Recombinant Human Reelin protein (His tag) is a Human Fragment protein, in the 26 to 254 aa range, expressed in Escherichia coli, with >90%, suitable for SDS-PAGE.
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Reelin, RELN
- SDS-PAGE
Supplier Data
SDS-PAGE - Recombinant Human Reelin protein (His tag) (AB236169)
Analysis of ab236169 by (Tris-Glycine gel) discontinuous SDS-PAGE (reduced) with 5% enrichment gel and 15% separation gel.
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This supplementary information is collated from multiple sources and compiled automatically.
Biological function summary
Reelin functions in the regulation of neuronal migration and positioning in the developing brain. Acting as a signaling molecule it forms part of a larger complex essential for proper neuronal layering and synaptic plasticity. Reelin interacts with various receptors on the cell surface initiating a cascade of intracellular signaling that influences cell orientation and dendritic growth.
Pathways
Reelin engages both the Reelin signaling pathway and the PI3K-Akt pathway highlighting its diverse influence on cellular processes. In the Reelin signaling pathway it associates with proteins like Dab1 and VLDLR playing an important role in the modulation of tyrosine kinases. This association affects neuronal structures by guiding their architectural development while interactions with the PI3K-Akt pathway impact cell survival and growth.
일반 정보
기능
Extracellular matrix serine protease secreted by pioneer neurons that plays a role in layering of neurons in the cerebral cortex and cerebellum by coordinating cell positioning during neurodevelopment. Regulates microtubule function in neurons and neuronal migration. Binding to the extracellular domains of lipoprotein receptors VLDLR and LRP8/APOER2 induces tyrosine phosphorylation of DAB1 and modulation of TAU phosphorylation. Affects migration of sympathetic preganglionic neurons in the spinal cord, where it seems to act as a barrier to neuronal migration. Enzymatic activity is important for the modulation of cell adhesion.
서열 유사성
Belongs to the reelin family.
Post-translational modifications
N-glycosylated and to a lesser extent also O-glycosylated.
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