Production of N-acetylgalactosaminyl-transferase 2 (GalNAc-T2) fused with secretory signal Igkappa in insect cells

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F61989592%3A15110%2F12%3A10224923" target="_blank" >RIV/61989592:15110/12:10224923 - isvavai.cz</a>
Result on the web
<a href="http://dx.doi.org/10.1016/j.pep.2011.10.006" target="_blank" >http://dx.doi.org/10.1016/j.pep.2011.10.006</a>
DOI - Digital Object Identifier
<a href="http://dx.doi.org/10.1016/j.pep.2011.10.006" target="_blank" >10.1016/j.pep.2011.10.006</a>

Result language
angličtina
Original language name
Production of N-acetylgalactosaminyl-transferase 2 (GalNAc-T2) fused with secretory signal Igkappa in insect cells
Original language description
The human UDP-N-acetyl-alfa-d-galactosamine:polypeptide N-acetylgalactosaminyl-transferase 2 (GalNAc-T2) is one of the key enzymes that initiate synthesis of hinge-region O-linked glycans of human immunoglobulin A1 (IgA1). We designed secreted soluble form of human GalNAc-T2 as a fusion protein containing mouse immunoglobulin light chain kappa secretory signal and expressed it using baculovirus and mammalian expression vectors. The recombinant protein was secreted by insect cells Sf9 and human HEK 293Tcells in the culture medium. The protein was purified from the media using affinity Ni-NTA chromatography followed by stabilization of purified protein in 50. mM Tris-HCl buffer at pH 7.4.
Czech name
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Czech description
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Type
J<sub>x</sub> - Unclassified - Peer-reviewed scientific article (Jimp, Jsc and Jost)
CEP classification
EC - Immunology
OECD FORD branch
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Project
Result was created during the realization of more than one project. More information in the Projects tab.
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)<br>Z - Vyzkumny zamer (s odkazem do CEZ)

Publication year
2012
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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