Expression and Purification of a Bispecific Antibody against CD16 and Hemagglutinin Neuraminidase (HN) in
Bispecific Antibody
Escherichia Coli
Immunotherapy
Natural Killer Cell (NK Cell)
Newcastle Disease Virus (NDV)
Journal
Reports of biochemistry & molecular biology
ISSN: 2322-3480
Titre abrégé: Rep Biochem Mol Biol
Pays: Iran
ID NLM: 101637937
Informations de publication
Date de publication:
Apr 2020
Apr 2020
Historique:
entrez:
22
8
2020
pubmed:
22
8
2020
medline:
22
8
2020
Statut:
ppublish
Résumé
: Immunotherapy of cancer by bispecific antibodies (bsAb) is an attractive approach for retargeting immune effector cells including natural killer (NK) cells to the tumor if the proper expression and purification of the bsAb for such applications could be addressed. Herein, we describe A bsAb-encoding pcDNA3.1 vector (anti-HN scFv-Fc-anti-CD16 scFv) was used as a template, and the scFv segments (after enzymatic digestion and cutting of the Fc part) were rejoined to construct the Fc-deprived bsAb (anti-HN scFv-anti-CD16 scFv; bsHN-CD16). The constructed bsHN-CD16 was inserted into the Analyses by SDS-PAGE and Western Blotting using Rabbit anti-human whole IgG-HRP conjugate, confirmed the expression and purification of the bsAb with the expected full size of 55 kDa and yields around 8% of the total protein. Results showed efficient production of the bsAb in
Sections du résumé
BACKGROUND
BACKGROUND
: Immunotherapy of cancer by bispecific antibodies (bsAb) is an attractive approach for retargeting immune effector cells including natural killer (NK) cells to the tumor if the proper expression and purification of the bsAb for such applications could be addressed. Herein, we describe
METHODS
METHODS
A bsAb-encoding pcDNA3.1 vector (anti-HN scFv-Fc-anti-CD16 scFv) was used as a template, and the scFv segments (after enzymatic digestion and cutting of the Fc part) were rejoined to construct the Fc-deprived bsAb (anti-HN scFv-anti-CD16 scFv; bsHN-CD16). The constructed bsHN-CD16 was inserted into the
RESULTS
RESULTS
Analyses by SDS-PAGE and Western Blotting using Rabbit anti-human whole IgG-HRP conjugate, confirmed the expression and purification of the bsAb with the expected full size of 55 kDa and yields around 8% of the total protein.
CONCLUSION
CONCLUSIONS
Results showed efficient production of the bsAb in
Identifiants
pubmed: 32821751
doi: 10.29252/rbmb.9.1.50
pii: rbmb-9-058
pmc: PMC7424422
doi:
Types de publication
Journal Article
Langues
eng
Pagination
50-57Références
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