ED 50 < 0.2 ng/ml, measured by a cell differentiation assay using TF-I cells, corresponding to a specific activity of > 5.0 × 10 6 units/mg.

LIF Protein, Human, Recombinant (E. coli) is expressed in E. coli. The accession number is P15018.

Human

E. coli

MLPLI,Melanoma-derived LPL inhibitor,Leukemia inhibitory factor,HILDA,Emfilermin,Differentiation- stimulating factor,DIA,D-FACTOR,D factor,CDF

Ser23-Phe202

> 95% as determined by SDS-PAGE

Reconstitute the lyophilized protein in sterile deionized water. The product concentration should not be less than 100 μg/ml. Before opening, centrifuge the tube to collect powder at the bottom. After adding the reconstitution buffer, avoid vortexing or pipetting for mixing.

Upon receiving, this product remains stable for up to 6 months at lower than -70°C. Upon reconstitution, the product should be stable for up to 1 week at 4°C or up to 3 months at -20°C. For long term storage it is recommended that a carrier protein (example 0.1% BSA) be added. Avoid repeated freeze-thaw cycles.

Leukemia Inhibitory Factor (LIF) is a pleiotropic cytokine belonging to the long four-helix bundle cytokine superfamily. LIF shares tertiary structure with several other cytokines, including Interleukin-6 (IL-6), Oncostatin M, ciliary neurotropic factor, and cardiotrophin-1, and their functions in vivo are also redundant to some extent. LIF can bind to the common receptor of IL-6 subfamily, gp130, and then recruit its own receptor LIF Receptor to form a ternary complex. The basal expression of LIF in vivo is low; and its expression is induced by pro-inflammatory factors, including lipopolysaccharide, IL-1, and IL-17, and inhibited by anti-inflammatory agents, including IL-4 and IL-13. The functions of LIF include proliferation of primordial germ cells, regulation in blastocyst implantation and early pregnancy, and maintenance of pluripotent embryonic stem cells.