isopropyl-thiogalactoside and Lymphoma

isopropyl-thiogalactoside has been researched along with Lymphoma* in 1 studies

Other Studies

1 other study(ies) available for isopropyl-thiogalactoside and Lymphoma

Article	Year
High-level production and one-step purification of biologically active human growth hormone in Escherichia coli. Gene, 1995, Nov-20, Volume: 165, Issue:2 A plasmid has been constructed to direct the synthesis of recombinant human growth hormone (re-hGH) in Escherichia coli as a fusion protein containing a His6 tag at the N-terminus under the control of the T5 promoter. The re-hGH was synthesized in large amounts and accumulated in the form of inclusion bodies upon induction with IPTG. Inclusion bodies were solubilized in 6 M guanidine.HCl and the re-hGH was purified by single-step affinity chromatography on Ni(2+)-nitrilotriacetic acid (NTA) agarose. At the shake flask level, the purified re-hGH was obtained with a yield of 30 mg/l of culture. The re-hGH was biologically active in a node rat lymphoma (Nb2) cell bioassay. Topics: Animals; Chromatography, Affinity; DNA, Complementary; Escherichia coli; Gene Expression Regulation, Bacterial; Growth Hormone; Histidine; Humans; Inclusion Bodies; Isopropyl Thiogalactoside; Lymphoma; Mitogens; Peptides; Plasmids; Rats; Recombinant Fusion Proteins; Tumor Cells, Cultured	1995

Article

Year

High-level production and one-step purification of biologically active human growth hormone in Escherichia coli.

Gene, 1995, Nov-20, Volume: 165, Issue:2

A plasmid has been constructed to direct the synthesis of recombinant human growth hormone (re-hGH) in Escherichia coli as a fusion protein containing a His6 tag at the N-terminus under the control of the T5 promoter. The re-hGH was synthesized in large amounts and accumulated in the form of inclusion bodies upon induction with IPTG. Inclusion bodies were solubilized in 6 M guanidine.HCl and the re-hGH was purified by single-step affinity chromatography on Ni(2+)-nitrilotriacetic acid (NTA) agarose. At the shake flask level, the purified re-hGH was obtained with a yield of 30 mg/l of culture. The re-hGH was biologically active in a node rat lymphoma (Nb2) cell bioassay.

Topics: Animals; Chromatography, Affinity; DNA, Complementary; Escherichia coli; Gene Expression Regulation, Bacterial; Growth Hormone; Histidine; Humans; Inclusion Bodies; Isopropyl Thiogalactoside; Lymphoma; Mitogens; Peptides; Plasmids; Rats; Recombinant Fusion Proteins; Tumor Cells, Cultured

1995