CD13 antibody | WM15
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Mouse anti Human CD13
- Product Type
- Monoclonal Antibody
| Mouse anti Human CD13 antibody, clone WM15 recognizes human CD13 also known as aminopeptidase N. CD13 is a single pass type II glycosylated integral membrane protein with a predicted molecular mass of ~110 kDa and an apparent molecular mass of ~150 kDa expressed by granulocytes, monocytes, fibroblasts, endothelial cells and by myeloid leukaemia cells (Bradstock et al. 1985). CD13 acts as a major cell surface receptor for group 1 coronoviruses (Breslin et al. 2003) which bind to a critical sequence encompassing amino acid residies 288-295 (Kolb et al. 1997).
CD13 functions as an aminopeptidase enzyme, a metalloprotease present as both a membrane bound form and also a soluble aminopeptidase N.
Mouse anti Human CD13, clone WM15 inhibits infection of cells by human coronavirus (Lachance et al. 1998) but not hepatitis C virus (Koutsoudakis et al. 2006) and inhibits aminopeptidase N activity of the CD13 molecule (Asmun et al. 1992).
- Target Species
- Species Cross-Reactivity
Target Species Cross Reactivity Rhesus Monkey
- N.B. Antibody reactivity and working conditions may vary between species.
- Product Form
- Purified IgG - liquid
- Purified IgG prepared by affinity chromatography on Protein A from tissue culture supernatant
- Buffer Solution
- Phosphate buffered saline
- Preservative Stabilisers
- 0.09% sodium azide (NaN3)
- Carrier Free
- Human AML cells.
- Approx. Protein Concentrations
- IgG concentration 1.0 mg/ml
- Fusion Partners
- Spleen cells from immunised BALB/c mice where fused with cells of the mouse NS1 myeloma cell line.
- For research purposes only
- 12 months from date of despatch
Avoid repeated freezing and thawing as this may denature the antibody. Storage in frost-free freezers is not recommended.
|Application Name||Verified||Min Dilution||Max Dilution|
|Immunohistology - Frozen|
- Flow Cytometry
- Use 10μl of the suggested working dilution to label 106 cells or 100μl whole blood
References for CD13 antibody
Bradstock, K.F. et al. (1985) Human myeloid differentiation antigens identified by monoclonal antibodies: expression on leukemic cells.
Pathology. 17 (3): 392-9.
Bradstock, K.F. et al. (1985) Myeloid progenitor surface antigen identified by monoclonal antibody.
Br J Haematol. 61 (1): 11-20.
Favaloro, E.J. et al. (1988) Further characterization of human myeloid antigens (gp160,95; gp150; gp67): investigation of epitopic heterogeneity and non-haemopoietic distribution using panels of monoclonal antibodies belonging to CD-11b, CD-13 and CD-33.
Br J Haematol. 69 (2): 163-71.
Favaloro, E.J. (1991) CD-13 (gp150; aminopeptidase-N): co-expression on endothelial and haemopoietic cells with conservation of functional activity.
Immunol Cell Biol. 69 ( Pt 4): 253-60.
Favaloro, E.J. et al. (1993) The hepatobiliary disease marker serum alanine aminopeptidase predominantly comprises an isoform of the haematological myeloid differentiation antigen and leukaemia marker CD-13/gp150.
Clin Chim Acta. 220 (1): 81-90.
Favaloro, E.J. et al. (1993) CD13 (GP150; aminopeptidase-N): predominant functional activity in blood is localized to plasma and is not cell-surface associated.
Exp Hematol. 21 (13): 1695-701.
Tavoosidana, G. et al. (2011) Multiple recognition assay reveals prostasomes as promising plasma biomarkers for prostate cancer.
Proc Natl Acad Sci U S A. 108: 8809-14.
Gredmark, S. et al. (2004) Human Cytomegalovirus Induces Inhibition of Macrophage Differentiation by Binding to Human Aminopeptidase N/CD13
J Immunol. 173: 4897-907
View The Latest Product References
Grzywacz, B. et al. (2011) Natural killer-cell differentiation by myeloid progenitors.
Blood. 117: 3548-58.
Stolzing, A. et al. (2008) Age-related changes in human bone marrow-derived mesenchymal stem cells: consequences for cell therapies.
Mech Ageing Dev. 129: 163-73.
Silk, K.M. et al. (2012) Rapamycin conditioning of dendritic cells differentiated from human ES cells promotes a tolerogenic phenotype.
J Biomed Biotechnol. 2012:172420.
Negussie, A.H. et al. (2010) Synthesis and in vitro evaluation of cyclic NGR peptide targeted thermally sensitive liposome.
J Control Release. 143: 265-73.
Lassnig, C. et al. (2005) Development of a transgenic mouse model susceptible to human coronavirus 229E.
Proc Natl Acad Sci U S A. 102 (23): 8275-80.
Thielitz, A. et al. (2004) Identification of extra- and intracellular alanyl aminopeptidases as new targets to modulate keratinocyte growth and differentiation.
Biochem Biophys Res Commun. 321 (4): 795-801.
McCormack, E. et al. (2013) Multiplexed mAbs: a new strategy in preclinical time-domain imaging of acute myeloid leukemia.
Blood. 121 (7): e34-42.
Fiddler, C.A. et al. (2016) The Aminopeptidase CD13 Induces Homotypic Aggregation in Neutrophils and Impairs Collagen Invasion.
PLoS One. 11 (7): e0160108.
Chaturvedi, C.P. et al. (2018) Altered Expression of Hematopoiesis Regulatory Molecules in Lipopolysaccharide-Induced Bone Marrow Mesenchymal Stem Cells of Patients with Aplastic Anemia.
Stem Cells Int. 2018: 6901761.
- Aminopeptidase N
- Entrez Gene
- GO Terms
- GO:0001525 angiogenesis
- GO:0004177 aminopeptidase activity
- GO:0008237 metallopeptidase activity
- GO:0005829 cytosol
- GO:0004872 receptor activity
- GO:0005887 integral to plasma membrane
- GO:0005793 ER-Golgi intermediate compartment
- GO:0008270 zinc ion binding
- GO:0030154 cell differentiation
- View More GO Terms
- GO:0044419 interspecies interaction between organisms
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