Expression and purification of fluorinated proteins from mammalian suspension culture.
Methods Enzymol
; 696: 341-354, 2024.
Article
in En
| MEDLINE
| ID: mdl-38658087
ABSTRACT
The site-specific encoding of noncanonical amino acids allows for the introduction of rationalized chemistry into a target protein. Of the methods that enable this technology, evolved tRNA and synthetase pairs offer the potential for expanded protein production and purification. Such an approach combines the versatility of solid-phase peptide synthesis with the scalable features of recombinant protein production. We describe the large scale production and purification of eukaryotic proteins bearing fluorinated phenylalanine in mammalian suspension cell preparations. Downstream applications of this approach include scalable recombinant protein preparation for ligand binding assays with small molecules and ligands, protein structure determination, and protein stability assays.
Key words
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Recombinant Proteins
/
Halogenation
Limits:
Animals
/
Humans
Language:
En
Journal:
Methods Enzymol
Year:
2024
Document type:
Article
Affiliation country:
United States
Country of publication:
United States