Recombinant Human Reelin Protein, CF

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8546-MR-050
R&D Systems Recombinant Proteins and Enzymes
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Recombinant Human Reelin Protein, CF Summary

Product Specifications

Purity
>90%, by SDS-PAGE with silver staining
Endotoxin Level
<0.10 EU per 1 μg of the protein by the LAL method.
Activity
Measured by its binding ability in a functional ELISA. When Recombinant Human Reelin is coated at 1.5 µg/mL (100 µL/well), the concentration of Recombinant Human Apolipoprotein E R2/ApoE R2 (Catalog # 3520-AR) that produces 50% optimal binding response is typically 50-300 ng/mL.
Source
Chinese Hamster Ovary cell line, CHO-derived human Reelin protein
Ser1221-Gln2666, with a C-terminal 6-His tag
Accession #
N-terminal Sequence
Analysis
Ser1221
Predicted Molecular Mass
163 kDa
SDS-PAGE
155-188 kDa, reducing conditions

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8546-MR

Carrier Free

What does CF mean?

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.

What formulation is right for me?

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.

8546-MR

Formulation Lyophilized from a 0.2 μm filtered solution in PBS.
Reconstitution Reconstitute at 400 μg/mL in PBS.
Shipping The product is shipped with polar packs. Upon receipt, store it immediately at the temperature recommended below.
Stability & 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.
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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). Human Reelin is synthesized as a 3460 amino acid (aa) precursor protein with a molecular weight of approximately 410 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, human Reelin shares 95% aa sequence identity with mouse and rat Reelin.

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 RELN gene results in lissencephaly with cerebellar hypoplasia (11, 18). In addition, abnormal Reelin expression in the 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). 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).

References
  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.
Entrez Gene IDs
5649 (Human); 19699 (Mouse); 24718 (Rat)
Alternate Names
EC 3.4.21; EC 3.4.21.-; Reeler; Reelin; RELN; RL; RLPRO1598

Citations for Recombinant Human Reelin Protein, CF

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.

3 Citations: Showing 1 - 3
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  1. Evidence of Reelin Signaling in GBM and Its Derived Cancer Stem Cells
    Authors: F Biamonte, G Sica, A Filippini, A D'Alessio
    Brain sciences, 2021;11(6):.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  2. Reelin Alleviates Mesenchymal Stem Cell Senescence and Reduces Pathological alpha-Synuclein Expression in an In Vitro Model of Parkinson's Disease
    Authors: E Cho, J Park, K Kim, MG Kim, SR Cho
    Genes, 2021;12(7):.
    Species: Human
    Sample Types: Whole Cells
    Applications: Bioassay
  3. Reelin is modulated by diet-induced obesity and has direct actions on arcuate proopiomelanocortin neurons
    Authors: BL Roberts, BJ Bennett, CM Bennett, JM Carroll, LS Dalbøge, C Hall, W Hassouneh, KM Heppner, MA Kirigiti, SR Lindsley, KG Tennant, CA True, A Whittle, AC Wolf, CT Roberts, M Tang-Chris, MW Sleeman, MA Cowley, KL Grove, P Kievit
    Mol Metab, 2019;0(0):.
    Species: Human
    Sample Types: Protein
    Applications: Bioassay

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