Anti-Reelin (CR-50) mAb

  • Applications
    • ICC
    • IHC
    • IP
    • WB
  • Target Reelin/CR-50
  • Host Species Mouse
  • Species Reactivities Mouse
  • Code # D223-3
  • Size 100 μg
  • Price
    $278.49
Specifications

Background

Reelin is a large extracellular glycoprotein of 420-450 kDa that controls cortical development and secreted by several neurons, such as cortical Cajal-Retzius cells. Defective Reelin is the cause of the reeler malformation in mouse and the Norman-Roberts type lissencephaly in human. Reelin is thought to deliver a signal to migrating neurons, instructing them to assume their correct position. Their response requires binding of Reelin to at least one of two lipoprotein receptors, very-low-density lipoprotein receptor (VLDLR) and apolipoprotein-E receptor type 2 (ApoER2), thereby inducing phosphorylation of the Dab1 (Disabled 1) adapter that interacts with the cytoplasmic tail of receptors. Anti-Reelin monoclonal antibody CR-50 interferes with Reelin homopolymerization and with Dab1 phosphorylation. Intraventricular injection of CR-50 disrupts the organized development of the hIPocampus, resulting in a pattern similar to that found in reeler.
  • Antibody Type:
    Monoclonal
  • Application:
    ICC, IHC, IP, WB
  • Clone Number:
    RE-3B9(R3B9)
  • Concentration:
    1 mg/mL
  • Conjugate:
    Unlabeled
  • Description:

    Monoclonal antibody of 100 μg targeting Reelin/CR-50 for ICC, IHC, IPP, WB.

  • Formulation:
    100 μg IgG in 100 μl PBS containing 50% glycerol, pH 7.2. Contains nopreservatives.
  • Gene ID (Human):
  • Gene ID (Mouse):
  • Host Species:
    Mouse
  • Immunogen:
    Homogenates of normal fetal brain
  • Isotype:
    IgG1
  • Product Type:
    Antibody
  • Reactivity:
    This antibody reacts with mouse Reelin. The CR-50 epitope is located between mouse Reelin amino acid 230 to 346 4.
  • Research Area:
    Neuroscience
  • Short Description:

    Reelin/CR-50 Monoclonal Antibody.

  • Size:
    100 μg
  • Species Reactivity:
    Mouse
  • Storage Temperature:
    -20°C
  • Target:
    Reelin/CR-50
Citations
  1. Courtès S et al. Reelin controls progenitor cell migration in the healthy and pathological adult mouse brain. PLoS One 6, e20430 (2011) ,
  2. Cuchillo-Ibáñez I et al. Heteromers of amyloid precursor protein in cerebrospinal fluid. PLoS One 8, e72297 (2013),
  3. D'Arcangelo G et al. Reelin is a secreted glycoprotein recognized by the CR-50 monoclonal antibody. J Neurosci. 17, 23-31 (1997),
  4. Del Rio JA, et al. A role for Cajal-Retzius cells and reelin in the development of hippocampal connections. Nature 385, 70-4 (1997),
  5. Miyata T et al. Regulation of Purkinje cell alignment by reelin as revealed with CR-50 antibody. J Neurosci. 17, 3599-609 (1997),
  6. Nakajima K et al. Disruption of hippocampal development in vivo by CR-50 mAb against reelin. PNAS 94, 8196-201 (1997),
  7. Nichols AJ, Olson EC. Reelin promotes neuronal orientation and dendritogenesis during preplate splitting. Cereb Cortex. 20, 2213-23 (2010),
  8. Ogawa M et al. The reeler gene-associated antigen on Cajal-Retzius neurons is a crucial molecule for laminar organization of cortical neurons. Neuron 14, 899-912 (1995),
  9. Rice DS et al. Disabled-1 acts downstream of Reelin in a signaling pathway that controls laminar organization in the mammalian brain. Development. 125, 3719-29 (1998),
  10. Utsunomiya-Tate N et al. Reelin molecules assemble together to form a large protein complex, which is inhibited by the function-blocking CR-50 antibody. PNAS 97, 9729-34 (2000),
  11. Wierenga CJ et al. Molecular and electrophysiological characterization of GFP-expressing CA1 interneurons in GAD65-GFP mice. PLoS One 5, e15915 (2010),
  12. Yip JW et al. Reelin controls position of autonomic neurons in the spinal cord. PNAS 97, 8612-6 (2000)
References
  1. Morimura, T., et al., J. Biol. Chem. 280, 16901-16908 (2005)
  2. Soda, T., et al., J. Neurosci. 23, 6272-6279 (2003)
  3. Tabata, H. and Nakajima, K. Neuroscience 103, 865-872 (2001)
  4. Utsunomiya-Tate, N., et al., PNAS 97, 9729-9734 (2000)
  5. Yip, J. W., et al., PNAS 97, 8612-8616 (2000)
  6. Rice, D. S., et al., Development 125, 3719-3729 (1998)
  7. Nakajima, K., et al., PNAS 94, 8196-8201 (1997)
  8. Miyata, T., et al., J. Neurosci. 17, 3599-3609 (1997)
  9. D'Arcangelo, G., et al., J. Neurosci. 17, 23-31 (1997)
  10. Del Rio, J. A., et al., Nature 385, 70-74 (1997)
  11. Ogawa, M., et al., Neuron 14, 899-912 (1995)