MAB5366
Anti-Reelin Antibody, a.a. 164-189 mreelin, clone 142
clone 142, Chemicon®, from mouse
Synonym(s):
reelin
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About This Item
UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41
Recommended Products
biological source
mouse
Quality Level
antibody form
purified antibody
antibody product type
primary antibodies
clone
142, monoclonal
species reactivity
mouse, vertebrates, human
species reactivity (predicted by homology)
rat
manufacturer/tradename
Chemicon®
technique(s)
immunohistochemistry: suitable
western blot: suitable
isotype
IgG1
NCBI accession no.
UniProt accession no.
shipped in
wet ice
target post-translational modification
unmodified
Gene Information
human ... RELN(5649)
General description
The highly layered structure of the cerebral cortex is established through the pattern of neuronal cell migrations. The first step is the creation of the primordial layer, the preplate, consisting of radial glial cells and the earliest generated neurons. Among these neurons are the Cajal-Retzius neurons. In the next step, the preplate splits into a superficial (marginal) zone, where the Cajal-Retzius neurons reside, and a deep subplate wherein the neurons form. Neurons migrating from the subplate form the cortical plate. This migration takes place on the radial glial fibers.
The reeler mutant in mouse displays an abnormal pattern of cell migration throughout the cerebral and cerebellar cortices. The preplate forms normally, and the neurons differentiate at the correct times in the ventricular zone. However, instead of forming the normal "inside-out" arrangement of neurons in the cortical plate, the older neurons are found furthest from the ventricular zone, while the younger neurons do not migrate far at all. The reeler cerebral cortex is inverted from that of the wild type mouse.
The defect of the reeler mice appears to be in the production of an extracellular matrix protein by the Cajal-Retzius cells (D′Arcangelo et al., 1995, Nature 374:719-723.; Ogawa et al., 1995 Neuron 14:899-912.) This 388kDa protein is made by wild-type mice but not by the reeler mutants. It is thought that this Reelin protein is crucial for positioning the migrating neuron within the cortical plate (Figure 1). In the absence of Reelin, the migrating neuron would be "lost," and the cortical plate would be abnormal. We do not yet know the mechanisms by which Reelin informs the cells as to their position, how the cell responds to Reelin, and why the absence of reelin should give an "inverted" plate. However, the identification of the protein encoded by the reeler gene should allow us to begin these studies.
The reeler mutant in mouse displays an abnormal pattern of cell migration throughout the cerebral and cerebellar cortices. The preplate forms normally, and the neurons differentiate at the correct times in the ventricular zone. However, instead of forming the normal "inside-out" arrangement of neurons in the cortical plate, the older neurons are found furthest from the ventricular zone, while the younger neurons do not migrate far at all. The reeler cerebral cortex is inverted from that of the wild type mouse.
The defect of the reeler mice appears to be in the production of an extracellular matrix protein by the Cajal-Retzius cells (D′Arcangelo et al., 1995, Nature 374:719-723.; Ogawa et al., 1995 Neuron 14:899-912.) This 388kDa protein is made by wild-type mice but not by the reeler mutants. It is thought that this Reelin protein is crucial for positioning the migrating neuron within the cortical plate (Figure 1). In the absence of Reelin, the migrating neuron would be "lost," and the cortical plate would be abnormal. We do not yet know the mechanisms by which Reelin informs the cells as to their position, how the cell responds to Reelin, and why the absence of reelin should give an "inverted" plate. However, the identification of the protein encoded by the reeler gene should allow us to begin these studies.
Specificity
Reelin. The epitope is between amino acids 164 and 189.
Immunogen
Epitope: a.a. 164-189
Recombinant reelin amino acids 40-189.
Application
Research Category
Neuroscience
Neuroscience
Research Sub Category
Growth Cones & Axon Guidance
Growth Cones & Axon Guidance
This Anti-Reelin Antibody, a.a. 164-189 mreelin, clone 142 is validated for use in IH, WB for the detection of Reelin.
Western blot:
1:250-1:500, In Western blots, reelin appears as three bands ~400 - 450, 300, and 180 - 200 kDa′s.
Immunohistochemistry:
1:250-1:500, 4% PFA fixed tissues. A previous lot of this antibody was used in IH.
Optimal working dilutions must be determined by the end user.
1:250-1:500, In Western blots, reelin appears as three bands ~400 - 450, 300, and 180 - 200 kDa′s.
Immunohistochemistry:
1:250-1:500, 4% PFA fixed tissues. A previous lot of this antibody was used in IH.
Optimal working dilutions must be determined by the end user.
Quality
Routinely evaluated by Western Blot on mouse brain lysates.
Western Blot Analysis:
1:1000 dilution of this lot detected Reelin on 10 μg of mouse brain lysates.
Western Blot Analysis:
1:1000 dilution of this lot detected Reelin on 10 μg of mouse brain lysates.
Target description
In Western blots, reelin can appear as three bands ~400 - 450, 300, and 180 - 200 kDa′s.
Physical form
Format: Purified
Protein A purified
Purified mouse monoclonal IgG1 in buffer containing 0.02M Phosphate buffer with 0.25M NaCl and 0.1% sodium azide.
Storage and Stability
Stable for 6 months at 2-8ºC in undiluted aliquots from date of receipt.
Analysis Note
Control
Mouse liver or kidney
Mouse liver or kidney
Other Notes
Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.
Legal Information
CHEMICON is a registered trademark of Merck KGaA, Darmstadt, Germany
Disclaimer
Unless otherwise stated in our catalog or other company documentation accompanying the product(s), our products are intended for research use only and are not to be used for any other purpose, which includes but is not limited to, unauthorized commercial uses, in vitro diagnostic uses, ex vivo or in vivo therapeutic uses or any type of consumption or application to humans or animals.
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Description
Pricing
Storage Class Code
10 - Combustible liquids
WGK
WGK 2
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Certificates of Analysis (COA)
Search for Certificates of Analysis (COA) by entering the products Lot/Batch Number. Lot and Batch Numbers can be found on a product’s label following the words ‘Lot’ or ‘Batch’.
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Akira Sobue et al.
Scientific reports, 8(1), 13046-13046 (2018-08-31)
Reelin protein (RELN), an extracellular matrix protein, plays multiple roles that range from embryonic neuronal migration to spine formation in the adult brain. Results from genetic studies have suggested that RELN is associated with the risk of psychiatric disorders, including
Jing Yang Tee et al.
NPJ schizophrenia, 2, 16027-16027 (2016-09-08)
Reelin expression is reduced in various regions in the post-mortem brain of schizophrenia patients but the exact role of reelin function in the neurobiology of schizophrenia remains elusive. Absence of reelin in knockout mouse causes inverted lamination of the neocortex
Brian R Mullen et al.
ASN neuro, 5(1), e00106-e00106 (2013-01-10)
Genetic and environmental factors are both likely to contribute to neurodevelopmental disorders, including ASDs (autism spectrum disorders). In this study, we examined the combinatorial effect of two factors thought to be involved in autism--reduction in the expression of the extracellular
Elisa Dalla Vecchia et al.
Frontiers in behavioral neuroscience, 13, 214-214 (2019-10-15)
Reelin (Reln) is an extracellular glycoprotein that is important for brain patterning. During development Reln coordinates the radial migration of postmitotic cortical neurons, cerebellar and hippocampal neurons, whereas it promotes dendrite maturation, synaptogenesis, synaptic transmission, plasticity and neurotransmitter release in
Csaba Varga et al.
Cerebral cortex (New York, N.Y. : 1991), 25(11), 4430-4449 (2015-03-20)
Transcription factors contribute to the differentiation of cortical neurons, orchestrate specific interneuronal circuits, and define synaptic relationships. We have investigated neurons expressing chicken ovalbumin upstream promoter transcription factor II (COUP-TFII), which plays a role in the migration of GABAergic neurons.
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