LIF Recombinant Protein Cat. No.: 40-684

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psi-iconSpecifications
SPECIES:Human, Mouse, Rat
SOURCE SPECIES:E. coli
SEQUENCE:SPLPITPVNA TCAIRHPCHN NLMNQIRSQL AQLNGSANAL FILYYTAQGE PFPNNLDKLC GPNVTDFPPF HANGTEKAKL VELYRIVVYL GTSLGNITRD QKILNPSALS LHSKLNATAD ILRGLLSNVL CRLCSKYHVG HVDVTYGPDT SGKDVFQKKK LGCQLLGKYK QIIAVLAQAF
BIOLOGICAL ACTIVITY: 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.
psi-iconProperties
PURITY:≥ 98% by SDS-PAGE gel and HPLC analyses.
PHYSICAL STATE:Lyophilized
STORAGE CONDITIONS:The recombinant protein is stable for at least 2 years from date of receipt at -20˚C. Reconstituted protein is stable for at least 3 months when stored in working aliquots with a carrier protein at -20˚C. As with any protein, exposing the recombinant protein to repeated freeze / thaw cycles is not recommended. When working with proteins care should be taken to keep recombinant protein at a cool and stable temperature.
psi-iconAdditional Info
ALTERNATE NAMES:Leukemia Inhibitory Factor, Differentiation-stimulating factor, D factor, Melanoma-derived LPL inhibitor (MLPLI), Interleukin 6 family cytokine
OFFICIAL SYMBOL:LIF
GENE ID:3976
psi-iconBackground and References
BACKGROUND: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.

FOR RESEARCH USE ONLY.

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