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AB10529

Sigma-Aldrich

Anti-GluR-2 Antibody, CT

serum, from rabbit

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Synonym(s):
glutamate receptor, ionotropic, AMPA 2, glutamate receptor 2, Glutamate receptor ionotropic, AMPA 2, AMPA-selective glutamate receptor 2
eCl@ss:
32160702
NACRES:
NA.41

biological source

rabbit

Quality Level

antibody form

serum

antibody product type

primary antibodies

clone

polyclonal

species reactivity

mouse, rat

technique(s)

western blot: suitable

NCBI accession no.

UniProt accession no.

shipped in

wet ice

target post-translational modification

unmodified

Gene Information

human ... GRIA2(2891)

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This Item
MABN71MAB397A4MABN1189
Anti-GluR-2 Antibody, CT serum, from rabbit

AB10529

Anti-GluR-2 Antibody, CT

Anti-GluR2 Antibody, clone L21/32 clone L21/32, from mouse

MABN71

Anti-GluR2 Antibody, clone L21/32

Quality Level

100

Quality Level

100

Quality Level

100

Quality Level

100

biological source

rabbit

biological source

mouse

biological source

mouse

biological source

mouse

Gene Information

human ... GRIA2(2891)

Gene Information

human ... GRIA2(2891)

Gene Information

human ... GRIA2(2891)

Gene Information

human ... GRIA2(2891)

clone

polyclonal

clone

L21/32, monoclonal

clone

6C4, monoclonal

clone

14C12.2, monoclonal

UniProt accession no.

P19491

UniProt accession no.

P42262

UniProt accession no.

P19491

UniProt accession no.

P19491

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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

This antibody recognizes GluR-2 at the C-terminus.

Immunogen

Epitope: C-terminus
Recombinant protein corresponding to the C-terminus of rat GluR-2.

Application

Anti-GluR-2 Antibody, C-terminus detects level of GluR-2 & has been published & validated for use in WB.
Immunoprecipitation: A previous lot of this antibody successfully immoprecipitated GluR-2 from a brain tissue lysate, as reported by an independent laboratory.
Research Category
Neuroscience
Research Sub Category
Neurotransmitters & Receptors

Quality

Evaluated by Western Blot in PC12 cell lysate.

Western Blot Analysis: A 1:1,000 dilution of this antibody detected GluR-2 on 10 µg of PC12 cell lysate.

Target description

~106 kDa Observed

Physical form

Rabbit polyclonal serum containing 0.05% sodium azide.
Unpurified

Storage and Stability

Stable for 1 year at -20°C 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 IgG and affect product performance.

Analysis Note

Control
PC12 cell lysate

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.

Storage Class

10 - Combustible liquids


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Josué Haubrich et al.
eLife, 9 (2020-05-19)
Memory reconsolidation is a fundamental plasticity process in the brain that allows established memories to be changed or erased. However, certain boundary conditions limit the parameters under which memories can be made plastic. Strong memories do not destabilize, for instance
Nerve injury increases GluA2-lacking AMPA receptor prevalence in spinal cords: functional significance and signaling mechanisms.
Chen, SR; Zhou, HY; Byun, HS; Pan, HL
Journal of Pharmacology and Experimental Therapeutics null
Shao-Rui Chen et al.
The Journal of pharmacology and experimental therapeutics, 371(2), 242-249 (2019-09-05)
Neuronal hyperactivity in the spinal dorsal horn can amplify nociceptive input in diabetic neuropathic pain. The glutamate N-methyl-d-aspartate and α-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid receptors (NMDA receptors and AMPA receptors, respectively) are involved in spinal nociceptive transmission. It is unclear, however, whether
Qin Ru et al.
The Journal of clinical investigation, 132(24) (2022-12-16)
Chronic pain often leads to depression, increasing patient suffering and worsening prognosis. While hyperactivity of the anterior cingulate cortex (ACC) appears to be critically involved, the molecular mechanisms underlying comorbid depressive symptoms in chronic pain remain elusive. T cell lymphoma
Jing-Jing Zhou et al.
Journal of neurochemistry, 161(1), 40-52 (2022-01-18)
Glutamate AMPA receptors (AMPARs) lacking GluA2 subunit are calcium permeable (CP-AMPARs), which are increased in the hypothalamic paraventricular nucleus (PVN) and maintain sympathetic outflow in hypertension. Here, we determined the role of α2δ-1, an NMDA receptor-interacting protein, in regulating synaptic

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