Abstract
Correction: Soluble Expression of Human Leukemia Inhibitory Factor with Protein Disulfide Isomerase in Escherichia coli and Its Simple Purification
Highlights
Human leukemia inhibitory factor, known as differentiation-stimulating factor (D factor) or melanoma-derived LPL inhibitor (MLPLI), is a cytokine that demonstrates multiple effects on cells, human physiology, and disease [1,2]. hLIF is absolutely required for maintaining the stemness of embryonic stem cell (ESC) lines [3,4,5,6]
The genes for hLIF and protein disulfide isomerase (PDI) were codon optimized for E. coli expression and synthesized (Figure S1 in File SI)
The PDIb'a' tag increased the solubility of the tagged hLIF by almost 2-fold
Summary
Human leukemia inhibitory factor (hLIF), known as differentiation-stimulating factor (D factor) or melanoma-derived LPL inhibitor (MLPLI), is a cytokine that demonstrates multiple effects on cells, human physiology, and disease [1,2]. hLIF is absolutely required for maintaining the stemness of embryonic stem cell (ESC) lines [3,4,5,6]. The expression of LIF in eukaryotic cells has been reported [13,14], the yields are low. In many cases the overall yield of biologically active protein from IBs is low [16]. Glutathione S-transferase (GST) and thioredoxin (Trx) have been reported either as tagged or independently expressed proteins to aid solubility and improve yields. These methods suffer from other issues, such as the tag was not removed or the levels of endotoxin were high or not tested, which are important considerations for maintaining biological activity in vivo [17,18,19,20,21]
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