Detection of the dystroglycanopathy protein, fukutin, using a new panel of site-specific monoclonal antibodies

2012 ◽  
Vol 424 (2) ◽  
pp. 354-357 ◽  
Author(s):  
Tracy A. Lynch ◽  
Le Thanh Lam ◽  
Nguyen thi Man ◽  
Kazuhiro Kobayashi ◽  
Tatsushi Toda ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Site Specific

Discrimination of rat Brunner's gland carbohydrate antigens by site-specific monoclonal antibodies

2016 ◽  
Vol 432 ◽  
pp. 76-82 ◽  
Author(s):  
Tomoyuki Chimuro ◽  
Hiroyuki Kuroyama ◽  
Yukinobu Goso ◽  
Kazuhiko Ishihara ◽  
Makoto Kurihara
Keyword(s):  
Monoclonal Antibodies ◽  
Carbohydrate Antigens ◽  
Site Specific ◽  
Brunner’S Gland ◽  
Brunner's Gland

Site-Specific Immobilization of Monoclonal Antibodies Using Spacer-Mediated Antibody Attachment

Langmuir ◽  
1996 ◽  
Vol 12 (17) ◽  
pp. 4292-4298 ◽  
Author(s):  
Shao-Chie (Patrick) Huang ◽  
Karin D. Caldwell ◽  
Jinn-Nan Lin ◽  
Hsu-Kun Wang ◽  
James N. Herron
Keyword(s):  
Monoclonal Antibodies ◽  
Site Specific

IRBP: preparation and characterization of site-specific monoclonal antibodies

1990 ◽  
Vol 9 (4) ◽  
pp. 357-362 ◽  
Author(s):  
Larry A. Donoso ◽  
Merlyn Rodrigues ◽  
Tamara R. Vrabec ◽  
Theodore W. Sery ◽  
Shao-Ling Fong
Keyword(s):  
Monoclonal Antibodies ◽  
Site Specific

Production of Monoclonal Antibodies with Site-Specific Reactivity in Human Colonic Mucosa

1994 ◽  
Vol 86 (s30) ◽  
pp. 11P-11P ◽  
Author(s):  
JE Smithson ◽  
C Prince ◽  
R Pigott ◽  
DP Jewell
Keyword(s):  
Monoclonal Antibodies ◽  
Colonic Mucosa ◽  
Site Specific ◽  
Specific Reactivity

scholarly journals Site-specific inhibition of myosin-mediated motility in vitro by monoclonal antibodies.

1985 ◽  
Vol 100 (4) ◽  
pp. 1024-1030 ◽  
Author(s):  
P F Flicker ◽  
G Peltz ◽  
M P Sheetz ◽  
P Parham ◽  
J A Spudich
Keyword(s):  
Electron Microscopy ◽  
Monoclonal Antibodies ◽  
Binding Sites ◽  
Functional Assay ◽  
Specific Inhibition ◽  
Myosin Molecule ◽  
Site Specific ◽  
Dictyostelium Myosin ◽  
Cell Biol

Monoclonal antibodies directed against seven different sites on Dictyostelium myosin (Peltz, G., J. A. Spudich, and P. Parham, 1985, J. Cell Biol., 100: 1016-1023) were tested for their ability to inhibit movement of myosin in vitro, using the Nitella-based myosin-mediated bead movement assay (Sheetz, M. P., R. Chasan, and J. A. Spudich, 1984, J. Cell Biol., 99: 1867-1871). To complement this functional assay, we located the binding sites of these antibodies by electron microscopy, using the rotary shadowing technique. One antibody bound to the 18,000-dalton light chain and inhibited movement completely. All of the remaining antibodies bound to various positions along the rod portion of the myosin molecule, which is approximately 1,800 A long. Antibodies that bound to the rod about 470, 680, and 1400 A from the head-tail junction did not alter myosin movement. One antibody appeared to bind very close to the head-tail junction and to inhibit movement 50%. Surprisingly, three antibodies that bound about 1,200 A from the head-tail junction inhibited movement completely. This inhibition did not depend on using intact IgG, since Fab' fragments had the same effect.

scholarly journals A comparison of HER2 tumor accumulations of Ga-67 labeled anti-HER2 antibody with chemically and site-specifically conjugated bifunctional chelators

2020 ◽  
Author(s):  
Yumiko Kono ◽  
Keita Utsunomiya ◽  
Yuta Ohira ◽  
Hirokazu Satoh ◽  
Naoki Kan ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Binding Capacity ◽  
Binding Activity ◽  
Pharmacokinetic Analysis ◽  
Pharmacokinetic Studies ◽  
Her2 Positive ◽  
Site Specific ◽  
Planar Images

Abstract Background Monoclonal antibodies (mAb) developed to target specific cancers have achieved considerable success to-date. To further enhance therapeutic efficacy monoclonal antibodies may be conjugated with a cytotoxic drug or radioisotope. We present the development of new method based on site-specific conjugation (SSC) for targeting HER2. The study design involves a comparison of the accumulation of Ga-67 labeled anti-HER2 antibodies with SSC versus conventional chemical conjugation in HER2-positive tumors. Anti-HER2 antibodies were chemically conjugated (Chem) with the bifunctional chelator deferoxamine (Chem-mAb). The resulting chemical conjugate was radiolabeled with Ga-67 yielding Ga-67-Chem -mAb. The SSC anti-HER2 antibodies enzymatically conjugated with deferoxamine using transglutaminase (SSC-mAb) and radiolabeled with Ga-67 yielding Ga-67-SSC-mAb. In vitro, the binding activity of HER2 to both conjugated antibodies was measured using surface Plasmon resonance. In vivo, a xenograft mouse model consisting of transplanted CHO/HER2 were divided into two groups, the Chem and the SSC group. Planar images were acquired over three days after each mAb injection, respectively. Pharmacokinetic analysis was used to compare the Chem group to the SSC group, for Ga-67 accumulation. Result The SSC and Chem groups were found to have similar HER2 binding capacity, however the tumor accumulation ratio gradually increased in the SSC group. The pharmacokinetic studies also found that radiolabeled mAb accumulation was significantly higher in the SSC group than the Chem group in not only the tumors, but also in blood and in other organs. Conclusion The new site-specific conjugation may improve targeted antigen-specific cancer radioimmunotherapy and may, due to higher retention, require a lower dose.

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