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Western blot analysis for CNTFRα. 20 ng (lane 1), 10 ng (lane 2) and 5 ng (lane 3) of recombinant human CNTFRα (R&D Systems cat. no. 303-CR-050) was probed with the purified Mouse Anti-CNTFRα antibody at a concentration of 0.25 µg/mL. CNTFRα is identified here as a protein of 50-60 kDa.


BD Pharmingen™ Purified Mouse Anti-CNTFRα

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- Since applications vary, each investigator should titrate the reagent to obtain optimal results.
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Ciliary neurotrophic factor receptor (CNTFR) shares functional and structural properties with members of the hematopoietic cytokine family. Signaling through the CNTFR involves the binding and activation of a multisubunit receptor complex composed of three components: a ligand-specific-α-receptor (CNTFRα), signal-transducing β-subunits of gp130 and leukemia inhibitory factor receptor-β (LIFR). Binding of CNTF to CNTFR triggers the association of the receptor complex components resulting in activation of a signal transduction cascade mediated by intracellular protein tyrosine kinases. CNTFR can function in a membrane-bound or soluble form; the membrane-bound form is expressed in neuronal and muscle cells, while the soluble form, once processed, can serve as a cofactor to potentiate CNTF actions. This action may serve to enhance the survival, proliferation, and maturation of oligodendrocyte lineage cells. AN-H6 recognizes human and mouse CNTFRα. The antibody is routinely tested by western blot analysis on L929 cells transfected with CNTFRα. The 40 and 60 kDa proteins are thought to represent the non-glycosylated and glycosylated forms of the CNTFRα, respectively.
Development References (1)
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Krüttgen A, Grötzinger J, Kurapkat G. Human ciliary neurotrophic factor: a structure-function analysis. Biochem J. 1995; 309(Pt 1):215-220. (Biology). View Reference
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