[High-level expression of human vascular endothelial growth factor in Pichia pastoris].
The gene of VEGF165 was subcloned into the P. pastoris secretive expression vector pHIL-S1 and the recombinant expression plasmid pHIL-S1-VEGF165 was constructed. After transformation into yeast GS115, the positive transformants were obtained through phenotype selection and DNA Dot blotting. After induction by methanol, soluble dimer VEGF165 were expressed and secreted into the culture supernatant with its expression occupying 47% of the total protein in the supernatant. Dot blot analysis showed that the expressed human VEGF165 could bind to its receptors flt-1 and KDR.
Yan
X Y
XY
State Key Laboratory of Microbial Resources, Chinese Academy of Sciences Beijing.
Tang
J
J
Huang
Y H
YH
D016228:Endothelial Growth Factors / Q000096:biosynthesis*; D006801:Humans; D008222:Lymphokines / Q000096:biosynthesis*; D010843:Pichia / Q000235:genetics*; D010957:Plasmids; D011994:Recombinant Proteins / Q000096:biosynthesis*; D042461:Vascular Endothelial Growth Factor A; D042442:Vascular Endothelial Growth Factors
D016228:Endothelial Growth Factors; D008222:Lymphokines; D011994:Recombinant Proteins; C467484:VEGFA protein, human; D042461:Vascular Endothelial Growth Factor A; D042442:Vascular Endothelial Growth Factors