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MilliporeSigma

AB1768-I

Sigma-Aldrich

Anti-GluR2 Antibody

from rabbit, purified by affinity chromatography

Synonym(s):

Glutamate receptor 2, GluR-2, AMPA-selective glutamate receptor 2, GluR-B, GluR-K2, Glutamate receptor ionotropic, AMPA 2, GluA2

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About This Item

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

Key Documents

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biological source

rabbit

Quality Level

100

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

purified by

affinity chromatography

species reactivity

mouse, rat, human

packaging

antibody small pack of 25 μg

technique(s)

immunohistochemistry: suitable (paraffin)
western blot: suitable

NCBI accession no.

NP_058957

UniProt accession no.

P19491

shipped in

wet ice

target post-translational modification

unmodified

Gene Information

human ... GRIA2(2891)

Related Categories

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. Relative calcium permeability in AMPA receptor channels may be significant in pathological neurotoxic damage and long term changes in nervous system responses.
~108 kDa observed. Three isoforms at 99 kDa, 99 kDa, and 100 kDa are known to exist due to alternative splicing.
There is no known homology to mouse and rat GluR1, GluR3 and GluR4. There was no homology detected to GluR1 and GluR3 in human, but there is 67% sequence homology to GluR4. An uncharacterized band may be observed at ~75 kDa in some cell lysates.

Immunogen

Epitope: Cytoplasmic domain
KLH-conjugated linear peptide corresponding to the cytoplasmic domain of rat GluR2.

Application

Immunohistochemistry Analysis: A 1:4,000 dilution from a representative lot detected GluR2 in normal human and rat brain tissues.
Research Category
Neuroscience
Research Sub Category
Signaling Neuroscience
This GluR2 antibody is validated for use in WB & IHC for the detection of the GluR2 protein.

Biochem/physiol Actions

This antibody recognizes the cytoplasmic domain of Glutamate Receptor 2.

Physical form

Affinity purified
Purified rabbit polyclonal 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
Mouse brain tissue lysate
Evaluated by Western Blotting in mouse brain tissue lysate.

Western Blotting Analysis: 0.5 µg/mL of this antibody detected GluR2 in 10 µg of mouse brain tissue lysate.

Other Notes

Concentration: Please refer to the Certificate of Analysis for the lot-specific concentration.
Replaces: AB1768-25UG

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

12 - Non Combustible Liquids

wgk_germany

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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Meenakshi M Asokan et al.
Nature communications, 9(1), 2468-2468 (2018-06-27)
Layer 5 (L5) cortical projection neurons innervate far-ranging brain areas to coordinate integrative sensory processing and adaptive behaviors. Here, we characterize a plasticity in L5 auditory cortex (ACtx) neurons that innervate the inferior colliculus (IC), thalamus, lateral amygdala and striatum.
Ji-Eun Kim et al.
International journal of molecular sciences, 21(16) (2020-08-13)
α-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid receptor (AMPAR) is one of the ligand-gated ion channels for glutamate, which is an important player in the generation and spread of seizures. The efficacy of AMPAR functionality is regulated by the trafficking, synaptic targeting, and phosphorylation. Paradoxically
Lei-Lei Liu et al.
Molecular vision, 25, 780-790 (2019-12-11)
The neuromodulator dopamine plays an important role in light adaptation for the visual system. Light can stimulate dopamine release from dopaminergic amacrine cells (DACs) by activating three classes of photosensitive retinal cells: rods, cones, and melanopsin-expressing intrinsically photosensitive retinal ganglion
Sung Eun Wang et al.
Experimental neurobiology, 28(4), 537-546 (2019-09-09)
Silent information regulator 2 (Sirtuin2 / SIRT2) is a NAD+-dependent deacetylase that regulates the cellular oxidative stress response. It modulates transcriptional silencing and protein stability through deacetylation of target proteins including histones. Previous studies have shown that SIRT2 plays a
Duk-Shin Lee et al.
Scientific reports, 13(1), 13927-13927 (2023-08-26)
Protein disulfide isomerase (PDI) is a redox-active enzyme and also serves as a nitric oxide donor causing S-nitrosylation of cysteine residues in various proteins. Although PDI knockdown reduces α-amino-3-hydroxy-5-methylisoxazole-4-propionic acid receptor (AMPAR)-mediated neuronal activity, the underlying mechanisms are largely unknown.
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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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