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Recombinant Mouse Reelin Protein, CF

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Product Details

Summary
Reactivity MuSpecies Glossary
Applications Binding Activity
Format
Carrier-Free

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Recombinant Mouse Reelin Protein, CF Summary

Details of Functionality
Measured by its ability to bind biotinylated rhApoE R2 in a functional ELISA.
Source
Mouse myeloma cell line, NS0-derived mouse Reelin protein
Leu1221-Ile2661, with a C-terminal 6-His tag
Accession #
N-terminal Sequence
Leu1221
Protein/Peptide Type
Recombinant Proteins
Gene
Reln
Purity
>85%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Endotoxin Note
<0.10 EU per 1 μg of the protein by the LAL method.

Applications/Dilutions

Dilutions
  • Binding Activity
Theoretical MW
162.1 kDa.
Disclaimer note: The observed molecular weight of the protein may vary from the listed predicted molecular weight due to post translational modifications, post translation cleavages, relative charges, and other experimental factors.
SDS-PAGE
145-160 kDa, reducing conditions
Publications
Read Publications using
3820-MR/CF in the following applications:

Packaging, Storage & Formulations

Storage
Use a manual defrost freezer and avoid repeated freeze-thaw cycles.
  • 12 months from date of receipt, -20 to -70 °C as supplied.
  • 1 month, 2 to 8 °C under sterile conditions after reconstitution.
  • 3 months, -20 to -70 °C under sterile conditions after reconstitution.
Buffer
Lyophilized from a 0.2 μm filtered solution in PBS.
Purity
>85%, by SDS-PAGE visualized with Silver Staining and quantitative densitometry by Coomassie® Blue Staining.
Reconstitution Instructions
Reconstitute at 100 μg/mL in sterile PBS.

Notes

This product is produced by and ships from R&D Systems, Inc., a Bio-Techne brand.

Alternate Names for Recombinant Mouse Reelin Protein, CF

  • EC 3.4.21
  • EC 3.4.21.-
  • Reeler
  • Reelin
  • RELN
  • RL
  • RLPRO1598

Background

Reelin is a secreted modular glycoprotein that exhibits serine protease activity and is crucial for brain development and function (1-3). It is composed of an N-terminal Reelin domain, eight EGF-like Reelin repeats (RR), and a highly basic C-terminal region (4-6). The N-terminal fragment is suggested to mediate dimerization/oligomerization and receptor recognition, the midpiece receptor binding, and the C-terminal fragment receptor signaling and recognition (1, 5, 7-9). Mouse Reelin is synthesized as a 3461amino acid (aa) precursor protein with a molecular weight of approximately 388 kDa (4). During processing, it can be cleaved between RR2 and RR3 or between RR6 and RR7, producing a 180 kDa and a 330 kDa peptide, respectively (1, 6, 10). Within shared regions in the central fragment, mouse Reelin shares 95% and 97% aa sequence identity with human and rat Reelin, respectively.

Reelin is secreted by Cajal-Retzius cells in the embryo (1, 4, 11). In the adult, it is expressed in the subventricular zone, rostral migratory stream, olfactory bulb, and in the CA1, CA3, and dentate gyrus regions of the hippocampus, as well as in cerebellar granule cells, pyramidal cells of the entorhinal cortex, GABA interneurons, and glial cells (1, 6, 12, 13). Reelin utilizes the receptors VLDLR and ApoE R2, which have been suggested to have divergent roles in Reelin-mediated neuronal migration (1, 2, 6, 12). It has also been shown to interact with Integrin alpha 3 beta 1 and APP (1, 6, 14, 15). During cortical plate development, Reelin controls cell-cell interactions critical for proper neuronal migration and positioning (1, 2, 4, 5, 11, 12, 16). In the adult, it plays a role in dendrite growth and maturation, and synapse formation (2, 6, 15). Additionally, Reelin has been shown to modulate synaptic transmission and plasticity by regulating the subunit composition and conductivity of NMDA receptors (2, 6, 17). Mutation of the human RELN gene results in lissencephaly with cerebellar hypoplasia (11, 18). In addition, abnormal Reelin expression in human brain has been associated with a variety of cognitive pathological conditions including autism, schizophrenia, bipolar disorder, major depression, and Alzheimer’s disease (1, 6, 11, 13, 19, 20). Reelin deficiency found in Reeler mutant mice causes ataxia, tremors, and impaired motor coordination (4, 16). Peripherally, Reelin is important in the development of neuromuscular junctions. But instead of utilizing the locally expressed ApoE R2 and VLDLR, this function requires the serine protease activity of Reelin (3, 21).

  1. Fatemi, S.H. (2005) Mol. Psychiatry 10:251.
  2. Förster, E. et al. (2010) Eur. J. Neurosci. 31:1511.
  3. Quattrocchi, C.C. et al. (2002) J. Biol. Chem. 277:303.
  4. D’Arcangelo, G. et al. (1995) Nature 374:719.
  5. Jossin, Y. et al. (2004) J. Neurosci. 24:514.
  6. Folsom, T.D. and S.H. Fatemi (2013) Neuropharmacology 68:122.
  7. Utsunomiya-Tate, N. et al. (2000) Proc. Natl. Acad. Sci. USA 97:9729.
  8. Nakano, Y. et al. (2007) J. Biol. Chem. 282:20544.
  9. Hibi, T. et al. (2009) Neurosci. Res. 63:251.
  10. Lambert de Rouvroit, C. et al. (1999) Exp. Neurol. 156:214.
  11. Meyer, G. (2010) J. Anat. 217:334.
  12. D’Arcangelo, G. et al. (1999) Neuron 24:471.
  13. Senkov, O. et al. (2014) Prog. Brain Res. 214:53.
  14. Dulabon, L. et al. (2000) Neuron 27:33.
  15. Hoe, H.S. et al. (2009) J. Neurosci. 29:7459.
  16. Hirotsune, S. et al. (1995) Nat. Genet. 10:77.
  17. Levy, A.D. et al. (2014) Front. Neuroanat. 8:116.
  18. Barros, C.S. et al. (2011) Cold Spring Harb. Perspect. Biol. 3:a005108.
  19. Botella-López, A. et al. (2006) Proc. Natl. Acad. Sci. USA 103:5573.
  20. Lubbers, B.R. et al. (2014) Prog. Brain Res. 214:263.
  21. Quattrocchi, C.C. et al. (2003) Science 301:649.

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Publications for Reelin (3820-MR/CF)(7)

We have publications tested in 2 confirmed species: Mouse, Rat.

We have publications tested in 2 applications: Bioassay, In Vivo.


Filter By Application
Bioassay
(6)
In Vivo
(1)
All Applications
Filter By Species
Mouse
(6)
Rat
(1)
All Species
Showing Publications 1 - 7 of 7.
Publications using 3820-MR/CF Applications Species
RE Niec, T Chu, M Schernthan, S Gur-Cohen, L Hidalgo, HA Pasolli, KA Luckett, Z Wang, SR Bhalla, F Cambuli, RP Kataru, K Ganesh, BJ Mehrara, D Pe'er, E Fuchs Lymphatics act as a signaling hub to regulate intestinal stem cell activity Cell Stem Cell, 2022-06-20;29(7):1067-1082.e18. 2022-06-20 [PMID: 35728595] (Bioassay, Mouse) Bioassay Mouse
K Mikulska-R, J Strzelecki, W Nowak Dynamics, nanomechanics and signal transduction in reelin repeats Sci Rep, 2019-12-12;9(1):18974. 2019-12-12 [PMID: 31831824] (Bioassay, Mouse) Bioassay Mouse
L Dairaghi, E Flannery, P Giacobini, A Saglam, H Saadi, S Constantin, F Casoni, BW Howell, S Wray Reelin Can Modulate Migration of Olfactory Ensheathing Cells and Gonadotropin Releasing Hormone Neurons via the Canonical Pathway Front Cell Neurosci, 2018-08-03;12(0):228. 2018-08-03 [PMID: 30127721] (Bioassay, Mouse) Bioassay Mouse
Hypervulnerability of the adolescent prefrontal cortex to nutritional stress via reelin deficiency Mol. Psychiatry, 2016-11-15;0(0):. 2016-11-15 [PMID: 27843148] (In Vivo, Mouse) In Vivo Mouse
Do H, Bruelle C, Tselykh T, Jalonen P, Korhonen L, Lindholm D Reciprocal regulation of very low density lipoprotein receptors (VLDLRs) in neurons by brain-derived neurotrophic factor (BDNF) and Reelin: involvement of the E3 ligase Mylip/Idol. J Biol Chem, 2013-08-29;288(41):29613-20. 2013-08-29 [PMID: 23990472] (Bioassay, Rat) Bioassay Rat
Smooth muscle-endothelial cell communication activates Reelin signaling and regulates lymphatic vessel formation. J. Cell Biol., 2012-06-04;197(6):837-49. 2012-06-04 [PMID: 22665518] (Bioassay, Mouse) Bioassay Mouse
Rebustini IT, Hayashi T, Reynolds AD miR-200c regulates FGFR-dependent epithelial proliferation via Vldlr during submandibular gland branching morphogenesis. Development, 2011-11-24;139(1):191-202. 2011-11-24 [PMID: 22115756] (Bioassay, Mouse) Bioassay Mouse

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Bioinformatics

Gene Symbol Reln
Uniprot