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MAB397

Sigma-Aldrich

Anti-Glutamate Receptor 2 Antibody, extracellular, clone 6C4

clone 6C4, Chemicon®, from mouse

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Synonym(s):
GluR2
eCl@ss:
32160702
NACRES:
NA.41

biological source

mouse

Quality Level

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

6C4, monoclonal

species reactivity

monkey

species reactivity (predicted by homology)

mouse, rat, canine

manufacturer/tradename

Chemicon®

technique(s)

ELISA: suitable
immunocytochemistry: suitable
immunohistochemistry: suitable
immunoprecipitation (IP): suitable
radioimmunoassay: suitable
western blot: suitable

isotype

IgG2a

NCBI accession no.

UniProt accession no.

target post-translational modification

unmodified

Gene Information

dog ... Gria2(482667)
mouse ... Gria2(14800)
rat ... Gria2(29627)
rhesus monkey ... Gria2(574344)

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This Item
AB10529MAB397A4ABN241
vibrant-m

AB10529

Anti-GluR-2 Antibody, CT

vibrant-m

ABN241

Anti-GluR1 Antibody

species reactivity

monkey

species reactivity

mouse, rat

species reactivity

mouse, rat

species reactivity

human, mouse, rat

biological source

mouse

biological source

rabbit

biological source

mouse

biological source

rabbit

Gene Information

dog ... Gria2(482667)
mouse ... Gria2(14800)
rat ... Gria2(29627)
rhesus monkey ... Gria2(574344)

Gene Information

human ... GRIA2(2891)

Gene Information

human ... GRIA2(2891)

Gene Information

human ... GRIA1(2890)
mouse ... Gria1(14799)
rat ... Gria1(50592)

clone

6C4, monoclonal

clone

polyclonal

clone

6C4, monoclonal

clone

polyclonal

NCBI accession no.

NP_058957

NCBI accession no.

NP_001077280

NCBI accession no.

NP_001077280

NCBI accession no.

NP_113796

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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 positionis 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.

Specificity

Recognizes the large N-terminal extracellular domain of Glutamate Receptor 2 (GluR2). No cross-reactivity observed with other AMPA/Kainate GluR subunits. On western blots of brain extracts from rat, macaque monkey, and dog, MAB397 recognizes a band at approximately 102 kDa corresponding to full length GluR2. Other proteins noted by Western blot at 66 kDa or lower molecular weight appear to be breakdown products of GluR2 (Vissavajjhala, 1996). By immunohistochemistry GluR2 is widely distributed at both the cellular and synaptic levels. MAB397 recognizes GluR2 present in a vast majority of, but not all, GABAergic interneurons (Vissavajjhala, 1996).

Application

Anti-Glutamate Receptor 2 Antibody, extracellular, clone 6C4 detects level of Glutamate Receptor 2 & has been published & validated for use in ELISA, IC, IH, IP, RIA & WB with more than 50 product citations.
Immunocytochemistry:
on 4% paraformaldehyde fixed cells was used in a previous lot:2-3 µg/mL (Vissavajjhala, 1996; Osten, 1998; Passafaro, 2001).

ELISA/RIA:
A previous lot of this antibody was used in ELISA/RIA.(Vissavajjhala, 1996).

Immunohistochemistry on 50 µm, 4% paraformaldehyde fixed brain sections: 1:500-1:800 (Vissavajjhala, 1996; Yung, 1998; Kumar; 2002).

Immunoprecipitation: 2-4 µg/mL (Osten, 1998).

Western blot: 1-2 µg/mL (Vissavajjhala, 1996; Osten, 1998); membrane preparations are suggested for enhanced signals.

Optimal working dilutions and protocols must be determined by end user.

Quality

Routinely evaluated by Western Blot on mouse brain lysates.

Western Blot Analysis:
1:1000 dilution of this lot detected glutamate receptor 2 on 10 μg of mouse brain lysates.

Target description

102 kDa

Physical form

Format: Purified
Purified immunoglobulin from culture supernatant
Purified mouse immunoglobin IgG2a liquid in buffer containing PBS, no preservative.

Storage and Stability

Stable for 6 months at -20ºC in undiluted aliquots from date of receipt.
Handling Recommendations: Upon receipt, and prior to removing the cap, centrifuge the vial and gently mix the solution. Aliquot into microcentrifuge tubes and store at -20°C. Avoid repeated freeze/thaw cycles, which may damage the IgG2a and affect product performance.

Analysis Note

Control
Positive Control: Cerebral cortex and pyramidal neurons, mouse brain lysate.

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

Storage Class

12 - Non Combustible Liquids

wgk_germany

WGK 2

flash_point_f

Not applicable

flash_point_c

Not applicable


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S-SCAM/MAGI-2 is an essential synaptic scaffolding molecule for the GluA2-containing maintenance pool of AMPA receptors.
Danielson, E; Zhang, N; Metallo, J; Kaleka, K; Shin, SM; Gerges, N; Lee, SH
The Journal of Neuroscience null
Differential regulation of AMPA receptor and GABA receptor trafficking by tumor necrosis factor-alpha.
Stellwagen, D; Beattie, EC; Seo, JY; Malenka, RC
The Journal of Neuroscience null
Tyrosine phosphatases regulate AMPA receptor trafficking during metabotropic glutamate receptor-mediated long-term depression.
Moult, PR; Gladding, CM; Sanderson, TM; Fitzjohn, SM; Bashir, ZI; Molnar, E; Collingridge, GL
The Journal of Neuroscience null
Melanie A Gainey et al.
Proceedings of the National Academy of Sciences of the United States of America, 112(27), E3590-E3599 (2015-06-26)
Synaptic scaling is a form of homeostatic plasticity that stabilizes neuronal firing in response to changes in synapse number and strength. Scaling up in response to action-potential blockade is accomplished through increased synaptic accumulation of GluA2-containing AMPA receptors (AMPAR), but
Reuben Saba et al.
Molecular and cellular biology, 32(3), 619-632 (2011-12-07)
The dynamic expression of AMPA-type glutamate receptors (AMPA-R) at synapses is a key determinant of synaptic plasticity, including neuroadaptations to drugs of abuse. Recently, microRNAs (miRNAs) have emerged as important posttranscriptional regulators of synaptic plasticity, but whether they target glutamate

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