Expression and Characterization of Recombinant Interleukin-21 Receptor and Its Targeting Single-Chain Variable Fragment Antibodies Selected from a Human Phage Display Library

2012 ◽  
Vol 31 (10) ◽  
pp. 1541-1548 ◽  
Author(s):  
Qinhang Wu ◽  
Juan Zhang ◽  
Chen Luo ◽  
Tao Zhang ◽  
Tong Wang ◽  
...  
Keyword(s):  
Phage Display ◽  
Phage Display Library ◽  
Single Chain Variable Fragment ◽  
Single Chain ◽  
Interleukin 21

Single chain variable fragment antibodies against Shiga toxins isolated from a human antibody phage display library

Vaccine ◽  
2011 ◽  
Vol 29 (33) ◽  
pp. 5340-5346 ◽  
Author(s):  
Paola Neri ◽  
Naoko Shigemori ◽  
Susumu Hamada-Tsutsumi ◽  
Kentaro Tsukamoto ◽  
Hideyuki Arimitsu ◽  
...  
Keyword(s):  
Phage Display ◽  
Phage Display Library ◽  
Human Antibody ◽  
Single Chain Variable Fragment ◽  
Single Chain ◽  
Shiga Toxins ◽  
Antibody Phage ◽  
Antibody Phage Display

scholarly journals Selection of Single-Chain Variable Fragment Antibodies to Black Currant Reversion Associated Virus from a Synthetic Phage Display Library

1998 ◽  
Vol 88 (3) ◽  
pp. 230-233 ◽  
Author(s):  
Petri Susi ◽  
Angelika Ziegler ◽  
Lesley Torrance
Keyword(s):  
Alkaline Phosphatase ◽  
Phage Display ◽  
Plant Extracts ◽  
Fusion Proteins ◽  
Phage Display Library ◽  
Antibody Fragments ◽  
Healthy Plant ◽  
Single Chain Variable Fragment ◽  
Single Chain ◽  
Black Currant

Single-chain variable fragment (scFv) antibodies that bind to black currant reversion associated virus (BRAV) were obtained from a synthetic phage display antibody gene library without recourse to animal immunizations. Several different BRAV-specific phage scFv were obtained quickly, after only three rounds of selection against immobilized virus antigen. The phage scFv gave enzyme-linked immunosorbent assay (ELISA) absorbance values that were greater than seven times the control healthy plant extracts. In contrast, comparative tests using a rabbit antiserum failed, because unacceptably high background values were obtained with healthy plant extracts. Two of the scFv were subcloned into the pDAP2 vector for the rapid and efficient production of scFv-alkaline phosphatase fusion proteins. Functional fusion proteins were obtained after expression in Escherichia coli, and preparations from periplasmic extracts detected BRAV in ELISA. The results demonstrate that antibody fragments obtained from a synthetic phage display library are useful research tools, and they proved to be a viable practical alternative when traditional antisera failed to detect BRAV, a weak immunogen. Furthermore, the genetic fusion of antibody fragments to alkaline phosphatase obviates the need for further chemical coupling procedures, and the fusion proteins can be obtained cheaply.

Isoenzyme-directed selection and characterization of anti-creatine kinase single chain Fv antibodies from a human phage display library

2002 ◽  
Vol 1579 (2-3) ◽  
pp. 124-132 ◽  
Author(s):  
Uwe Schlattner ◽  
Christof Reinhart ◽  
Thorsten Hornemann ◽  
Malgorzata Tokarska-Schlattner ◽  
Theo Wallimann
Keyword(s):  
Creatine Kinase ◽  
Phage Display ◽  
Phage Display Library ◽  
Single Chain ◽  
Single Chain Fv

scholarly journals Isolation of a novel Anti-KDR3 Single-chain Variable Fragment Antibody from a Phage Display Library

2019 ◽  
Author(s):  
Shirafkan Kordi ◽  
Mohammad Rahmati-Yamchi ◽  
Mehdi Asghari Vostakolaei ◽  
Ali Etemadie ◽  
Abolfazl Barzegari ◽  
...  
Keyword(s):  
Phage Display ◽  
Growth Factor Receptor ◽  
Phage Display Library ◽  
Vital Role ◽  
Scfv Antibody ◽  
Single Chain Variable Fragment ◽  
Single Chain ◽  
Phage Display Technology ◽  
Display Technology ◽  
Domain 3

Vascular endothelial growth factor receptor 2 (VEGFR-2) is known as one of the important antigens playing a vital role in angiogenesis. In this study, phage display technology (PDT) was used to produce a single-chain variable fragment (scFv) antibody against a region of the domain 3 in VEGFR-2 called kinase insert domain receptor 3 (KDR3). After designing the KDR3 peptide and biopanning, a colony was chosen for scFv antibody expression. Following expression and purification; western blotting, dot blotting and immunofluorescence (IF) were used to evaluate the antibody function. Surface plasmon resonance (SPR) was also employed to measure affinity of produced antibody. Once a colony was selected and transferred to the expression host, the scFv antibody was expressed in the expected range of 28 kDa. Using a designed chromatography column, antibody purification was found to be about 95%. In this study, a novel scFv with the capability of binding to KDR3 was isolated and purified and its intracellular function was investigated and verified.

Selection of single chain variable fragment (scFv) antibodies from a hyperimmunized phage display library for the detection of the antibiotic monensin

2010 ◽  
Vol 360 (1-2) ◽  
pp. 103-118 ◽  
Author(s):  
Shokouh Makvandi-Nejad ◽  
Claudia Sheedy ◽  
Linda Veldhuis ◽  
Gabrielle Richard ◽  
J. Christopher Hall
Keyword(s):  
Phage Display ◽  
Phage Display Library ◽  
Single Chain Variable Fragment ◽  
Single Chain ◽  
Selection Of
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