>85%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
<0.10 EU per 1 μg of the protein by the LAL method.
Measured by its binding ability in a functional ELISA. When Recombinant Human C1qTNF14/C1qL1 is immobilized at 1 μg/mL, 100 μL/well, the concentration of
Recombinant Human BAI3
that produces 50% of the optimal binding
response is approximately 0.4-2.4 μg/mL
E. coli-derived Thr125-Asp258, with an N-terminal Met and 6-His tag
When Recombinant Human C1qTNF14/C1qL1 (Catalog # 9134-TN) is coated at 1 µg/mL (100 μL/well), Recombinant Human BAI3 (Catalog # (Catalog # 9106-BA) binds with a typical ED50 of 0.4-2.4 μg/mL.
C1qTNF14 (CTRP14), also known as C1qL1, is an approximately 30 kDa member of the C1q family of secreted proteins (1, 2). Mature human C1qTNF14 contains a collagen-like region and one C1q-like domain and can form disulfide-linked heteromers with C1qTNF11/C1qL4 (3, 4). Within the C1q-like domain, human C1qTNF14 shares 100% aa sequence identity with mouse and rat C1qTNF14. C1qTNF14 is expressed in the inferior olive, hippocampus, and cerebral cortex (5). Similarly to C1qTNF13/C1qL3, C1qTNF10/C1qL2, and C1qTNF11/C1qL4, C1qTNF14 binds to BAI3 in the cerebral cortex and on cerebellar Purkinje cells (5-8). C1qTNF14/C1qL1 binding to BAI3 induces the formation and maintenance of excitatory synapses between climbing fibers and parallel fibers with Purkinje cells (5, 7).
Grebrehiwet, B. et al. (2012) Front. Immunol. 5:3.
Yuzaki, M. (2010) Eur. J. Neurosci. 32:191.
Ressl, S. et al. (2015) Structure 23:688.
Wei, Z. et al. (2013) J. Biol. Chem. 288:10214.
Sigoillot, S.M. et al. (2015) Cell Rep. 10:820.
Lanoue, V. et al. (2013) Mol. Psychiatry 18:943.
Kakegawa, W. et al. (2015) Neuron 85:316.
Bolliger, M.F. et al. (2011) Proc. Natl. Acad. Sci. USA 108:2534.