibody (HY-P83652). DAB was used as the chromogen. Tissues were counterstained with hematoxylin and mounted with DPX. -
Immunohistochemical analysis of paraffin-embedded human prostate using CD13 antibody. The section was pre-treated using heat mediated antigen retrieval with EDTA (pH 9.0) for 14 minutes. The tissues were blocked in 5% BSA for 30 minutes at room temperature, washed with TBST, and then probed with the primary antibody (HY-P81508, 1/200) for 30 minutes at room temperature. The detection was performed using Polymer HRP-conjugated Goat Anti-Mouse/Rabbit lgG(H&L) secondary antibody (HY-P83652). DAB was used as the chromogen. Tissues were counterstained with hematoxylin and mounted with DPX. -
Immunohistochemical analysis of paraffin-embedded human prostate cancer using CD13 antibody. The section was pre-treated using heat mediated antigen retrieval with EDTA (pH 9.0) for 14 minutes. The tissues were blocked in 5% BSA for 30 minutes at room temperature, washed with TBST, and then probed with the primary antibody (HY-P81508, 1/200) for 30 minutes at room temperature. The detection was performed using Polymer HRP-conjugated Goat Anti-Mouse/Rabbit lgG(H&L) secondary antibody (HY-P83652). DAB was used as the chromogen. Tissues were counterstained with hematoxylin and mounted with DPX. -
Immunohistochemical analysis of paraffin-embedded human liver using CD13 antibody. The section was pre-treated using heat mediated antigen retrieval with EDTA (pH 9.0) for 14 minutes. The tissues were blocked in 5% BSA for 30 minutes at room temperature, washed with TBST, and then probed with the primary antibody (HY-P81508, 1/200) for 30 minutes at room temperature. The detection was performed using Polymer HRP-conjugated Goat Anti-Mouse/Rabbit lgG(H&L) secondary antibody (HY-P83652). DAB was used as the chromogen. Tissues were counterstained with hematoxylin and mounted with DPX. -
Immunohistochemical analysis of paraffin-embedded human bladder cancer using CD13 antibody. The section was pre-treated using heat mediated antigen retrieval with EDTA (pH 9.0) for 14 minutes. The tissues were blocked in 5% BSA for 30 minutes at room temperature, washed with TBST, and then probed with the primary antibody (HY-P81508, 1/200) for 30 minutes at room temperature. The detection was performed using Polymer HRP-conjugated Goat Anti-Mouse/Rabbit lgG(H&L) secondary antibody (HY-P83652). DAB was used as the chromogen. Tissues were counterstained with hematoxylin and mounted with DPX. -
Immunohistochemical analysis of paraffin-embedded human stomach cancer using CD13 antibody. The section was pre-treated using heat mediated antigen retrieval with EDTA (pH 9.0) for 14 minutes. The tissues were blocked in 5% BSA for 30 minutes at room temperature, washed with TBST, and then probed with the primary antibody (HY-P81508, 1/200) for 30 minutes at room temperature. The detection was performed using Polymer HRP-conjugated Goat Anti-Mouse/Rabbit lgG(H&L) secondary antibody (HY-P83652). DAB was used as the chromogen. Tissues were counterstained with hematoxylin and mounted with DPX. -
Immunohistochemical analysis of paraffin-embedded human pancreatic cancer using CD13 antibody. The section was pre-treated using heat mediated antigen retrieval with EDTA (pH 9.0) for 14 minutes. The tissues were blocked in 5% BSA for 30 minutes at room temperature, washed with TBST, and then probed with the primary antibody (HY-P81508, 1/200) for 30 minutes at room temperature. The detection was performed using Polymer HRP-conjugated Goat Anti-Mouse/Rabbit lgG(H&L) secondary antibody (HY-P83652). DAB was used as the chromogen. Tissues were counterstained with hematoxylin and mounted with DPX.
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; CD antigen CD13
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Research Field
Immunology
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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