The Study of a Reshaping Anti-CD28 Heavy-chain Variable Domain(VH)Antibody with CDR Mutations
One gene with CDR mutations of the reshaping anti-CD28 heavy-chain variable domain(VH) antibodies, which had high antigen binding activity, was obtained from a phage library of the reshaping anti-CD28 heavy-chain variable domain(VH) antibodies. It's deduced amino acid sequence was most homologous as the acceptor human antibody FRs. To compare it's deduced amino acid sequence with the original mouse anti-human CD28 VH amino acid sequence, We found that there were a deletion mutation of Ala53 and a insertion mutation of Arg65a in CDR2; deletion mutations of Asp95,Lys96,Gly97,Tyr98 in CDR3; and deletion mutations of Lys82a,Ser82b,Leu82c in FR3. Because there were many mutations in this gene, a further study was carried out. It was co-expressed with c-myc tag and the hinge region of human IgG3'CL gene in E.coli. BL21, and the results of ELISA showed that antigen binding activity of the refolding fusion protein was still kept in a high level.
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NSTL
万方数据
维普
