Adding value to fusion proteins through covalent labeling
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Recent advances in genomics, proteomics, and structural biology raised the general need for significant amounts of pure recombinant protein (r-protein). Because of the difficulty in obtaining in some cases proper protein folding in bacteria, several method ...
A general method for covalent labeling of fusion proteins in vivo that complements the existing methods for protein labeling in vivo and in vitro is presented. This new method might lead to new ways of studying and manipulating proteins in living cells. Co ...
A method using O-alkylguanine-DNA alkyltransferases (AGT) is disclosed for transferring a label from a substrate to a fusion protein comprising the AGT. This allows the detection and/or manipulating of the fusion protein, both in vitro and in vivo, by a ...
With the human genome and many other eukaryotic and procaryotic genomes sequenced, the interest in life sciences is shifting towards the examination of the function, modification and regulation of the encoded proteins. Proteins are involved in virtually al ...
The present invention relates to methods of transferring a label from suitable substrates to O6-alkylguanine-DNA alkyltransferase (AGT) fusion proteins, to suitable fusion proteins, to suitable variants of AGT, and to novel labeled fusion proteins obtained ...
(Ecole Polytechnique Federale de Lausanne (EPFL), Switz.).2004
O6-substituted guanine derivs. are described for use as substrates for O6-alkylguanine-DNA alkyltransferases (AGT) that can be used to label the enzyme or fusion proteins contg. it. Proteins of interest are incorporated into an AGT fusion protein, the AGT ...
(Ecole Polytechnique Federale de Lausanne (EPFL), Switz.).2004
Cultivated mammalian cells have become the dominant system for the production of recombinant proteins for clinical applications because of their capacity for proper protein folding, assembly and post-translational modification. Thus, the quality and effica ...
The specific and covalent labeling of fusion proteins with synthetic mols. opens up new ways to study protein function in the living cell. Here the authors present a novel method that allows for the specific and exclusive extracellular labeling of proteins ...
Recently the sequencing project of the human genome has been completed. The interest of the post-sequencing-era is shifting nowadays towards the investigation of the biological function and localization of the encoded proteins. Proteins are essential parts ...
Site-specific protein labeling with synthetic dyes is an emerging technique for live cell imaging. A protein or peptide tag fused to the protein of interest provides the means for attachment of a fluorophore or other small molecule probe, to allow non-inva ...