Reelin, Recombinant, Mouse

Reelin is a 400kD modular glycoprotein that is critical in brain development and function(1). Reeler mutant mice have a Reelin deficiency and exhibit ataxia, tremors, and impaired motor coordination (2, 3). Reelin consists of an N-terminal Reelin domain, eight domains that consist of an EGF-like repeat flanked by two subrepeats, and a C-terminal arginine-rich region (2). Reelin is cleaved into three fragments in vivo by metalloproteases (4). One (or central) fragment includes domains # 3-6 and retains many of the capabilities of the full length molecule (5). Within this fragment, mouse Reelin shares 95% and 97% aa sequence identity with human and rat Reelin, respectively. In addition to being a protease substrate, Reelin itself has serine protease activity (6). Reelin forms disulfide-linked homodimers and large noncovalently-linked polymers (7,8). It utilizes VLDLR and ApoE R2 as receptors, through which it regulates several nervous system functions (9-11). Reelin is secreted by Cajal-Retzius cells and cerebellar granule cells during cortical plate development, and is required for proper neuronal migration and positioning (2, 3, 9). The N-terminal domain binds integrin a3/b1, leading to a disruption of neuronal-glial cell interactions and inhibition of neuronal migration (12). In the adult hippocampus, cortex, and amygdala, Reelin is required for dendrite growth and maturation, synaptic plasticity, and associative/contextual learning (10, 11, 13, 14). In this capacity, it regulates the subunit composition of NMDA receptors and modulates NMDA currents, even though it does not interact directly with the receptor (11, 15). Deficits in ApoE R2, Reelin, and ApoE function have been linked to several cognitive and mood disorders (1). Peripherally, Reelin is important in the development of neuromuscular junctions. But instead of utilizing the locally expressed ApoE R2 and VLDLR, this involvement requires the serine protease activity of Reelin (16). Description: Recombinant mouse Reelin (Leu 1221-Ile 2661, NCBI Accession #NP_035391) with a C-terminal 6-His tag, expressed in mouse myeloma NSO cell line. Molecular Mass: Based on N-terminal amino acid sequencing, the recombinant mouse Reelin starts at Leu 1221. It has a calculated molecular mass of 162.1kD. As a result of glycosylation, the recombinant monomer migrates as an approximately 180kD protein in SDS-PAGE under reducing conditions. Activity: Measured by its ability to bind biotinylated rhApoE R2 in a functional ELISA type binding assay., , Storage and Stability: Lyophilized powder may be stored at -20°C. Stable for 12 months at -20°C. Reconstitute with sterile PBS, 0.1% BSA or HSA. Aliquot and store at -20°C. Reconstituted product is stable for 6 months at -20°C. For maximum recovery of product, centrifuge the original vial after thawing and prior to removing the cap. Further dilutions can be made in assay buffer.