[Cloning and expression of fusion gene of transmembrane domain of human CD20 and g3pN in Escherichia coli].
OBJECTIVE
To construct the expression vector containing transmembrane domain gene of human CD20 and g3pN1 gene and express the fusion gene high-efficiently in E.coli.


METHODS
The human CD20 gene and g3pN1 domain gene were amplified by RT-PCR and PCR from Daudi cells and M13K07 phage antibody library, respectively, and then cloned into expression vector pTIG-Trx. The constructed expression vector was expressed in E.coli.


RESULTS
Western blot analysis showed that expressed product could bind to anti-CD20 mAb.


CONCLUSIONS
The pTIG-GS has been constructed and expressed successfully in E.coli, which lays the foundation for further screening anti-CD20 antibody from phage antibody library.
Zhang
Xiao-yun
XY
Department of Biochemistry, Hebei North College, Zhangjiakou 075000, China. xyz700928@yahoo.com.cn
Sun
Zhi-wei
ZW
Yu
Wei-yuan
WY
Cheng
Jian-zhen
JZ
D018951:Antigens, CD20 / Q000096:biosynthesis / Q000235:genetics*; D002051:Burkitt Lymphoma / Q000473:pathology; D003001:Cloning, Molecular; D018076:DNA, Complementary / Q000235:genetics; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism*; D005822:Genetic Vectors; D006801:Humans; D019151:Peptide Library; D011993:Recombinant Fusion Proteins / Q000096:biosynthesis / Q000235:genetics; D014407:Tumor Cells, Cultured
D018951:Antigens, CD20; D018076:DNA, Complementary; D019151:Peptide Library; D011993:Recombinant Fusion Proteins