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globo H monoclonal antibody (MBr1)

 
ALX-804-550-C050 50 µg 269.00 USD
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The murine monoclonal antibody to globo H (clone MBr1) is raised against the breast cancer cell line MCF7 and recognizes a saccharidic epitope (CaMBr1) overexpressed on a high percentage of human breast, ovary lung and prostate carcinomas. This antigen was originally identified on the immunogen as a globo-series glycosphingolipid with a H-like determinant at its terminus (globo-H), identical to GL6 isolated from human teratocarcinoma. MAb to MBr1 was also found to be reactive with different glycoconjugates (glycoproteins, mucins and glycolipids) in breast and small cell lung carcinoma. Retrospective as well as prospective studies suggest that CaMBr1 expression is associated with tumor aggressiveness and survival outcome in breast and small cell lung cancer and that poor prognosis is more frequently associated with CaMBr1 expression on glycoproteins. The epitope recognized by the MAb to MBr1 consists of the tetrasaccharide Fucα1-2Galβ1-3GalNacβ1-3Gal, available as a synthetic oligosaccharide exploitable for the development of new anti-cancer vaccines. Carbohydrate antigens expressed at the cell surface of human cancer cells hold promise as targets for active immunization with vaccines.CaMBR1 is also expressed on some normal tissues, and its expression restricted tissue distribution makes it a suitable target for oncologic clinical applications. In particular the MAb to MBr1 can be succesfully used for immunocytochemical detection of micrometastatic cells.

Product Specification

Clone:MBr1
 
Host:Mouse
 
Isotype:IgM
 
Immunogen:Membrane preparation from the human breast carcinoma cell line MCF7.
 
Species reactivity:Human, Rat
Cat, Dog
 
Specificity:Recognizes membrane bound glycoconjugates (glycoproteins, mucins and glycolipids) expressing the globo H or its tetrasaccharide terminus. Recognizes an epitope consisting of the tetrasaccharide Fucα1-2Galβ1-3GalNacβ1-3Gal.
 
Crossreactivity:Does not cross-react with mouse. Cross-reactivity with other species has not been tested.
 
Applications:Flow Cytometry, ICC, IHC (FS), IHC (PS), WB
 
Recommended Dilutions/Conditions:Flow Cytometry (1-10µg/ml)
Immunocytochemistry (1-10µg/ml)
Immunohistochemsitry (frozen sections, 1-10µg/ml)
Immunohistochemistry (paraffin sections, 1-10µg/ml, no need of antigen retrieval)
Western Blot (1-10µg/ml, for glycoproteins)
Suggested dilutions/conditions may not be available for all applications.
Optimal conditions must be determined individually for each application.
 
Application Notes:Not recommended for immunoprecipitation.
 
Purity Detail:Purified from concentrated hybridoma cell culture supernatant by thiophilic adsorption chromatography.
 
Formulation:Liquid. In 50mM PBS, pH 8.0, containing 150mM sodium chloride. Contains no sodium azide.
 
Handling:Avoid freeze/thaw cycles.
 
Shipping:Shipped on Blue Ice
 
Long Term Storage:+4°C
 

Product Literature References

Neofunctionalization of the Sec1 α1,2fucosyltransferase Paralogue in Leporids Contributes to Glycan Polymorphism and Resistance to Rabbit Hemorrhagic Disease Virus: K. Nyström, et al.; PLoS Pathog. 11, e1004759 (2015), Application(s): Assay, Abstract; Full Text
Carbohydrate microarray for profiling the antibodies interacting with Globo H tumor antigen: C.Y. Huang, et al.; PNAS 103, 15 (2006), Abstract;
Improvement of the synthesis of immunological carbohydrate vaccines containing the tumour associate antigen CaMBr1: L. Lay, et al.; Eur. J. Org. Chem. 22, 4331 (2001), Abstract;
Role for alpha1,2-fucosyltransferase and histo-blood group antigen H type 2 in resistance of rat colon carcinoma cells to 5-fluorouracil: S. Cordel, et al.; Int. J. Cancer 85, 142 (2000), Abstract;
Expression profile of saccharide epitope CaMBr1 in normal and neoplastic tissue from dogs, cats, and rats: implication for the development of human-derived cancer vaccines: E. Adobati, et al.; Histochem. J. 31, 729 (1999), Abstract;
Synthesis, modeling and binding affinity of an ester analogue of the terminal trisaccharide of the tumor-associated antigen globo-H: S. Canevari, et al.; Tetrahedron 55, 1469 (1999),
In vitro mimicry of CaMBr1 tumor-associated antigen by synthetic oligosaccharides: E. Adobati, et al.; Glycobiology 7, 173 (1997), Abstract;
Oligosaccharides related to tumor-associate antigens, Part 3: L. Lay, et al.; Helv. Chim. Acta 78, 533 (1995),
Prognostic significance of the CaMBr1 antigen on breast carcinoma: relevance of the type of recognised glycoconjugate: F. Perrone, et al.; Eur. J. Cancer 29A, 2113 (1993), Abstract;
Study of the expression and function of the tumour-associated antigen CaMBr1 in small cell lung carcinomas: S. Martignone, et al.; Eur. J. Cancer 29A, 2020 (1993), Abstract;
Expression of two antigens defined by monoclonal antibodies in normal, benign and malignant human mammary tissues: F. Perrone, et al.; Tumori 76, 525 (1990), Abstract;
Use of monoclonal antibody MBr1 to detect micrometastases in bone marrow specimens of breast cancer patients: B. Salvadori, et al.; Eur. J. Cancer 26, 865 (1990), Abstract;
Use of monoclonal antibody MBr1 to detect micrometastases in bone marrow specimens of breast cancer patients: B. Salvadori, et al.; Eur. J. Cancer 26, 865 (1990), Abstract;
Chapter 17: Immunoblotting detection of carbohydrate epitopes in glycolipids and glycoproteins of tumoral origin: D. Miotti, et al.; Gangliosides and Cancer (Weinheim, VCH Verlagsgesellschaft) 169 (1989),
In vivo and in vitro growth of SCLC cells derived from biopsies: S. Giani, et al.; Tumori 75, 570 (1989), Abstract;
Relationship between CaMBr1 expression and tumor progression in small cell lung carcinomas: S. Martignone, et al.; Tumori 75, 373 (1989), Abstract;
Type 4 chain H expression by bile ductules and hepatocytes in cirrhosis: Y. Okada, et al.; J. Pathol. 157, 329 (1989), Abstract;
Association of monoclonal antibody-recognized antigen with steroid receptors in gynecologic tumors: K.C. Wang, et al.; Cancer Invest. 6, 151 (1988), Abstract;
Monoclonal antibody detection of carcinoma cells in bone marrow biopsy specimens from breast cancer patients: G. Porro, et al.; Cancer 61, 2407 (1988), Abstract;
Carcinoma of the breast and of the ovary as a model for the application of monoclonal antibodies to diagnostic pathology: F. Rilke, et al.; Monogr. Pathol. 27, 206 (1986), Abstract;
Characterization of a glycosphingolipid antigen defined by the monoclonal antibody MBr1 expressed in normal and neoplastic epithelial cells of human mammary gland: E.G. Bremer, et al.; J. Biol. Chem. 259, 14773 (1984), Abstract; Full Text
Immunohistochemical reactivity of a monoclonal antibody prepared against human breast carcinoma: R. Mariani-Costantini, et al.; Virchows Arch. A Pathol. Anat. Histopathol. 402, 389 (1984), Abstract;
Reactivity of a monoclonal antibody with tissues and tumors from the human breast. Immunohistochemical localization of a new antigen and clinicopathologic correlations: R. Mariani-Costantini, et al.; Am. J. Pathol. 115, 47 (1984), Abstract;
Generation of monoclonal antibodies reacting with normal and cancer cells of human breast: S. Menard, et al.; Cancer Res. 43, 1295 (1983), Abstract;
Immunochemical analysis of the determinant recognized by a monoclonal antibody (MBr1) which specifically binds to human mammary epithelial cells: S. Canevari, et al.; Cancer Res. 43, 1301 (1983), Abstract;

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