Recombinant Human LIFR alpha (Mammalian-expressed), CF Summary
Details of Functionality
Measured by its ability to inhibit LIF-dependent proliferation of TF‑1 human erythroleukemic cells. Kitamura, T. et al. (1989) J. Cell Physiol. 140:323. The ED50 for this effect is typically 1-6 μg/mL in the presence of 0.3 ng/mL of recombinant human LIF.
Source
Human embryonic kidney cell, HEK293-derived human LIF R alpha protein Met1-Ser833
Gln45 predicted: No result obtained, sequencing might be blocked
Protein/Peptide Type
Recombinant Proteins
Gene
LIFR
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.
Applications/Dilutions
Dilutions
Bioactivity
Theoretical MW
89.4 kDa. Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
110-140 kDa, reducing conditions
Publications
Read Publication using 7487-LR in the following applications:
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
12 months from date of receipt, -20 to -70 °C as supplied.
1 month, 2 to 8 °C under sterile conditions after reconstitution.
3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS.
Purity
>95%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 300 μg/mL in PBS.
Notes
This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.
Alternate Names for Recombinant Human LIFR alpha (Mammalian-expressed), CF
CD118 antigen
CD118
FLJ98106
FLJ99923
leukemia inhibitory factor receptor alpha
leukemia inhibitory factor receptor
LIF R alpha
LIF R beta
LIF receptor
LIFR alpha
LIFR
LIF-R
LIFRa
SJS2
STWS
SWS
Background
Leukemia Inhibitory Factor Receptor alpha (LIF R alpha ), also known as LIFR beta and CD118, is a 190 kDa type I transmembrane protein in the Interleukin-6 receptor family. Members of this family mediate the biological effects of Cardiotrophin-1, CLC, CNTF, IL-6, IL-11, IL-27, and Oncostatin M (1). Mature human LIF R alpha consists of a 789 amino acid (aa) extracellular domain (ECD) with two cytokine receptor homology domains, one WSxWS motif, and three fibronectin type III repeats, followed by a 25 aa transmembrane segment and a 239 aa cytoplasmic domain (2). Within the ECD, human LIF R alpha shares 72% aa sequence identity with mouse and rat LIF R alpha . LIF R alpha binds the pleiotropic cytokine LIF with low affinity (3). Binding affinity is increased by the ligand-induced association of LIF R alpha with the signal transducing subunit gp130 (4, 6). The LIF R alpha /gp130 receptor complex also transduces Oncostatin M signals, although LIF R alpha alone does not interact with Oncostatin M (4). gp130 associates with different ligand-specific receptors to form signaling receptor complexes for the other IL-6 family ligands (1). The CNTF receptor is a ternary complex that contains CNTF R alpha and gp130 as well as LIF R alpha (6, 7). LIF R alpha is widely expressed, and LIF induces the proliferation, differentiation, and activation of cells in many tissues (8, 9). In particular, LIF R alpha plays an important role in several aspects of early pregnancy such as blastocyst implantation in the uterus (10-12).
Muller-Newen, G. (2003) Science STKE 2003:pe40.
Gearing, D.P. et al. (1991) EMBO J. 10:2839.
Layton, M.J. et al. (1992) Proc. Natl. Acad. Sci. 89:8616.
Gearing, D.P. et al. (1992) Science 255:1434.
Giese, B. et al. (2005) J. Cell Sci. 118:5129.
Ip, N.Y. et al. (1992) Cell 69:1121.
Davis, S. et al. (1993) Science 260:1805.
Metcalf, D (2003) Stem Cells 21:5.
Kubota, Y. et al. (2008) J. Clin. Invest. 118:2393.
Paiva, P. et al. (2009) Cytokine Growth Factor Rev. 20:319.
Stewart, C.L. et al. (1992) Nature 359:76.
Cheng, J.-G. et al. (2001) Proc. Natl. Acad. Sci. 98:8680.
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