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

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

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 125 (13) ◽  
pp. 3791-3796 ◽  
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

scholarly journals Introduction of spacer peptides N-terminal to a cleavage recognition motif in recombinant fusion proteins can improve site-specific cleavage

1997 ◽  
Vol 10 (6) ◽  
pp. 615-619 ◽  
Author(s):  
S. W. Polyak ◽  
G. Forsberg ◽  
B. E. Forbes ◽  
K. A. McNeil ◽  
S. E. Aplin ◽  
...  
Keyword(s):  
Fusion Proteins ◽  
Site Specific ◽  
Recombinant Fusion Proteins ◽  
Recognition Motif

[19] Production of site-specific P450 antibodies using recombinant fusion proteins as antigens

1991 ◽  
pp. 193-201 ◽  
Author(s):  
Thomas Friedberg ◽  
Wolfgang Kissel ◽  
Michael Arand ◽  
Franz Oesch
Keyword(s):  
Fusion Proteins ◽  
Site Specific ◽  
Recombinant Fusion Proteins

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.

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

scholarly journals Enhancing site-specific DNA integration by a Cas9 nuclease fused with a DNA donor-binding domain

2020 ◽  
Vol 48 (18) ◽  
pp. 10590-10601
Author(s):  
Shufeng Ma ◽  
Xinlong Wang ◽  
Yongfei Hu ◽  
Jie Lv ◽  
Chengfang Liu ◽  
...  
Keyword(s):  
Fusion Proteins ◽  
Sleeping Beauty ◽  
Binding Domain ◽  
Protein Fusion ◽  
Site Specific ◽  
Dna Integration ◽  
Cas9 Nuclease ◽  
Human T Cells ◽  
Dna Insertion ◽  
Aavs1 Locus

Abstract The CRISPR/Cas system is widely used for genome editing. However, robust and targeted insertion of a DNA segment remains a challenge. Here, we present a fusion nuclease (Cas9-N57) to enhance site-specific DNA integration via a fused DNA binding domain of Sleeping Beauty transposase to tether the DNA segment to the Cas9/sgRNA complex. The insertion was unidirectional and specific, and DNA fragments up to 12 kb in length were successfully integrated. As a test of the system, Cas9-N57 mediated the insertion of a CD19-specific chimeric antigen receptor (CD19-CAR) cassette into the AAVS1 locus in human T cells, and induced intrahepatic cholangiocarcinoma in mice by simultaneously mediating the insertion of oncogenic KrasG12D into the Rosa26 locus and disrupting Trp53 and Pten. Moreover, the nuclease-N57 fusion proteins based on AsCpf1 (AsCas12a) and CjCas9 exhibited similar activity. These findings demonstrate that CRISPR-associated nuclease-N57 protein fusion is a powerful tool for targeted DNA insertion and holds great potential for gene therapy applications.

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