Recombinant Human LIFR alpha Protein, CF
Recombinant Human LIFR alpha Protein, CF Summary
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
|Formulation||Lyophilized from a 0.2 μm filtered solution in PBS.|
|Reconstitution||Reconstitute at 100 μg/mL in sterile PBS.|
|Shipping||The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below.|
|Stability & Storage:||Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
Background: LIFR alpha
The activities of the pleiotropic cytokine LIF are mediated through a high-affinity heterodimeric receptor complex consisting of two membrane glycoproteins: an alpha subunit (LIF R alpha, also known as LIF R beta and CD118) that binds LIF with low affinity and the 130 kDa (gp130) subunit that does not bind LIF by itself, but is required for high-affinity binding of LIF by the complex. The gp130 subunit was first described as the signal transducing subunit of the high-affinity IL-6 receptor complex. Besides LIF, the high-affinity heterodimeric LIF receptor complex has been shown to mediate the activities of oncostatin M (OSM), cardiotrophin-1 and ciliary neurotrophic factor (CNTF).
Human LIF R alpha cDNA encodes a 1097 amino acid (aa) residue precursor type I membrane protein with a 44 aa residue signal peptide, a 789 aa residue extracellular domain, a 26 aa residue transmembrane domain, and a 238 aa residue cytoplasmic domain. LIF R alpha is a member of the cytokine receptor family and has extensive homology to gp130. The extracellular domain of LIF R alpha has two cytokine receptor domains and three fibronectin type III repeats. In mouse, mRNAs encoding a soluble LIF R alpha and lacking transmembrane and intracellular domains, have been isolated. Soluble LIF R alpha has been shown to bind LIF and has LIF antagonistic activity.
- Bazan, J.F. (1990) Proc. Natl. Acad. Sci. USA 87:6934.
- Gearing, D.P. (1994) Guidebook to Cytokines and Their Receptors, Academic Press, p130.
- Pennica D. et al. (1995) J. Biol. Chem. 270:10915.
Citations for Recombinant Human LIFR alpha Protein, CF
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
Citations: Showing 1 - 2
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A unique loop structure in oncostatin M determines binding affinity toward oncostatin M receptor and leukemia inhibitory factor receptor.
Authors: Chollangi, Srinivas, Mather, Timothy, Rodgers, Karla K, Ash, John D
J Biol Chem, 2012;287(39):32848-59.
Sample Types: Recombinant Protein
Applications: ELISA (Capture)
Gp130 activation by soluble interleukin-6 receptor/interleukin-6 enhances osteoblastic differentiation of human bone marrow-derived mesenchymal stem cells.
Authors: Erices A, Conget P, Rojas C, Minguell JJ
Exp. Cell Res., 2002;280(1):24-32.
Sample Types: Whole Cells
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