LIF (human) (rec.)

AdipoGen Life Sciences

LIF (human) (rec.)

10

Research Use Only

>95%

Leukemia inhibitory factor

LIF has the capacity to induce terminal differentiation in leukemic cells. Its activities also include the induction of hematopoietic differentiation in normal and myeloid leukemia cells, the induction of neuronal cell differentiation and the stimulation of acute-phase protein synthesis in hepatocytes. LIF activates JAK & STAT signaling in human embryonic stem (ES) cells, but this pathway does not maintain pluripotency in these cells, which instead rely on FGF2-mediated ERK signaling. By contrast, mouse ES cells can be maintained by LIF-mediated JAK & STAT signaling. LIF binds to a high affinity heterodimeric receptor complex consisting of two proteins: LIF-R alpha that binds LIF with low affinity and the 130kDa (gp130) subunit that by itself does not bind LIF, but is required for high affinity binding of LIF. - Protein. Human LIF (aa 23-202) is fused at the N-terminus to a tag. Source: E. coli. Endotoxin content: <0.05EU/microg purified protein (LAL test; Lonza). Lyophilized. Contains PBS. Mouse and human embryonic stem cells. Purity: >95% (SDS-PAGE). LIF has the capacity to induce terminal differentiation in leukemic cells. Its activities also include the induction of hematopoietic differentiation in normal and myeloid leukemia cells, the induction of neuronal cell differentiation and the stimulation of acute-phase protein synthesis in hepatocytes. LIF activates JAK & STAT signaling in human embryonic stem (ES) cells, but this pathway does not maintain pluripotency in these cells, which instead rely on FGF2-mediated ERK signaling. By contrast, mouse ES cells can be maintained by LIF-mediated JAK & STAT signaling. LIF binds to a high affinity heterodimeric receptor complex consisting of two proteins: LIF-R alpha that binds LIF with low affinity and the 130kDa (gp130) subunit that by itself does not bind LIF, but is required for high affinity binding of LIF.

2°C to 8°C,-20°C

12352202