LIF is a pleiotrophic factor produced by multiple cell types, including T cells, myelomonocytic lineages, fibroblasts, liver, heart and melanoma. LIF promotes long-term maintenance of embryonic stem cells by suppressing spontaneous differentiation. Other activities include the stimulation of acute phase protein synthesis by hepatocytes, stimulation of differentiation of cholinergic nerves, and suppression of adipogenesis by inhibiting the lipoprotein lipase in adipocytes. While human LIF is active on mouse cells and is widely used in the maintenance of murine ESC to prevent spontaneous differentiation, mouse LIF is not active on human cells due to its inability to bind to the human LIF receptor. Recombinant Human LIF is a 19.7 kDa protein containing 180 amino acid residues, including three disulfide bonds.
Leukemia Inhibitory Factor, Differentiation-stimulating factor, D factor, Melanoma-derived LPL inhibitor (MLPLI), Interleukin 6 family cytokine
SPLPITPVNA TCAIRHPCHN NLMNQIRSQL AQLNGSANAL FILYYTAQGE PFPNNLDKLC GPNVTDFPPF HANGTEKAKL VELYRIVVYL GTSLGNITRD QKILNPSALS LHSKLNATAD ILRGLLSNVL CRLCSKYHVG HVDVTYGPDT SGKDVFQKKK LGCQLLGKYK QIIAVLAQAF
≥ 98% by SDS-PAGE gel and HPLC analyses.
Determined by its ability to stimulate the proliferation of human TF-1 cells. The expected ED50 is ≤ 0.1 ng/ml, corresponding to a specific activity of ≥ 1 x 107 units/mg. This product has been tested against the WHO standard. International Unit information can be found here.
Calculated Molecular Weight:
Endotoxin level is < 0.1 ng/ug of protein (< 1 EU/ug)
Not for human use.