Marion michael nude

03-Aug-2020 04:06

We could confirm the physical interaction between endogenous and exogenous human TUSC3, respectively, and the STT3B (Figures 1a and b), the core catalytic protein of the complex, by co-immunoprecipitation in HEK293T cells.In contrast, STT3A did not co-immunoprecipitate with TUSC3 in these cells (data not shown).N-glycosylation is a ubiquitous posttranslational modification of eukaryotic proteins that modulates protein folding, protects them from degradation, and regulates their function as well as their immunogenicity.UPR then facilitates cellular adaptation to ER stress by several distinct mechanisms in order to modulate the crosstalk between autophagy and apoptosis, and its deregulation might thus further contribute to carcinogenesis.TUSC3 shares homologies with the yeast oligosaccharyltransferase (OST) complex subunit Ost3p, suggesting a role in protein glycosylation.

Ig G heavy chain (Ig G HC) represents the loading control. (b) HEK293T cells were transfected with TUSC3 or an empty control pc DNA 3.1 vector (V).

Lysates from transfected cells were immunoprecipitated using STT3B antibody or control Ig G and TUSC3 was detected using western blot.