This antibody recognizes an extracellular epitope within EGF-like domain I of CD326, a marker of epithelial lineages. This antibody strongly stains various normal epithelial cells and carcinomas.

Anwendungen

Flow Cytometry

Verdünnungen

Flow Cytometry: The reagent is designed for analysis of human blood cells using 20 µl reagent / 100 µl of whole blood or 10⁶ cells in a suspension. The content of a vial (2 ml) is sufficient for 100 tests.

Reaktivität

Human

Immunogen

Small cell lung carcinoma cell line H69.

Wirt

Mouse

Klonalität

Monoclonal

Klon

VU-1D9

Isotyp

IgG1

Konjugat

Excitation: 565nm, Emission: 578nm

Reinigung

This antibody is conjugated with R-phycoerythrin (PE) under optimum conditions. The conjugate is purified by size-exclusion chromatography; removing unconjugated antibody and free fluorochrome.

Produktform

Liquid

Formulierung

Supplied in Phosphate Buffered Saline, pH 7.4, with 15 mM Sodium Azide.

Lagerung

Shipped at 4°C. Store in the dark at 2-8°C. Do not freeze!

Synonyme

17 1A, 323/A3, Adenocarcinoma associated antigen, Adenocarcinoma-associated antigen, Antigen identified by monoclonal, AUA1, CD326, CD326 antigen, Cell surface glycoprotein Trop 1, Cell surface glycoprotein Trop 2, Cell surface glycoprotein Trop-1, CO 17A, CO17 1A, CO17A, DIAR5, EGP, EGP 2, EGP2, EGP314, EGP40, Ep CAM, Ep-CAM, EpCAM1, EPCAM_HUMAN, Epithelial cell adhesion molecule, Epithelial Cell Adhesion Molecule Intracellular Domain (EpCAM-ICD), Epithelial cell surface antigen, Epithelial cellular adhesion molecule, Epithelial glycoprotein, Epithelial glycoprotein 1, Epithelial glycoprotein 314, ESA, GA733 1, GA733 2, GA733-2, gastrointestinal tumor-associated antigen 2, 35-KD glycoprotein, gp4, hEGP 2, hEGP314, HNPCC8, Human epithelial glycoprotein 2, KS 1/4 antigen, KS1/4, KSA, Ly74, Lymphocyte antigen 74, M1S 1, M1S2, M4S1, Major gastrointestinal tumor associated protein GA733 2, Major gastrointestinal tumor-associated protein GA733-2, mEGP314, Membrane component chromosome 4 surface marker (35kD glycoprotein), Membrane component, chromosome 4, surface marker, Membrane component, chromosome 4, surface marker 1, MIC18, MK 1, Protein 289A, TACD1, TACSTD1, TROP1, Tumor associated calcium signal transducer 1, Tumor associated calcium signal transducer 2 precursor, Tumor-associated calcium signal transducer 1

Isotyp-Kontrollantikörper

Mouse IgG1 [MOPC-21] (PE) (A86199)

Haftungsausschluss

Dieses Produkt ist nur für Forschungszwecke bestimmt. Es ist nicht für diagnostische oder therapeutische Zwecke bestimmt.

Produktbilder (1)

Bild Vergrößern

Figure 1: Flow Cytometry - Anti-EpCAM Antibody [VU-1D9] (PE) (A86151)

Surface staining of human MCF-7 cell line with Anti-CD326 Antibody (A86151).

Produktreferenzen für diesen Klon (5)

Bild Vergrößern

(2)

The epithelial cell adhesion molecule (Ep-CAM) as a morphoregulatory molecule is a tool in surgical pathology.

Verweise: Anti-EpCAM Antibody [VU-1D9] (PE) (ab112068)

Abstrakt:

Cell adhesion receptors (CAMs) are actively involved in regulating various cell processes, including growth, differentiation, and cell death. Therefore, CAMs represent a large group of morphoregulating molecules, mediating cross-talk between cells and of cells with their environment. From this perspective, CAMs do contribute to cells and tissue organization, and in diseased tissue, to the disease development and biological characteristics. Therefore, observed changes in expression patterns of adhesion molecules may contribute to establish a diagnosis. A distinct shift in expression patterns in neoplastic epithelium has been described, for example for cadherins, integrins, and CD44. A relatively novel cell CAM, Ep-CAM, was first reported to be a pan-carcinoma antigen, although it is rather a marker of epithelial lineage. Several antibodies directed to Ep-CAM have been generated, and many epithelial tissues and their neoplastic appendages have been studied. This article outlines the results of these studies. Based on the results of these studies, we conclude that Ep-CAM immunohistochemistry can be a useful tool in the diagnosis of disturbed epithelial tissues.

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Immunohistochemical localization of epithelial glycoprotein EGP-2 and carcinoembryonic antigen in normal colonic mucosa and colorectal tumors.

Verweise: Anti-EpCAM Antibody [VU-1D9] (PE) (ab112068)

Abstrakt:

Epithelial glycoprotein EGP-2 and carcinoembryonic antigen (CEA) are transmembrane glycoproteins and cell surface markers. Eighty-four colorectal tumors including 23 adenomas (2 mild, 13 moderate, and 8 severe atypia) and 61 adenocarcinomas (33 well- and 28 moderately differentiated) as well as adjacent normal colonic mucosa (51 cases) were studied for the immunolocalization of EGP-2 as detected by the monoclonal antibody VU-1D9, and compared with CEA expression. In the normal colonic mucosa, basolateral VU-1D9 expression in the surface epithelial cells was constantly seen in all 51 cases, while weak apical CEA staining in the surface epithelium was seen in 25% (13/51) of the cases. In 91% (21/23) of the adenomas, regardless of the grade of atypia, VU-1D9 labeled the basolateral membrane of a few surface lining cells leaving atypically proliferating glands negative, while CEA expressed strong apical staining in the surface epithelial cells as well as atypically proliferating glands. The well-differentiated adenocarcinomas showed homogeneous basolateral staining for VU-1D9 and strong apical staining for CEA; the moderately differentiated adenocarcinomas showed membranous as well as cytoplasmic VU-1D9 staining and luminal as well as cytoplasmic CEA staining. The VU-1D9 and CEA localizations and the stage of expression in relation to tumor progression were completely different. Strong CEA expression was seen in the adenomatous stage, while the homogeneous VU-1D9 expression required tumor progression to the carcinomatous stage. VU-1D9 especially when applied in combination with CEA, will be a useful marker for colorectal lesions, and its reactivity patterns in carcinoma can predict the prognosis.

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Immunohistochemical demonstration of breast-derived and/or carcinoma-associated glycoproteins in normal skin appendages and their tumors.

Verweise: Anti-EpCAM Antibody [VU-1D9] (PE) (ab112068)

Abstrakt:

Sixty-six benign and malignant skin appendage tumors were studied for the expression and localization of the glycoproteins identified by the monoclonal antibodies (MoAbs) GCDFP-15, CU18, B72.3, and VU-1D9. Formalin-fixed, paraffin-embedded tissue was processed by the avidin-biotin complex method. In normal eccrine and apocrine sweat glands, GCDFP-15, CU18, B72.3, and VU-1D9 staining was localized differently (intracellular, membranous, or intraluminal), whereas eccrine glands showed no B72.3 staining. There were various patterns of positive staining of tumors arising from sweat glands, but no immunoreactivity for B72.3 was found in eccrine-derived tumors. CU18 and VU-1D9 labeled mature sebocytes in a vacuolar fashion and stained sebaceous carcinomas. VU-1D9 labeled membranes of the secondary germ cells in early anagen of a hair follicle bulb as well as the basaloid cells of trichoepitheliomas and basal cell carcinomas. These MoAbs appear to be valuable markers for the study of normal skin appendages and their tumors.

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EpCAM is predominantly expressed in high grade and advanced stage urothelial carcinoma of the bladder.

Verweise: Anti-EpCAM Antibody [VU-1D9] (PE) (ab112068)

Abstrakt:

BACKGROUND:

EpCAM is an adhesion molecule of the basolateral membranes in a variety of epithelial cells. Over-expression has been detected in many epithelial tumours and has been associated with high stage, high grade and a worse survival in some tumour types.

AIMS:

To assess the prognostic value of EpCAM in urothelial carcinoma of the bladder.

METHODS:

EpCAM expression was analysed by immunohistochemistry using a monoclonal antibody (clone VU-1D9) on a tissue microarray comprising 99 urothelial carcinomas of the bladder diagnosed between 1994 and 1997.

RESULTS:

A significant relationship between high grade, advanced stage, and EpCAM expression was found, and expression of EpCAM was associated with a worse overall survival when compared to EpCAM negative tumours (p = 0.033). Multivariate analysis showed that EpCAM expression was not an independent prognostic factor for overall survival in urothelial carcinoma of the bladder.

CONCLUSION:

EpCAM expression is associated with advanced stage, high grade and poor overall survival in urothelial carcinoma of the bladder, but lacks an independent prognostic significance. The strong association with high grade tumours suggests a possible role during tumour progression and makes EpCAM a potential target for antibody mediated therapy.

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Flow cytometric analysis of antigen expression in malignant and normal renal cells.

Verweise: Anti-EpCAM Antibody [VU-1D9] (PE) (ab112068)

Abstrakt:

Flow cytometry allows quantitative analysis of cancer cells. The aim of this study was to make a quantitative study of antigen expression in malignant and normal renal cells in order to find the efficient monoclonal antibodies (mAbs) for labelling renal cancer cells.

MATERIAL AND METHODS:

15 malignant and adjacent normal renal tissues and three renal carcinoma cell lines (ACHN, A704 and CAKI-2) were analyzed. The malignant and normal renal tissues were dissociated mechanically into cell suspension. The mAbs and isotype controls were used for immunochemical labelling. The stained cells were analyzed by flow cytometry.

RESULTS:

Renal tumor associated antigen G 250 was frequently detected in malignant renal cells but not in normal renal cells. Renal tumor associated antigen gp200 recognized by 66.4.C2 and PN-15 was frequently detected in malignant cells, normal renal cells and also in all three carcinoma cell lines. Epithelial antigens were strongly positive in normal renal cells. Compared with MOC 31, Ber-EP4 and E 29, W-lD9 was mostly reactive to malignant renal cells. VU-1D9 was strongly positive on ACHN and A704. The carbohydrate carcinoma antigens CA 125, DF3 and Sialyl Lewis(a) were detectable in some of the malignant and normal renal cells. Sialyl Lewis(a) could be weakly detected on ACHN and A 704. Pan-cytokeratins and cytokeratin (CK) 8 were strongly expressed in malignant and normal renal cells and in all three cell lines.

CONCLUSION:

Our results indicated that G 250, 66.4.Ca, PN-15, VU-1D9, MNF116 and anti-ckg were efficient mAbs for labelling renal cancer cells. Their potential clinical application by flow cytometry should be explored.

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