Induction of Multi-Specific Antibodies to Bovine Serum Albumin after Production of Anti-Idiotype Antibodies to an Albumin-Specific Monoclonal Antibody

1983 ◽  
Vol 418 (1 Immune Networ) ◽  
pp. 305-312 ◽  
Author(s):  
NANCY J. KRIEGER ◽  
AMADEO J. PESCE ◽  
J. GABRIEL MICHAEL
Keyword(s):  
Monoclonal Antibody ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Specific Monoclonal Antibody ◽  
Specific Antibodies

Rhamnose modified bovine serum albumin as a carrier protein promotes the immune response against sTn antigen

2020 ◽  
Vol 56 (90) ◽  
pp. 13959-13962
Author(s):  
Han Lin ◽  
Haofei Hong ◽  
Jinfeng Wang ◽  
Chen Li ◽  
Zhifang Zhou ◽  
...  
Keyword(s):  
Immune Response ◽  
Bovine Serum Albumin ◽  
Immune Responses ◽  
Serum Albumin ◽  
Cancer Vaccine ◽  
Bovine Serum ◽  
Vaccine Development ◽  
Carrier Protein ◽  
Antigen Uptake ◽  
Specific Antibodies

Rhamnose and sTn antigen were co-conjugated to bovine serum albumin (BSA) for cancer vaccine development. The immune responses against sTn have been significantly augmented with the involvement of Rha-specific antibodies to enhance antigen uptake.

Radioimmunoassay for 13, 14-dihydro-15-ketoprostaglandin F2α and its application in normo- and anovulatory women

1982 ◽  
Vol 100 (1) ◽  
pp. 98-104 ◽  
Author(s):  
Werner Schlegel ◽  
Jaime Urdinola ◽  
Hermann P. G. Schneider
Keyword(s):  
Menstrual Cycle ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Rapid Method ◽  
Plasma Levels ◽  
Bovine Serum ◽  
Limit Of Detection ◽  
Cross Reactivity ◽  
Specific Antibodies ◽  
Standard Range

Abstract. Highly specific antibodies to 13, 14-dihydro-15-ketoprostaglandin F2α (PGFM) were raised in rabbits. The animals were immunized with PGFM-bovine serum albumin (BSA)-conjugates. Prior to the incubation procedure PGFM was extracted by a rapid method with dichloromethane followed by column chromatography. The antisera dilution was 1:10000 and the cross-reactivity towards prostaglandin A2, E2, F2α, 13, 14-dihydro-15-ketoprostaglandin E2 and the 15-ketoprostaglandin E2 and F2α was < 1%. The limit of detection was 1.9 ± 0.6 pg/ml plasma over the standard range 1.9–250 pg. The intra- and inter-assay variations were 3.9 and 15%, respectively. PGFM was measured throughout the menstrual cycle in female volunteers. In normal ovulatory women (n = 3) plasma levels of PGFM varied between 65.6 to 107.1 pg/ml. No significant variations of plasma PGFM were seen during the cycle. In anovulatory women (n = 4) no difference of PGFM was found during the cycle. PGFM levels in hyperprolactinaemic but ovulating women tend to be higher than in anovulatory, and normoprolactinaemic subjects. These data strongly indicate that PGFM is not correlated with other hormonal parameters tested here in the normal and anovulatory cycles.

The production of polyclonal antibodies against the mycotoxin derivative patulin hemiglutarate

1993 ◽  
Vol 39 (9) ◽  
pp. 861-863 ◽  
Author(s):  
L. J. McElroy ◽  
C. M. Weiss
Keyword(s):  
Molecular Weight ◽  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Antibody Titer ◽  
Bovine Serum ◽  
Polyclonal Antibodies ◽  
Competitive Elisa ◽  
Low Molecular Weight ◽  
Specific Antibodies ◽  
Indirect Competitive Elisa

The mycotoxin patulin is a toxic, carcinogenic, unsaturated lactone produced by a number of molds. Polyclonal antibodies against patulin hemiglutarate were produced. Specific antibodies against patulin alone, however, were not clearly demonstrated. Because of its low molecular weight, patulin required conjugation to bovine serum albumin (BSA) to increase its immunogenicity. Anti-patulin-hemiglutarate-BSA antibody titer and specificity were determined using indirect and indirect competitive ELISA, respectively. Immunoassays would facilitate detection and quantitation of patulin.Key words: patulin, mycotoxin, antibodies.

Radioimmunoassay of class-specific antibodies (RIACA): Chicken antibodies to bovine serum albumin

1975 ◽  
Vol 12 (8) ◽  
pp. 699-705 ◽  
Author(s):  
Matti K. Viljanen ◽  
Kaisa Granfors ◽  
Paavo Toivanen
Keyword(s):  
Bovine Serum Albumin ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Specific Antibodies

scholarly journals Study of the transit of an integral membrane protein from secretory granules through the plasma membrane of secreting rat basophilic leukemia cells using a specific monoclonal antibody.

1986 ◽  
Vol 102 (2) ◽  
pp. 516-522 ◽  
Author(s):  
J S Bonifacino ◽  
P Perez ◽  
R D Klausner ◽  
I V Sandoval
Keyword(s):  
Monoclonal Antibody ◽  
Bovine Serum Albumin ◽  
Membrane Protein ◽  
Serum Albumin ◽  
Bovine Serum ◽  
Secretory Granules ◽  
Integral Membrane Protein ◽  
Rat Basophilic Leukemia Cells ◽  
Rbl Cells ◽  
Basophilic Leukemia

The monoclonal antibody 5G10 reacted specifically with an 80-kD integral membrane protein in rat basophilic leukemia (RBL) cells. Immunofluorescence microscopy studies of RBL cells, fixed and permeabilized, revealed that the 80-kD protein was located in the membrane of cytoplasmic vesicles. The vesicles were identified as secretory granules by their content in immunoreactive serotonin. Expression of the 5G10 antigen on the surface of unstimulated RBL cells was low. However, RBL cells stimulated to secrete with anti-dinitrophenyl IgE followed by dinitrophenyl-bovine serum albumin or with the Ca2+ ionophore A-23187 displayed an increased expression of the antigen on their surface. Surface exposure of the 5G10 antigen was maximal at 5 min after stimulation of secretion. Removal of dinitrophenyl-bovine serum albumin from the incubation medium resulted in internalization of 50% of the antigen within 10 min.

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