| Autor: |
Bernard, A., Griffiths, B., Noé, W., Wurm, F., Kunert, R., Steinfellner, W., Assadian, A., Katinger, H. |
| Zdroj: |
Animal Cell Technology: Products from Cells, Cells as Products; 2000, p397-399, 3p |
| Abstrakt: |
The human monoclonal antibody 2F5 (Buchacher et al., 1994) is a potent candidate for immunotherapy of HIV-1 (Katinger et al., 1995). The hybridoma derived humAb is of IgG3 kappa isotype. Since the IgGl isotype has a longer half-life in human than IgG3, we switched the subclass-type to IgGl by ligation of the 2F5 heavy chain variable region to an IgGl constant region and expressed the IgGl kappa molecule in CHO-cells. Stable recombinant 2F5-IgGl expressing CHO-cells were isolated and the recombinant protein compared to the hybridoma derived immunoglobulin. Here we confirm, that specificity and affinity of different isotypes has not changed. Stability assays of the recombinant 2F5 IgGl clone were performed with and without selection pressure. [ABSTRACT FROM AUTHOR] |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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