Site-directed Protein Labeling
Proteins with unique functional groups such as affinity labels, fluorescence moieties or drug conjugates offer high potential in many biotechnological or biomedical applications.
An attractive alternative to known conventional posttranslational methods of protein modification is the site-directed incorporation of unnatural amino acids. In a specialized cell-free system, amino acids labeled with dyes or chemoselective reactive amino acids are incorporated stoichiometrically at defined positions of the expressed protein. Such homogenous site specific-modified proteins are the basis for a broad range of downstream applications.
Stoichiometric incorporation of dyes, PEG or other functionality
Labeling with a broad range of commercially available chemoselective reagents
- Efficient incorporation of chemoselective reactive amino acids
- High-yield synthesis of proteins with unnatural amino acids
- No protein purification necessary prior to labeling
- Minimal change of native protein structure
- Stoichiometric incorporation (1 label per 1 protein)
- Amber suppression-based expansion of the genetic code
- Synthesis of proteins containing a site specifically incorporated chemoselective reactive amino acid
- Site-directed incorporation of dyes, PEG or other labels
- Labeling with commercially available reagents
- Labeled proteins for fluorescence-based applications such as microscale thermophoresis
Starting at: €870.00
Does not include applicable tax, shipping & handling, or other charges.