protein

Reelin/RELN Protein, Human (P.pastoris, His)

HY-P72276

2 μg;10 μg;20 μg;50 μg;100 μg

51;128;200;355;570 USD

Reelin/RELN Protein, Human (P.pastoris, His)

proteins

P. pastoris

2 μg;10 μg;20 μg;50 μg;100 μg

51;128;200;355;570 USD

Reelin/RELN proteins regulate neuronal delamination in the cerebral cortex and cerebellum, affecting microtubule function and neuronal migration. Reelin/RELN Protein, Human (P.pastoris, His) is the recombinant human-derived Reelin/RELN protein, expressed by P. pastoris , with N-6*His labeled tag. The total length of Reelin/RELN Protein, Human (P.pastoris, His) is 229 a.a., with molecular weight of 26-30 kDa.

Human

The Reelin/RELN protein, an extracellular matrix serine protease, plays a pivotal role in the layered organization of neurons in the cerebral cortex and cerebellum. Its regulatory influence extends to microtubule function in neurons and neuronal migration, contributing to the intricate architecture of neural networks. Furthermore, Reelin/RELN affects the migration of sympathetic preganglionic neurons in the spinal cord, where it appears to function as a barrier to neuronal migration. Its enzymatic activity is crucial for modulating cell adhesion, emphasizing its involvement in fundamental cellular processes. Through binding to the extracellular domains of lipoprotein receptors VLDLR and LRP8/APOER2, Reelin/RELN induces tyrosine phosphorylation of DAB1 and modulates TAU phosphorylation, suggesting intricate signaling pathways in neuronal regulation. Structurally, it exists as an oligomer of disulfide-linked homodimers and binds to the ectodomains of VLDLR and LRP8/APOER2, underscoring its multifaceted role in orchestrating molecular interactions essential for proper neural development and organization.

LIS2; PRO1598; Reeler; Reelin; RELN;

Greater than 90% as determined by reducing SDS-PAGE.

Lyophilized from a 0.2 μm sterile filtered 20 mM Tris-HCl, 0.5 M NaCl, 3% Trehalose, pH 8.0 or PBS, 6% Trehalose, pH 7.4.

Room temperature in continental US; may vary elsewhere.