Expression and purification of soluble non-fusion vasostatin in Escherichia coli.
Vasostatin has previously been expressed in fused form or in inclusion body form in Escherichia coli. Here the protein was expressed in soluble non-fusion form in BL21(DE3)pLysS by IPTG induction. The expression level of vasostatin was about 15% of the total cellular protein. The expressed vasostatin was purified and its biological activity was investigated by an endothelial cell proliferation assay.
Wu
Xiaoping
X
Biopharmaceutical Research & Development Center, Pharmacy College, Jinan University, Guangzhou 510632, P. R. China.
Li
Xiaokun
X
Su
Zhijian
Z
Zheng
Qing
Q
Xu
Hua
H
Wu
Sixian
S
Feng
Ya
Y
Zhao
Wen
W
D037282:Calreticulin / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism* / Q000494:pharmacology; D002460:Cell Line; D049109:Cell Proliferation / Q000187:drug effects; D042783:Endothelial Cells / Q000187:drug effects; D004926:Escherichia coli / Q000235:genetics*; D015870:Gene Expression / Q000235:genetics*; D010446:Peptide Fragments / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism* / Q000494:pharmacology; D011994:Recombinant Proteins / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism / Q000494:pharmacology; D012995:Solubility
D037282:Calreticulin; D010446:Peptide Fragments; D011994:Recombinant Proteins; C121986:vasostatin