scholarly journals Fusion of a recombinant antibody fragment with a homo-amino-acid polymer: effects on biophysical properties and prolonged plasma half-life

2007 ◽  
Vol 20 (6) ◽  
pp. 273-284 ◽  
Author(s):  
M. Schlapschy ◽  
I. Theobald ◽  
H. Mack ◽  
M. Schottelius ◽  
H.-J. Wester ◽  
...  
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Vol 85 (5) ◽  
pp. 463-474 ◽  
Author(s):  
Christina Chen ◽  
Brad Snedecor ◽  
Julie C. Nishihara ◽  
John C. Joly ◽  
Nancy McFarland ◽  
...  

2008 ◽  
Vol 153 (6) ◽  
pp. 1075-1084 ◽  
Author(s):  
Martin Orecchia ◽  
Greta Nölke ◽  
Pasquale Saldarelli ◽  
Mariangela Dell’Orco ◽  
Kerstin Uhde-Holzem ◽  
...  

PLoS ONE ◽  
2013 ◽  
Vol 8 (12) ◽  
pp. e83678 ◽  
Author(s):  
Claire Cunningham ◽  
Akshay Srivastava ◽  
Estelle Collin ◽  
Sibylle Grad ◽  
Mauro Alini ◽  
...  

Medicina ◽  
2021 ◽  
Vol 57 (9) ◽  
pp. 981
Author(s):  
Chang-Hun Yeom ◽  
Hee-Jin Jeong

Matrix metalloproteinase 9 (MMP9) is involved in several aspects of the pathology of cancer, including invasion, metastasis, and angiogenesis. In this study, we expressed a recombinant scFv-type anti-MMP9 antibody in soluble form using Escherichia coli, purified it, and confirmed its antigen-binding ability. The convenient, rapid, inexpressive system used in this study for producing recombinant antibody fragments needs only five days, and thus can be used for the efficient production of scFv against MMP9, which can be used in a range of applications and industrial fields, including diagnosis and treatment of inflammatory and cancer-related diseases.


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