Ontology highlight
ABSTRACT:
SUBMITTER: O'Rourke SM
PROVIDER: S-EPMC7451022 | biostudies-literature | 2019 Dec
REPOSITORIES: biostudies-literature
O'Rourke Sara M SM Morozov Giora I GI Roberts Jacob T JT Barb Adam W AW Sgourakis Nikolaos G NG
Protein engineering, design & selection : PEDS 20191201 12
Current approaches for generating major histocompatibility complex (MHC) Class-I proteins with desired bound peptides (pMHC-I) for research, diagnostic and therapeutic applications are limited by the inherent instability of empty MHC-I molecules. Using the properties of the chaperone TAP-binding protein related (TAPBPR), we have developed a robust method to produce soluble, peptide-receptive MHC-I molecules in Chinese Hamster Ovary cells at high yield, completely bypassing the requirement for la ...[more]