>90%, 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 C1qL3
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 0.3-1.8 μg/mL.
Human embryonic kidney cell, HEK293-derived Ala25-Thr880, with C-terminal 6-His tag
When Recombinant Human C1qL3 (Catlog # 9115-TN) is coated at 1 µg/mL (100 μL/well), Recombinant Human BAI3 (Catlog # 9106-BA) binds with a typical ED50 of 0.3-1.8 μg/mL.
Brain angiogenesis inhibitor 3 (BAI3) is
an approximately 180 kDa adhesion GPCR that plays a role in neuronal synapse
formation and maintenance. Mature human BAI3 consists of an 856 amino acid (aa)
N-terminal extracellular domain (ECD) with one CUB domain, four TSP1 domains,
and a GPS protease sensitive linker, followed by a region with seven
transmembrane segments and a 376 aa C-terminal cytoplasmic domain (1, 2).
Within the N-terminal ECD, human BAI3 shares 98% and 97% aa sequence identity
with mouse and rat BAI3, respectively. BAI3 is primarily expressed post-synaptically
in the cerebral cortex and on cerebellar Purkinje cells (1-5), and it binds to the
TNF-like proteins C1qL1, 2, 3, and 4 (6). BAI3 interaction with C1qL1 is
required for the formation and maintenance of excitatory synapses between
climbing fibers and parallel fibers with Purkinje cells (4, 5). BAI3 ligation
can also reduce excitatory synaptic density in hippocampal neurons, decrease
dendrite arborization, and promote axon pruning in climbing fibers (3, 4, 6). It
is additionally expressed in developing muscle where it is required for
myoblast fusion (7).
Shiratsuchi, T. et al. (1997) Cytogenet. Cell Genet. 79:103.
Kee, H.J. et al. (2004) FEBS Lett. 569:307.
Lanoue, V. et al. (2013) Mol. Psychiatry 18:943.
Kakegawa, W. et al. (2015) Neuron 85:316.
Sigoillot, S.M. et al. (2015) Cell Rep. 10:820.
Bolliger, M.F. et al. (2011) Proc. Natl. Acad. Sci. USA 108:2534.
Hamoud, N. et al. (2014) Proc. Natl. Acad. Sci. USA 111:3745.
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