Development of a high affinity monoclonal antibody against imazapyr and its configuration in a sensitive ELISA suitable for field use

2001 ◽  
Vol 5 (6) ◽  
pp. 281-287
Author(s):  
L. K. Siew ◽  
J. L. Dessi ◽  
J. A. Spoors ◽  
L. Winger ◽  
L. Jennens ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
High Affinity

Selection of aptamers with high affinity and high specificity against C595, an anti-MUC1 IgG3 monoclonal antibody, for antibody targeting

2005 ◽  
Vol 296 (1-2) ◽  
pp. 45-62 ◽  
Author(s):  
Sotiris Missailidis ◽  
Despina Thomaidou ◽  
K. Eszter Borbas ◽  
Mike R. Price
Keyword(s):  
Monoclonal Antibody ◽  
High Specificity ◽  
High Affinity ◽  
Antibody Targeting ◽  
Selection Of

scholarly journals Rolling on E- or P-selectin induces the extended but not high-affinity conformation of LFA-1 in neutrophils

Blood ◽  
2010 ◽  
Vol 116 (4) ◽  
pp. 617-624 ◽  
Author(s):  
Yoshihiro Kuwano ◽  
Oliver Spelten ◽  
Hong Zhang ◽  
Klaus Ley ◽  
Alexander Zarbock
Keyword(s):  
Monoclonal Antibody ◽  
Tyrosine Kinase ◽  
Binding Assay ◽  
P38 Map Kinase ◽  
Intercellular Adhesion Molecule ◽  
Reporter Assay ◽  
Rolling Velocity ◽  
High Affinity ◽  
Velocity Reduction ◽  
Blood Neutrophils

Abstract Human blood neutrophils rolling on E- or P-selectin reduced their rolling velocity when intercellular adhesion molecule (ICAM)–1 was available. Similar to mouse neutrophils, this was dependent on P-selectin glycoprotein ligand 1 (PSGL1), αLβ2 integrin, the Src family tyrosine kinase FGR and spleen tyrosine kinase SYK. Blocking phospholipase C or p38 MAP kinase attenuated, but did not abolish the velocity reduction. To test expression of integrin activation epitopes, we adapted an immobilized reporter assay and developed a new homogeneous microfluidics-based reporter antibody binding assay. Rolling on E- or P-selectin induced the extension reporter epitopes KIM127 and NKI-L16, but not the high affinity reporter epitope monoclonal antibody (mAb) 24. This enabled rolling neutrophils to bind to immobilized extension reporter, but not activation reporter antibodies and allowed binding of soluble KIM127 during rolling. We conclude that human neutrophil rolling on E- or P-selectin induces the extended αLβ2 integrin conformation through signaling triggered by PSGL-1 engagement.

scholarly journals Structure and characterization of a high affinity C5a monoclonal antibody that blocks binding to C5aR1 and C5aR2 receptors

mAbs ◽  
2017 ◽  
Vol 10 (1) ◽  
pp. 104-117 ◽  
Author(s):  
Caroline S. Colley ◽  
Bojana Popovic ◽  
Sudharsan Sridharan ◽  
Judit E. Debreczeni ◽  
David Hargeaves ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
High Affinity

Development of XPA067.06, a potent high affinity human anti-gastrin monoclonal antibody

2008 ◽  
Vol 76 (3) ◽  
pp. 340-352
Author(s):  
Ssucheng J. Hsu ◽  
Amita Patel ◽  
Paul D. Larsen ◽  
David J. Bohmann ◽  
Robert J. Bauer ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
High Affinity

scholarly journals G196 epitope tag system: a novel monoclonal antibody, G196, recognizes the small, soluble peptide DLVPR with high affinity

2017 ◽  
Vol 7 (1) ◽  
Author(s):  
Kasumi Tatsumi ◽  
Gyosuke Sakashita ◽  
Yuko Nariai ◽  
Kosuke Okazaki ◽  
Hiroaki Kato ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Epitope Tag ◽  
Soluble Peptide ◽  
High Affinity ◽  
System A

Preparation Of Factor IX-Deficient Human Plasma Using RFF-IX/1 Monoclonal Antibody

1981 ◽  
Author(s):  
F Rotblat ◽  
A H Goodall ◽  
G Janossy ◽  
G Kemble ◽  
D P O’Brien ◽  
...  
Keyword(s):  
Monoclonal Antibody ◽  
Cell Line ◽  
Factor Ix ◽  
Hybrid Cells ◽  
Spleen Cells ◽  
High Affinity ◽  
A Cell ◽  
A Site ◽  
Monoclonal Cell Line ◽  
Mouse Myeloma

A cell line that secretes a monoclonal antibody to factor IX has been produced by fusing spleen cells from a mouse that had been hyper immunised to purified factor IX with mouse myeloma cells (line P3-NSI/I-Ag4-1). Hybrid cells were selected and a monoclonal cell line has been established in culture. This cell line secretes an IgGl(k) antibody (RFF-IX/1) with high affinity for a site related to the coagulant function of factor IX.Monoclonal antibody was partially purified from ascitic fluid from mice implanted with the RFF-IX/1 secreting cells by precipitation at 50% saturation with ammonium sulphate. This fraction has typically 630 NIH units/ml anti IX activity and 13.5 mg/ml protein. It was coupled to cyanogen bromide activated Sepharose 2B in the ratio of 9 mg. protein/1 ml gel. A column containing 10 ml of this gel removed all the assayable factor IX from the first 280 ml of normal ci.trated plasma that was passed over it. After that volume small amounts of factor IX could be detected in the effluent. Subsequently 10-20% of the factor IX activity adsorbed could be recovered by eluting the column with 3 M potassium iodide.Immuno-affinity depleted plasma could be used as substrate in a one-stage factor IX assay under routine laboratory conditions and was undistinguishable for that purpose from severe Christmas disease plasma.

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