Measured in a cell proliferation assay using TF-1 cells. The ED50 for this effect is typically 4.8 ng/mL in the presence of 1.0 μg/mL Recombinant Human CNTFR alpha Protein (rp169598).
Ciliary neurotrophic factor (CNTF) is a member of the cytokine family. It is a polypeptide hormone that has functions in promoting neurotransmitter synthesis and neurite outgrowth in certain neuronal populations. Its actions appear to be restricted to the nervous system. Ciliary neurotrophic factor (CNTF) has biological effects through the activation of a multi-subunit receptor complex, consisting of an extracellular CNTF binding subunit (CNTFα) and two transmembrane signal transduction proteins: glycoprotein gp130 and LIF receptor. CNTF is considered as a potent survival factor of neurons and oligodendrocyteands may be relevant in reducing tissue destruction during inflammatory attacks. CNTF also is a survival factor for neurons of the peripheral sensory sympathetic and ciliary ganglia. It has been reported that CNTF could be an agent that has therapeutic potential and possibly induces differentiation of large multipolar ganglionic phenotype in a subset of progenitors.
生物活性
Measured in a cell proliferation assay using TF-1 cells. The ED50 for this effect is typically 4.8 ng/mL in the presence of 1.0 μg/mL Recombinant Human CNTFR alpha Protein (rp169598).
Recombinant Human CNTF Protein (rp302373) - Protein Bioactivity
Measured in a cell proliferation assay using TF-1 cells. The ED₅₀ for this effect is typically 4.8 ng/mL in the presence of 1.0 μg/mL Recombinant Human CNTFR alpha Protein (rp169598).
Recombinant Human CNTF Protein (rp302373) - SDS-PAGE
3 μg/lane of Recombinant Human CNTF Protein was resolved with SDS-PAGE under reducing (R) and non-reducing (N) conditions and visualized by Coomassie® Blue staining, showing the bands at 27.6 kDa under reducing and 27.6 & 50.2 kDa under non-reducing conditions.
The observation of protein as both dimers and monomers under non-reducing (NR) conditions suggests that a portion of the protein forms dimers. This dimerization may be mediated by (or stabilized by) disulfide bonds (UniProt: P26441).