6,589 Views
•
11:25 min
•
October 04, 2017
DOI:
Podsumowanie
Automatically generated
Biochemical and structural analyses of glycosylated proteins require relatively large amounts of homogeneous samples. Here, we present an efficient chemical method for site-specific glycosylation of recombinant proteins purified from bacteria by targeting reactive Cys thiols.
Powiązane Filmy
09:14
Synthesis of Protein Bioconjugates via Cysteine-maleimide Chemistry
Powiązane Filmy
38540 Views
08:58
Characterization of Glycoproteins with the Immunoglobulin Fold by X-Ray Crystallography and Biophysical Techniques
Powiązane Filmy
12597 Views
08:47
Synthesis and Bioconjugation of Thiol-Reactive Reagents for the Creation of Site-Selectively Modified Immunoconjugates
Powiązane Filmy
9373 Views
N/A
Preparation of Site-Specific Cytotoxic Protein Conjugates via Maleimide-thiol Chemistry and Sortase A-Mediated Ligation
Powiązane Filmy
1847 Views
07:16
Resin-Assisted Capture Coupled with Isobaric Tandem Mass Tag Labeling for Multiplexed Quantification of Protein Thiol Oxidation
Powiązane Filmy
1680 Views
11:55
Examining the Conformational Dynamics of Membrane Proteins in situ with Site-directed Fluorescence Labeling
Powiązane Filmy
15018 Views
13:53
Homogeneous Glycoconjugate Produced by Combined Unnatural Amino Acid Incorporation and Click-Chemistry for Vaccine Purposes
Powiązane Filmy
4950 Views
13:21
Chemically-blocked Antibody Microarray for Multiplexed High-throughput Profiling of Specific Protein Glycosylation in Complex Samples
Powiązane Filmy
15690 Views
10:31
Residue-Specific Exchange of Proline by Proline Analogs in Fluorescent Proteins: How "Molecular Surgery" of the Backbone Affects Folding and Stability
Powiązane Filmy
2908 Views
06:53
Rapid Antibody Glycoengineering in Chinese Hamster Ovary Cells
Powiązane Filmy
3139 Views
Read Article
Cytuj ten artykuł
Choi, Y. J., Zhu, J., Chung, S., Siddiqui, N., Feng, Q., Stathopulos, P. B. Targeting Cysteine Thiols for in Vitro Site-specific Glycosylation of Recombinant Proteins. J. Vis. Exp. (128), e56302, doi:10.3791/56302 (2017).
Copy