+32 1658 9045
0032 (0)16 41 44 07
+32 1650 9045
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tel +32 1658 9045
fax +32 1650 9045
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tel +81 78 386 0860
fax +81 78 306 0296
Česká republika Praha
US New York
0032 (0)16 41 44 07
Recombinant Human Leukemia Inhibitory Factor (LIF)
(Cat. No.: C017)
Leukemia Inhibitory Factor (LIF) is a lymphoid factor which promotes long-term maintenance of embryonic stem cells by suppressing spontaneous differentiation. LIF has a number of other activities including cholinergic neuron differentiation, control of stem cell pluripotency, bone and fat metabolism, mitogenesis of certain factor dependent cell lines and promotion of megakaryocyte production in vivo. Human and murine mature LIF exhibit a 78% sequence identity at the amino acid control. Human LIF is equally active on both human and mouse cells. Murine LIF is approximately 1000 fold less active on human cells, than hLIF.
Recombinant Human LIF produced in E. coli is a single, non-glycosylated, polypeptide chain containing 180 amino acids and having a molecular mass of 19717 Dalton.
Biological activity: The ED50 was determined by the M1 cell differentiation assay is < 0.01 ng/ml, corresponding to a specific activity of 1.0 x 108 IU/mg.
Purity: Greater than 95% as determined by
(a) Analysis by RP-HPLC.
(b) Anion-exchange FPLC.
(c) Analysis by reducing and non-reducing SDS-PAGE Silver Stained gel..
Amino-Acid Sequence: The sequence of the first five N-terminal amino acids was determined and was found to be Ser-Pro-Leu-Pro-Ile.
Endotoxin: Less than 0.1ng/µg (1IEU/µg) of LIF.
Formulation: LIF was lyophilized after extensive dialysis against PBS.
Storage: Lyophilized rHuLIF although stable at room temperature for 3 weeks, should be stored desiccated below -18oC. Upon reconstitution rHuLIF should be stored at 4oC between 2-7 days and for future use below -18oC. For long-term storage it is recommended to add a carrier protein (0.1% HSA or BSA).
Please avoid freeze-thaw cycles.
Reconstitution: We recommend a quick spin followed by reconstitution in water to a concentration of 0.1-1.0mg/ml. It is recommended that further dilutions be made into buffer or medium to which protein (e.g., 1% BSA) or Tween 20 has been added. This solution can then be stored at 4oC for 1 week or -20oC for future use.
1: J Chem Phys 2008 Dec;Vol 129(24)
Application of improved virtual orbital based multireference methods to N2, LiF, and C4H6 systems.
[Abstract] The improved virtual orbital (IVO) complete active space configuration interaction (CASCI) based multiconfigurational quasidegenerate perturbation theory (MCQDPT) and its single-root version (termed as MRMPPT) are applied to assess the efficacy and the reliability of these two methods. Applications involve the ground and/or excited state potential energy curves (PECs) of N(2), LiF, and C(4)H(6) (butadiene) molecules, systems that are sufficiently complex to assess the applicability of these methods. The ionic-neutral curve crossing involving the lowest two (1)Sigma(+) states of LiF molecule is studied using the IVO-MCQDPT method, while its single-root version (IVO-MRMPPT) is employed to study the ground state PEC for isomerization of butadiene and to model the
bond dissociation of N(2) molecule. Comparisons with the standard methods (full CI, coupled cluster with singles and doubles, etc.) demonstrate that the IVO-based MRMPPT and MCQDPT approaches provide smooth and reliable PECs for all the systems studied. The IVO-CASCI method is explored to enable geometry optimization for ground state of C(4)H(6) using numerical energy gradients. The ground spectroscopic constants of N(2) and LiF determined using the numerical gradient based IVO-CASCI method are in accord with experiment and with other correlated calculations. As an illustration, we may point out that the maximum deviation from the experiment in our estimated normal mode frequency of LiF is 34 cm(-1), whereas for the bond length, the maximum error is just 0.012 A.
2: Neurol Res 2008 Dec;
Response of neural precursor cells in the brain of Parkinson's disease mouse model after LIF administration.
[Abstract] OBJECTIVE: To access the response of endogenous neural precursor cells (NPCs) in the area of substantia nigra (SN) in the mouse model of Parkinson's disease (PD). To evaluate whether leukemia inhibitory factor (LIF) can up-regulate the expression of NPCs and their fate in differentiation. METHODS: NPCs were measured and the number and density were estimated using the confocal counting system in normal control (CON), normal control LIF treated (CON + LIF), PD (PD) and LIF treated PD (PD + LIF) mice. RESULTS: The PD + LIF group showed a statistically significant improvement in the number and density of NPCs compared with PD group, and NPCs are rarely seen in CON and CON + LIF groups. CONCLUSION: LIF may be a useful treatment for PD by up-regulating the
re-expression of NPCs, which may represent the neuroprotection mechanism of LIF.
3: Biomed Khim ;Vol 54(5)
[The influence of LIF (leukemia inhibitory factor) on the functional status of mouse line R1 embryonic stem cells]
[Abstract] The influence of cytokine LIF (Leukemia Inhibitory Factor) on the viability, and proliferation of mouse R1 line embryonic stem cells (ESC) and their distribution by cell cycle stages has been investigated. LIF (5-20 ng/ml) increased growth of colonies and maintained high proliferative and pluripotent properties of R1. LIF was also involved into the inhibition of spontaneous cell differentiation and apoptotic cell death; it also decreased the rations of S/G2+M cell cycle and doubling-time of cell population.
4: J Neurosci 2008
Leukemia inhibitory factor extends the lifespan of injured photoreceptors in vivo.
[Abstract] Survival and death of photoreceptors in degenerative diseases of the retina is controlled by a multitude of genes and endogenous factors. Some genes may be involved in the degenerative process itself whereas others may be part of an endogenous defense system. We show in two models of retinal degeneration that photoreceptor death strongly induces expression of leukemia inhibitory factor (LIF) in a subset of Muller glia cells in the inner nuclear layer of the retina. LIF expression is essential to induce an extensive intraretinal signaling system which includes Muller cells and photoreceptors and is characterized by an upregulation of Edn2, STAT3, FGF2 and GFAP. In the absence of LIF, Muller cells remain quiescent, the signaling system is not activated and
retinal degeneration is strongly accelerated. Intravitreal application of recombinant LIF induces the full molecular pathway including the activation of Muller cells in wild-type and Lif(-/-) mice. Interruption of the signaling cascade by an Edn2 receptor antagonist increases whereas activation of the receptor decreases photoreceptor cell death. Thus, LIF is essential and sufficient to activate an extensive molecular defense response to photoreceptor injury. Our data establish LIF as a Muller cell derived neuronal survival factor which controls an intrinsic protective mechanism that includes Edn2 signaling to support photoreceptor cell survival and to preserve vision in the injured retina.
Protein Accession No.:
SPLPI TPVNA TCAIR HPCHN NLMNQ IRSQL AQLNG SANAL FILYY TAQGE PFPNN LDKLC GPNVT DFPPF HANGT EKAKL VELYR IVVYL GTSLG NITRD QKILN PSALS LHSKL NATAD ILRGL LSNVL CRLCS KYHVG HVDVT YGPDT SGKDV FQKKK LGCQL LGKYK QIIAV LAQAF
*NOTE: ALL PRODUCTS ARE FOR RESEARCH USE ONLY