Human LIF is a glycoprotein with a molecular weight of approximately 19.7 kDa, consisting of 181 amino acid residues . The recombinant form of LIF is often expressed in Escherichia coli (E. coli) as a fusion protein with Glutathione S-transferase (GST) using the pGEX expression system . This fusion protein is then cleaved from the GST moiety with thrombin and purified by High-Performance Liquid Chromatography (HPLC) .
LIF has a wide range of biological activities:
The activity of human LIF is determined by its ability to induce differentiation of M1 myeloid leukemic cells. The minimum detectable concentration of human LIF in this assay is 0.5 ng/mL, with a specific activity of greater than 1 x 10^8 units/mg . This makes LIF a valuable tool in both research and clinical settings, particularly in the fields of stem cell biology and cancer research.
The discovery of LIF dates back to 1969, when it was first described as a factor that could induce differentiation in murine myeloid leukemia cells . Over the years, LIF has been rediscovered and studied in various contexts, leading to a better understanding of its multifunctional roles in different biological systems .