2007•Chinese Journal of Disease Control and PreventionRequires access
Secretory expression of human soluble TALL-1 in Pichia pastoris
Cheng Tian-mi
Open publisher page 0 citations
Abstract
Objective To study the secretory expression of human soluble TALL-1 in Pichia pastoris.Methods The human sTALL-1 cDNA was cloned into yeast expression vector pPIC9K containing AOXI promoter and the sequences of secreting signal peptides.Recombinant plasmid was lined by Sac I and transformed into Pichia Pastoris GS115.Positive integrated clones were screened and cultured in flasks,and sTALL-1 was expressed under the induction of 1% methanol.Results Recombinant expression plasmid pPIC9K-sTALL-1 was successfully constructed.The human sTALL-1 was expressed in BMMY after optimization of inducing expression condition.Western blot and ELISA assay revealed recombinant products could combine with specific antibody.The expressed product could inhibit the proliferation of Hela cells by MTT assay.Conclusions The secretory expression of human sTALL-1 had been successfully achieved in Pichia pastoris expression system.