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Merck
CN

MABN71

Sigma-Aldrich

Anti-GluR2 Antibody, clone L21/32

clone L21/32, from mouse

Synonym(s):

glutamate receptor, ionotropic, AMPA 2, glutamate receptor 2, Glutamate receptor ionotropic, AMPA 2, AMPA-selective glutamate receptor 2

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About This Item

UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41

Key Documents

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biological source

mouse

Quality Level

100

conjugate

unconjugated

antibody form

purified antibody

antibody product type

primary antibodies

clone

L21/32, monoclonal

species reactivity

rat

species reactivity (predicted by homology)

mouse (based on 100% sequence homology), human (immunogen homology)

technique(s)

immunohistochemistry: suitable
western blot: suitable

isotype

IgG1κ

NCBI accession no.

NP_000817

UniProt accession no.

P42262

shipped in

wet ice

target post-translational modification

unmodified

Gene Information

human ... GRIA2(2891)

General description

Glutamate receptors (GluRs) can be categorized as ionotropic or metabotropic and subcatergorized by their agonist preferences (NMDA, AMPA or Kainic acid). There are four types of AMPA selective GluR subunits (GluR1, GluR2, GluR3 and GluR4). Tetrameric or pentameric combinations of different subunits contributes to the functional diversity of AMPA receptors. In general, AMPA receptors mediate fast synaptic current at most excitatory synapses, with stoichiometry characterized by subtype composition. Although subunit composition of AMPA receptors varies, they must contain at least one edited GluR2 subunit to be calcium impermeable. The critical residue controlling calcium permeability is in the pore loop region. In GluR1, GluR3, and GluR4, this position is occupied by a Gln residue. In GluR2, it is occupied by an Arg residue. It has been shown experimentally that the presence of Arg in this position blocks Ca2+ ion permeability, while a Gln does not. Relative calcium permeability in AMPA receptor channels may be significant in pathological neurotoxic damage and long term changes in nervous system responses.
~ 96 kDa observed

Immunogen

Recombinant protein corresponding to human GluR2.

Application

Detect GluR2 using this Anti-GluR2 Antibody, clone L21/32 validated for use in WB, IH.
Immunohistochemistry Analysis: 1:300 dilution of this antibody from a previous lot detected GluR2 in rat cerebellum and hippocampus tissue.
Research Category
Neuroscience

Neuroscience
Research Sub Category
Neurodegenerative Diseases

Neurotransmitters & Receptors

Physical form

Format: Purified
Protein G
Purified mouse monoclonal IgG1κ in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.

Preparation Note

Stable for 1 year at 2-8°C from date of receipt.

Analysis Note

Control
Rat brain membrane tissue lysate
Evaluated by Western Blot in rat brain membrane tissue lysate.

Western Blot Analysis: 0.5 µg/mL of this antibody detected GluR2 on 10 µg of rat brain membrane tissue lysate.

Other Notes

Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.

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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Storage Class Code

12 - Non Combustible Liquids

WGK

WGK 1

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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Venkat Swaroop Achuta et al.
Science signaling, 11(513) (2018-01-18)
Altered neuronal network formation and function involving dysregulated excitatory and inhibitory circuits are associated with fragile X syndrome (FXS). We examined functional maturation of the excitatory transmission system in FXS by investigating the response of FXS patient-derived neural progenitor cells
Maria Arvaniti et al.
Journal of neurochemistry, 138(6), 806-820 (2016-06-28)
Nicotinic acetylcholine receptors (nAChRs) affect multiple physiological functions in the brain and their functions are modulated by regulatory proteins of the Lynx family. Here, we report for the first time a direct interaction of the Lynx protein LY6/PLAUR domain-containing 6
Joseph A McQuail et al.
Neuropharmacology, 197, 108720-108720 (2021-07-18)
Ionotropic glutamate receptors of the NMDA and AMPA subtypes transduce excitatory signaling on neurons in the prefrontal cortex (PFC) in support of cognitive flexibility. Cognitive flexibility is reliably observed to decline at advanced ages, coinciding with changes in PFC glutamate
Xiang-Dong Sun et al.
Nature neuroscience, 19(8), 1010-1018 (2016-06-14)
Neurotransmission requires precise control of neurotransmitter release from axon terminals. This process is regulated by glial cells; however, the underlying mechanisms are not fully understood. We found that glutamate release in the brain was impaired in mice lacking low-density lipoprotein
Hai-Long Zhang et al.
Neuroscience bulletin, 37(12), 1645-1657 (2021-07-07)
Steroid hormones play important roles in brain development and function. The signaling of steroid hormones depends on the interaction between steroid receptors and their coactivators. Although the function of steroid receptor coactivators has been extensively studied in other tissues, their
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Related Content

Pathways and Biomarkers of Glutamatergic Synapse Flyer

Glutamate is an excitatory neurotransmitter found in the synaptic vesicles of glutamatergic synapses. The post-synaptic neurons in these synapses contain ionotropic and metabotropic glutamate receptors. Glutamate binds to AMPA (α-amino-3-hydroxy-5- methylisoxazole-4-propionic acid) subtype glutamate receptors, leading to sodium influx into the post-synaptic cell and resulting in neuronal excitability and synaptic transmission. The NMDA (N-methyl-d-aspartate) subtype glutamate receptors, on the other hand, regulate synaptic plasticity, and can influence learning and memory. The metabotropic g-protein coupled mGluRs modulate downstream calcium signaling pathways and indirectly influence the synapse’s excitability. The synaptic architecture includes intracellular scaffolding proteins (PSD-95, GRIP), intercellular cell adhesion molecules (NCAMs, N-Cadherins), and a variety of signaling proteins (CaMKII/PKA, PP1/PP2B). Processes critical for synaptic transmission and plasticity are influenced by these molecules and their interactions. When the function of these molecules is disrupted, it leads to synaptic dysfunction and degeneration, and can contribute to dementia as seen in Alzheimer’s disease.

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