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European Journal of Microbiology and Immunology
Authors: P. Vidyasagar, V. Nimmagadda Sridevi PhD, S. Rajan, A. Praveen, A. Srikanth, G. Abhinay, V. Siva Kumar, R. R. Verma, and L. Rajendra

C.A. Reed 1996 Surface conformational and linear epitopes on HPV-16 and HPV-18 L1 virus-like particles as defined by monoclonal antibodies Virology

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SM Anderton 2006 Comment on “Cutting edge: anti-CD25 monoclonal antibody injection results in the functional inactivation, not depletion, of CD4+CD25+ T regulatory cells” J

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Acta Veterinaria Hungarica
Authors: Ildikó Bódi, Nándor Nagy, Lídia Sinka, Botond-Zoltán Igyártó, and Imre Oláh

. and Ginsberg, M. H. (1991): Monoclonal antibodies to ligand-occupied conformers of integrin alpha IIb beta 3 (glycoprotein IIb–IIIa) alter receptor affinity, specificity, and function. J. Biol. Chem. 26 , 17106

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. Assoc. 190 1450 1458 Bolin, S., Moennig, V., Gourley, N. E. K. and Ridpath, J. 1988: Monoclonal antibodies

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human monoclonal antibodies for therapeutics. Curr. Opin. Biotechnol., 2002, 13 , 593–597. Green L. L. Antibody discovery: the use of transgenic mice to generate human monoclonal

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11 215 Nishio, O., Ooseto, M., Takagi, K., Yamasita, Y., Ishihara, Y., Isomura, S.: Enzyme-linked immunosorbent assay employing monoclonal antibodies for direct

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Abstract  

Human AFP was used as an antigen for the development of monoclonal antibodies by the hybridoma technique. Balb/c mice were immunized with highly purified AFP. The preparation of I125-AFP was carried out by lactoperoxidase oxidation method, preparation of AFP standards was carried out from cord sera. The antibody titer of the serum was tested by RIA-AFP system. The spleen of the immunized Balb/c was fused with Sp20 mouse myeloma cells. The cells from the positive hybridomas were cloned twice using limiting dilution method. Eleven stable clones were thus established for secreting monoclonal antibodies to AFP. Cells in this growth phase were chosen for freezing.

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Abstract  

Prostate specific antigen (PSA) is a reliable biochemical marker used in screening for prostate carcinoma. Immunoradiometric assays (IRMA) are generally used for the estimation of total/free PSA in serum samples. Radiolabeled antibody, an important reagent of IRMA was prepared and characterized using an in-house anti-PSA monoclonal antibody (Mab), Mab-2S. Mab-2S was radiolabeled with 125I and characterized for immunoreactivity and radiochemical purity. The usability of the radioiodinated Mab as tracer in IRMA was ascertained using authentic reagents for IRMA of PSA.

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Abstract  

A method for labeling of anti-carcinoembryonic antigen (CEA) monoclonal antibody (MAb) BW 431/26 is described. For preparations of99mTc-anti-CEA complex, a solution (1 ml) of tetrasodium-1,1,3,3-propanetetetraphosphate dihydrate (2.7 mg), stannous chloride dihydrate (0.12 mg) and sodium chloride (0.2 mg) in 5 ml of 0.9% saline was added to a vial containing monoclonal antibody (2 mg) from mouse (MAb BW 431/26), D-glucitol (2 mg) and sodium sulfate (2 mg) to obtain a clear solution. A quantitative labeling yield of the MAb BW 431/26 was achieved by addition of 5 ml (40.5 mCi, 1.5 Gbq) technetium-99m-pertechnetate (99mTcO4) generator eluate at room temperature within 10 minutes. The radiochemical purity determined by ITLC (Gelman, SG) plates was >95%.

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Summary  

A simple, one step, inclusive immunoradiometric assay for human chorionic gonadotropin (hCG) employing monoclonal antibodies is described. Commercially available monoclonal antibodies from various commercial sources were screened. Identified “detection” antibody was radiolabeled with 125I and the selected “capture” antibody was chemically coupled to magnetizable cellulose to form a solid phase. In the procedure developed, standard/sample, radiolabeled antibody and capture antibody were incubated together for 3 hours at room temperature with shaking. After incubation, the bound complex was quantitated for the associated radioactivity. The analytical sensitivity observed was 1.0 mIU/ml with a wide concentration range up to 1000 mIU/ml of hCG. “High dose hook” of the developed assay was observed beyond 2000 mIU/ml. Results showed that the developed assay had a good precision: intra-assay CV less than 8%, inter-assay CV less than 10% and good analytical recovery of 97-109%. The clinical samples analyzed by the developed procedure showed a good correlation with that of the commercial kit (r = 0.92; y = 0.99x+0.51).

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