Recombinant Mouse Reelin Protein Summary
Product Specifications
Analysis
Product Datasheets
Carrier Free
CF stands for Carrier Free (CF). We typically add Bovine Serum Albumin (BSA) as a carrier protein to our recombinant proteins. Adding a carrier protein enhances protein stability, increases shelf-life, and allows the recombinant protein to be stored at a more dilute concentration. The carrier free version does not contain BSA.
In general, we advise purchasing the recombinant protein with BSA for use in cell or tissue culture, or as an ELISA standard. In contrast, the carrier free protein is recommended for applications, in which the presence of BSA could interfere.
3820-MR
| Formulation | Lyophilized from a 0.2 μm filtered solution in PBS with BSA as a carrier protein. |
| Reconstitution | Reconstitute at 100 μg/mL in sterile PBS containing at least 0.1% human or bovine serum albumin. |
| Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. |
| Stability & Storage: | Store the unopened product at -20 to -70 °C. Use a manual defrost freezer and avoid repeated freeze-thaw cycles. Do not use past expiration date. |
3820-MR/CF
| Formulation | Lyophilized from a 0.2 μm filtered solution in PBS. |
| Reconstitution | Reconstitute at 100 μg/mL in sterile PBS. |
| Shipping | The product is shipped at ambient temperature. Upon receipt, store it immediately at the temperature recommended below. |
| Stability & Storage: | Store the unopened product at -20 to -70 °C. Use a manual defrost freezer and avoid repeated freeze-thaw cycles. Do not use past expiration date. |
Reconstitution Calculator
Background: Reelin
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).
- Fatemi, S.H. (2005) Mol. Psychiatry 10:251.
- Förster, E. et al. (2010) Eur. J. Neurosci. 31:1511.
- Quattrocchi, C.C. et al. (2002) J. Biol. Chem. 277:303.
- D’Arcangelo, G. et al. (1995) Nature 374:719.
- Jossin, Y. et al. (2004) J. Neurosci. 24:514.
- Folsom, T.D. and S.H. Fatemi (2013) Neuropharmacology 68:122.
- Utsunomiya-Tate, N. et al. (2000) Proc. Natl. Acad. Sci. USA 97:9729.
- Nakano, Y. et al. (2007) J. Biol. Chem. 282:20544.
- Hibi, T. et al. (2009) Neurosci. Res. 63:251.
- Lambert de Rouvroit, C. et al. (1999) Exp. Neurol. 156:214.
- Meyer, G. (2010) J. Anat. 217:334.
- D’Arcangelo, G. et al. (1999) Neuron 24:471.
- Senkov, O. et al. (2014) Prog. Brain Res. 214:53.
- Dulabon, L. et al. (2000) Neuron 27:33.
- Hoe, H.S. et al. (2009) J. Neurosci. 29:7459.
- Hirotsune, S. et al. (1995) Nat. Genet. 10:77.
- Levy, A.D. et al. (2014) Front. Neuroanat. 8:116.
- Barros, C.S. et al. (2011) Cold Spring Harb. Perspect. Biol. 3:a005108.
- Botella-López, A. et al. (2006) Proc. Natl. Acad. Sci. USA 103:5573.
- Lubbers, B.R. et al. (2014) Prog. Brain Res. 214:263.
- Quattrocchi, C.C. et al. (2003) Science 301:649.
Citations for Recombinant Mouse Reelin Protein
R&D Systems personnel manually curate a database that contains references using R&D Systems products. The data collected includes not only links to publications in PubMed, but also provides information about sample types, species, and experimental conditions.
7
Citations: Showing 1 - 7
Filter your results:
Filter by:
-
Lymphatics act as a signaling hub to regulate intestinal stem cell activity
Authors: 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
Cell Stem Cell, 2022-06-20;29(7):1067-1082.e18.
Species: Mouse
Sample Types: Organoid
Applications: Bioassay -
Dynamics, nanomechanics and signal transduction in reelin repeats
Authors: K Mikulska-R, J Strzelecki, W Nowak
Sci Rep, 2019-12-12;9(1):18974.
Species: Mouse
Sample Types: Whole Cells
Applications: Bioassay -
Reelin Can Modulate Migration of Olfactory Ensheathing Cells and Gonadotropin Releasing Hormone Neurons via the Canonical Pathway
Authors: L Dairaghi, E Flannery, P Giacobini, A Saglam, H Saadi, S Constantin, F Casoni, BW Howell, S Wray
Front Cell Neurosci, 2018-08-03;12(0):228.
Species: Mouse
Sample Types: Whole Cells
Applications: Bioassay -
Hypervulnerability of the adolescent prefrontal cortex to nutritional stress via reelin deficiency
Mol. Psychiatry, 2016-11-15;0(0):.
Species: Mouse
Sample Types: In Vivo
Applications: In Vivo -
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.
Authors: Do H, Bruelle C, Tselykh T, Jalonen P, Korhonen L, Lindholm D
J Biol Chem, 2013-08-29;288(41):29613-20.
Species: Rat
Sample Types: Whole Cells
Applications: Bioassay -
Smooth muscle-endothelial cell communication activates Reelin signaling and regulates lymphatic vessel formation.
J. Cell Biol., 2012-06-04;197(6):837-49.
Species: Mouse
Sample Types: Whole Cells
Applications: Bioassay -
miR-200c regulates FGFR-dependent epithelial proliferation via Vldlr during submandibular gland branching morphogenesis.
Authors: Rebustini IT, Hayashi T, Reynolds AD
Development, 2011-11-24;139(1):191-202.
Species: Mouse
Sample Types: Whole Cells
Applications: Bioassay
FAQs
No product specific FAQs exist for this product, however you may
View all Proteins and Enzyme FAQsReviews for Recombinant Mouse Reelin Protein
Average Rating: 5 (Based on 1 Review)
Have you used Recombinant Mouse Reelin Protein?
Submit a review and receive an Amazon gift card.
$25/€18/£15/$25CAN/¥75 Yuan/¥1250 Yen for a review with an image
$10/€7/£6/$10 CAD/¥70 Yuan/¥1110 Yen for a review without an image
Filter by:
