Sample preparation for N-glycosylation analysis of therapeutic monoclonal antibodies by electrophoresis
The result's identifiers
Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F15%3A00082381" target="_blank" >RIV/00216224:14740/15:00082381 - isvavai.cz</a>
Alternative codes found
RIV/68081715:_____/15:00444012
Result on the web
<a href="https://link.springer.com/protocol/10.1007%2F978-1-4939-2353-3_16" target="_blank" >https://link.springer.com/protocol/10.1007%2F978-1-4939-2353-3_16</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1007/978-1-4939-2353-3_16" target="_blank" >10.1007/978-1-4939-2353-3_16</a>
Alternative languages
Result language
angličtina
Original language name
Sample preparation for N-glycosylation analysis of therapeutic monoclonal antibodies by electrophoresis
Original language description
There are a considerable number of biopharmaceuticals that have been approved for clinical use in the past decade. Over half of these new generation drugs are glycoproteins, such as monoclonal antibodies or other recombinant glycoproteins, which are mostly produced in mammalian cell lines. The linked carbohydrate moieties affect not only their physicochemical properties and thermal stability but also crucial features like receptor-binding activity, circulating half-life, as well as immunogenicity. The structural diversity of these attached glycans can be manifested in altered monosaccharide composition and linkages/positions among the monosaccharide building blocks. In addition, as more and more biosimilar products hit the market, understanding the effects of their glycosylation modification has become a recent target in efficacy and safety issues. To ensure consistent quality of these products, glycosylation profiles have to be monitored and controlled in all steps of the manufacturin
Czech name
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Czech description
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Classification
Type
C - Chapter in a specialist book
CEP classification
CB - Analytical chemistry, separation
OECD FORD branch
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Result continuities
Project
<a href="/en/project/GAP301%2F11%2F2055" target="_blank" >GAP301/11/2055: New methods of analysis of proteins and their glycosylation in cancer - combination of electrochemistry, microfludic biosensors and mass spectrometry.</a><br>
Continuities
I - Institucionalni podpora na dlouhodoby koncepcni rozvoj vyzkumne organizace
Others
Publication year
2015
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů
Data specific for result type
Book/collection name
Methods in Molecular Biology
ISBN
9781493923526
Number of pages of the result
13
Pages from-to
183-195
Number of pages of the book
200
Publisher name
Springer Science+Business Media
Place of publication
NEW YORK
UT code for WoS chapter
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