Isolation and Characterization of Phage-Displayed Single Chain Antibodies Recognizing Nonreducing Terminal Mannose Residues. 2. Expression, Purification, and Characterization of Recombinant Single Chain Antibodies†

Biochemistry ◽  
2007 ◽  
Vol 46 (1) ◽  
pp. 263-270 ◽  
Author(s):  
Wei Zhang ◽  
Ayano Matsumoto-Takasaki ◽  
Yu Kusada ◽  
Hiroyuki Sakaue ◽  
Keiko Sakai ◽  
...  
Keyword(s):  
Single Chain ◽  
Purification And Characterization ◽  
Single Chain Antibodies ◽  
Isolation And Characterization ◽  
Terminal Mannose

Isolation and Characterization of Phage-Displayed Single Chain Antibodies Recognizing Nonreducing Terminal Mannose Residues. 1. A New Strategy for Generation of Anti-Carbohydrate Antibodies†

Biochemistry ◽  
2007 ◽  
Vol 46 (1) ◽  
pp. 253-262 ◽  
Author(s):  
Keiko Sakai ◽  
Yoshitaka Shimizu ◽  
Tomoki Chiba ◽  
Ayano Matsumoto-Takasaki ◽  
Yu Kusada ◽  
...  
Keyword(s):  
Single Chain ◽  
Single Chain Antibodies ◽  
Isolation And Characterization ◽  
New Strategy ◽  
Terminal Mannose

Isolation and Characterization of Neutralizing Single-Chain Antibodies againstXenopusMitogen-Activated Protein Kinase Kinase from Phage Display Libraries†

Biochemistry ◽  
1996 ◽  
Vol 35 (40) ◽  
pp. 13212-13221 ◽  
Author(s):  
Hidetaka Kosako ◽  
Yoshiko Akamatsu ◽  
Naoya Tsurushita ◽  
Kyung-Kwon Lee ◽  
Yukiko Gotoh ◽  
...  
Keyword(s):  
Protein Kinase ◽  
Phage Display ◽  
Single Chain ◽  
Single Chain Antibodies ◽  
Isolation And Characterization ◽  
Phage Display Libraries ◽  
Protein Kinase Kinase

Isolation and characterization of rabbit single chain antibodies to human Reg Iα protein

2002 ◽  
Vol 266 (1-2) ◽  
pp. 197-207 ◽  
Author(s):  
X.Sherry Chi ◽  
Yvonne Landt ◽  
Dan L Crimmins ◽  
Brian K Dieckgraefe ◽  
Jack H Ladenson
Keyword(s):  
Single Chain ◽  
Single Chain Antibodies ◽  
Isolation And Characterization ◽  
Reg Iα

Characterization of three different single chain antibodies recognizing non-reducing terminal mannose residues expressed in Escherichia coli by an inducible T7 expression system

2011 ◽  
Vol 150 (4) ◽  
pp. 439-450 ◽  
Author(s):  
A. Matsumoto-Takasaki ◽  
N. Yuasa ◽  
D. Katagiri ◽  
T. Koyama ◽  
K. Sakai ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Expression System ◽  
Single Chain ◽  
Single Chain Antibodies ◽  
T7 Expression System ◽  
Terminal Mannose

Construction and characterization of two anti-sweetener single chain antibodies using radioligand binding, fluorescence and circular dichroism spectroscopy

1999 ◽  
Vol 12 (4) ◽  
pp. 258-266 ◽  
Author(s):  
David W. Pledger ◽  
Thomas C. Brodnicki ◽  
Brent L. Graham ◽  
Sergey Tetin ◽  
David M. Kranz ◽  
...  
Keyword(s):  
Circular Dichroism ◽  
Radioligand Binding ◽  
Circular Dichroism Spectroscopy ◽  
Single Chain ◽  
Single Chain Antibodies ◽  
Circular Dichroïsm

Purification and characterization of a single-chain chimeric anti-p185 antibody expressed by CHO–GS system

2005 ◽  
Vol 41 (1) ◽  
pp. 68-76 ◽  
Author(s):  
Jing Wang ◽  
Yu Shi ◽  
Yanqi Liu ◽  
Siyi Hu ◽  
Jun Ma ◽  
...  
Keyword(s):  
Single Chain ◽  
Purification And Characterization

scholarly journals Development and Characterization of Nanobodies Targeting the Kupffer Cell

2021 ◽  
Vol 12 ◽  
Author(s):  
Fang Zheng ◽  
Jinhong Zhou ◽  
Zhenlin Ouyang ◽  
Jiaxin Zhang ◽  
Xinyi Wang ◽  
...  
Keyword(s):  
Kupffer Cell ◽  
Cell Receptor ◽  
Therapeutic Agents ◽  
Membrane Receptors ◽  
Single Chain ◽  
Single Chain Antibodies ◽  
Functional Investigation ◽  
And Function ◽  
Distinct Features

Nanobodies that are derived from single-chain antibodies of camelids have served as powerful tools in diagnostics, therapeutics and investigation of membrane receptors' structure and function. In this study, we developed a series of nanobodies by a phage display screening building from lymphocytes isolated from an alpaca immunized with recombinant mouse Kupffer cell receptor Clec4F, which is involved in pathogen recognition by binding to galactose and N-acetylgalactosamine. Bio-panning selections retrieved 14 different nanobodies against Clec4F with an affinity ranging from 0.2 to 2 nM as determined by SPR. Those nanobodies mainly recognize 4 different epitopes as analyzed via competitive epitope binning. By analysis of the radioactivity in each organ after injection of 99mTc labeled Clec4F nanobodies in naïve mice, we found that these nanobodies are targeting the liver. Furthermore, we performed a structural characterization at atomic resolution of two of the Clec4F nanobodies from different epitope groups, which revealed distinct features within the CDR2 and CDR3 regions. Taken together, we developed a series of nanobodies targeting multiple distinct recognition epitopes of the Kupffer cell-specific receptor Clec4F which may be useful for its structural and functional investigation as well as for use as molecular imaging and therapeutic agents.

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