Bacterial expression of a kemptide fusion protein facilitates 32P labeling of a humanized, anti-carcinoembryonic antigen (hMN-14) antibody fragment.
Leung, S O
Bacterial expression of a kemptide fusion protein facilitates 32P labeling of a humanized, anti-carcinoembryonic antigen (hMN-14) antibody fragment. [electronic resource] - Cancer research Dec 1995 - 5968s-5972s p. digital
Publication Type: Journal Article; Research Support, U.S. Gov't, P.H.S.
0008-5472
Amino Acid Sequence
Animals
Carcinoembryonic Antigen--immunology
Cattle
Escherichia coli--genetics
Gene Transfer Techniques
Immunoglobulin Fab Fragments--biosynthesis
Isotope Labeling--methods
Molecular Sequence Data
Oligopeptides--biosynthesis
Phosphorus Radioisotopes
Recombinant Fusion Proteins--biosynthesis
Bacterial expression of a kemptide fusion protein facilitates 32P labeling of a humanized, anti-carcinoembryonic antigen (hMN-14) antibody fragment. [electronic resource] - Cancer research Dec 1995 - 5968s-5972s p. digital
Publication Type: Journal Article; Research Support, U.S. Gov't, P.H.S.
0008-5472
Amino Acid Sequence
Animals
Carcinoembryonic Antigen--immunology
Cattle
Escherichia coli--genetics
Gene Transfer Techniques
Immunoglobulin Fab Fragments--biosynthesis
Isotope Labeling--methods
Molecular Sequence Data
Oligopeptides--biosynthesis
Phosphorus Radioisotopes
Recombinant Fusion Proteins--biosynthesis