Leukemia Inhibitory Factor (LIF) is a pleiotropic glycoprotein originally described to inhibit the proliferation of the murine myeloid leukemic cell line M1, while inducing differentiation into macrophages. Other activities were later identified to LIF, which is known by a variety of synonyms, including DIF, D-factor, DIA, DRF, CNDF, HILDA, HSF-III, and MLPLI. Human LIF exerts its actions through a receptor comprising a 190 kDa LIF-binding α-chain (130 kDa, mouse) and a 130 kDa signal-transducing β-chain (gp130), which is shared with CNTF, OSM, L-6 and IL-11. As such, it is a member of the gp130 family of the cytokine receptor superfamily. LIF receptors have been identified on several cells, including monocytes, liver, placenta and embryonic stem cells. Natural LIF is heavily glycosylated, showing an apparent molecular weight of 32 kDa to 62 kDa, depending on the source, but absence of glycosylation appears not to affect its biological activity. A single gene encodes LIF, which is secreted as a single chain glycoprotein containing 180 amino acids for human or mouse with a conserved disulfide bond. Human and mouse LIF share 78% sequence homology. Human LIF can activate mouse cells, but mouse LIF cannot activate human cells.
Leukemia Inhibitory Factor (LIF) Murine Recombinant produced in E.Coli is a single, non-glycosylated, polypeptide chain containing 181 amino acids and having a molecular mass of 20 kDa.
The Leukemia Inhibitory Factor (LIF) is purified by proprietary chromatographic techniques.
Leukemia Inhibitory Factor also called LIF is a lymphoid factor that promotes long-term maintenance of embryonic stem cells by suppressing spontaneous differentiation. Leukemia Inhibitory Factor has several functions such as cholinergic neuron differentiation, control of stem cell pluripotency, bone & fat metabolism, mitogenesis of factor dependent cell lines & promotion of megakaryocyte production in vivo. Human and mouse LIF exhibit a 78% identity in its amino acid sequence.
