scholarly journals Use of Recombinant Fusion Proteins in a Fluorescent Protease Assay Platform and Their In-gel Renaturation

10.3791/58824 ◽  
2019 ◽  
Author(s):  
Beáta Bozóki ◽  
János András Mótyán ◽  
Márió Miczi ◽  
Lívia Diána Gazda ◽  
József Tőzsér
Keyword(s):  
Fusion Proteins ◽  
Recombinant Fusion Proteins ◽  
Protease Assay

Use of recombinant fusion proteins for generation and rapid characterization of monoclonal antibodies

1992 ◽  
Vol 147 (1) ◽  
pp. 1-11 ◽  
Author(s):  
D. Wunderlich ◽  
A. Lee ◽  
R.P. Fracasso ◽  
D.V. Mierz ◽  
R.M. Bayney ◽  
...  
Keyword(s):  
Monoclonal Antibodies ◽  
Fusion Proteins ◽  
Recombinant Fusion Proteins ◽  
Rapid Characterization

scholarly journals New Opportunities in Glycan Engineering for Therapeutic Proteins

Antibodies ◽  
2022 ◽  
Vol 11 (1) ◽  
pp. 5
Author(s):  
Xiaotian Zhong ◽  
Aaron M. D’Antona ◽  
John J. Scarcelli ◽  
Jason C. Rouse
Keyword(s):  
Fusion Proteins ◽  
Therapeutic Proteins ◽  
Quality Attributes ◽  
Efficacy And Safety ◽  
Biological Functions ◽  
Next Generation ◽  
Lysosomal Degradation ◽  
Critical Quality Attributes ◽  
Recombinant Fusion Proteins ◽  
Antibody Diversification

Glycans as sugar polymers are important metabolic, structural, and physiological regulators for cellular and biological functions. They are often classified as critical quality attributes to antibodies and recombinant fusion proteins, given their impacts on the efficacy and safety of biologics drugs. Recent reports on the conjugates of N-acetyl-galactosamine and mannose-6-phosphate for lysosomal degradation, Fab glycans for antibody diversification, as well as sialylation therapeutic modulations and O-linked applications, have been fueling the continued interest in glycoengineering. The current advancements of the human glycome and the development of a comprehensive network in glycosylation pathways have presented new opportunities in designing next-generation therapeutic proteins.

Tag Removal by Site-Specific Cleavage of Recombinant Fusion Proteins

2010 ◽  
pp. 349-367 ◽  
Author(s):  
Adam Charlton ◽  
Michael Zachariou
Keyword(s):  
Fusion Proteins ◽  
Site Specific ◽  
Recombinant Fusion Proteins

Glucose Dehydrogenase as Detector Protein of Recombinant Fusion-Proteins Directly in SDS Gels

2001 ◽  
pp. 66-68
Author(s):  
Christa Burger ◽  
Winfried Linxweiler ◽  
Oliver Pöschke ◽  
Andrea Wolf ◽  
Uwe Hofmann ◽  
...  
Keyword(s):  
Fusion Proteins ◽  
Glucose Dehydrogenase ◽  
Recombinant Fusion Proteins

Exploration of Recombinant Fusion Proteins YAPO and YAPL as Carrier Proteins for Glycoconjugate Vaccine Design against Streptococcus pneumoniae Infection

2020 ◽  
Vol 6 (8) ◽  
pp. 2181-2191
Author(s):  
Shaojie Feng ◽  
Chenghe Xiong ◽  
Guirong Wang ◽  
Subo Wang ◽  
Guoxia Jin ◽  
...  
Keyword(s):  
Streptococcus Pneumoniae ◽  
Fusion Proteins ◽  
Vaccine Design ◽  
Carrier Proteins ◽  
Recombinant Fusion Proteins ◽  
Glycoconjugate Vaccine

scholarly journals Three-in-One Chromatography-Free Purification, Tag Removal, and Site-Specific Modification of Recombinant Fusion Proteins Using Sortase A and Elastin-like Polypeptides

2013 ◽  
Vol 52 (13) ◽  
pp. 3703-3708 ◽  
Author(s):  
Joseph J. Bellucci ◽  
Miriam Amiram ◽  
Jayanta Bhattacharyya ◽  
Dewey McCafferty ◽  
Ashutosh Chilkoti
Keyword(s):  
Fusion Proteins ◽  
Sortase A ◽  
Site Specific ◽  
Specific Modification ◽  
Recombinant Fusion Proteins

Recombinant fusion proteins A and protein G with glutathione S-transferase as reporter molecules

1991 ◽  
Vol 136 (2) ◽  
pp. 211-219 ◽  
Author(s):  
Andrew M. Lew ◽  
Dianne J. Beck ◽  
Lynda M. Thomas
Keyword(s):  
Fusion Proteins ◽  
Protein G ◽  
Glutathione S Transferase ◽  
Recombinant Fusion Proteins

An ELISA sandwich capture assay for recombinant fusion proteins containing glutathione-S-transferase

1992 ◽  
Vol 156 (1) ◽  
pp. 101-105 ◽  
Author(s):  
Daniel U. Rabin ◽  
Rebecca Palmer-Crocker ◽  
Diane V. Mierz ◽  
Kwok K. Yeung
Keyword(s):  
Fusion Proteins ◽  
Glutathione S Transferase ◽  
Recombinant Fusion Proteins ◽  
Capture Assay
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