LIFR Protein, Mouse, Recombinant (His Tag): Product Information
> 95 % as determined by SDS-PAGE
< 1.0 EU per μg of the protein as determined by the LAL method
1. Measured by its ability to bind mouse LIF-Fc (Cat:50755-M02H) in a functional ELISA. 2. Measured by its ability to inhibit the recombinant human LIF mediated inhibition in the M1 mouse myeloid leukemia cells. The ED50 for this effect is typically 5-20 ng/mL in the presence of 2 ng/mL recombinant human LIF.
A DNA sequence encoding the extracellular domain of mouse LIFR (NP_038612.1) (Met 1-Ser 828) was expressed, with a polyhistidine tag at the C-terminus.
The recombinant mouse LIFR consists of 796 amino acids and has a predicted molecular mass of 90 kDa. In SDS-PAGE under reducing conditions, the apparent molecular mass of rm LIFR is approximately 110-120 kDa due to glycosylation.
Lyophilized from sterile PBS, pH 7.4 Please contact us for any concerns or special requirements. Normally 5 % - 8 % trehalose, mannitol and 0.01% Tween80 are added as protectants before lyophilization.
Please refer to the specific buffer information in the hard copy of CoA.
In general, recombinant proteins are provided as lyophilized powder which are shipped at ambient temperature. Bulk packages of recombinant proteins are provided as frozen liquid. They are shipped out with blue ice unless customers require otherwise.
Stability & Storage
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃ Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
A hardcopy of COA with reconstitution instruction is sent along with the products. Please refer to it for detailed information.
LIFR (leukemia inhibitory factor receptor) belongs to the family of cytokine receptors. LIFR forms a high-affinity receptor complex with gp13, which mediates the activity of LIF (leukemia inhibitory factor) and thus affects the differentiation, proliferation, and survival of a wide variety of cells in the adult and the embryo. Besides LIF, LIFR can also bind to and activate CNTF (ciliary neurotrophic factor) and CLC (cardiotrophin like cytokine). Evidence showed that in the retina, LIFR activating LIF, CT-1 and cardiotrophin like cytokine (CLC) are strongly upregulated in response to preconditioning with bright cyclic light leading to robust activation of signal transducer and activator of transcription-3 (STAT3) in a time-dependent manner. Further, blocking LIFR activation during preconditioning using a LIFR antagonist (LIF5) attenuated the induced STAT3 activation and also resulted in reduced preconditioning-induced protection of the retinal photoreceptors. These data demonstrate that LIFR and its ligands play an essential role in endogenous neuroprotective mechanisms triggered by preconditioning-induced stress. LIFR was newly found to be a suppressor of hepatocellular carcinoma (HCC), one of the world's top five causes of cancer-related deaths.
leukemia inhibitory factor receptor alpha
Gearing, D.P. et al.,1991, EMBO J. 10 (10): 2839-2848.
Gearing, D.P. et al.,1992, New Biol. 4 (1): 61-65.
Mosley, B. et al.,1996, J. Biol. Chem. 271 (51): 32635-32643.
Timmermann, A. et al.,2002, Eur. J. Biochem. 269 (11): 2716-2726.
Lass, A. et al.,2002, Fertil. Steril. 76 (6): 1091-1096.
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