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MABN71

Sigma-Aldrich

Anti-GluR2 Antibody, clone L21/32

clone L21/32, from mouse

Synonim(y):

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

Zaloguj sięWyświetlanie cen organizacyjnych i kontraktowych


About This Item

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

pochodzenie biologiczne

mouse

Poziom jakości

forma przeciwciała

purified antibody

rodzaj przeciwciała

primary antibodies

klon

L21/32, monoclonal

reaktywność gatunkowa

rat

reaktywność gatunkowa (przewidywana na podstawie homologii)

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

metody

immunohistochemistry: suitable
western blot: suitable

izotyp

IgG1κ

numer dostępu NCBI

numer dostępu UniProt

Warunki transportu

wet ice

docelowa modyfikacja potranslacyjna

unmodified

informacje o genach

human ... GRIA2(2891)

Opis ogólny

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.

Immunogen

Recombinant protein corresponding to human GluR2.

Zastosowanie

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

Jakość

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.

Opis wartości docelowych

~ 96 kDa observed

Postać fizyczna

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.

Przechowywanie i stabilność

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

Komentarz do analizy

Control
Rat brain membrane tissue lysate

Inne uwagi

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

Oświadczenie o zrzeczeniu się odpowiedzialności

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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Kod klasy składowania

12 - Non Combustible Liquids

Klasa zagrożenia wodnego (WGK)

WGK 1

Temperatura zapłonu (°F)

Not applicable

Temperatura zapłonu (°C)

Not applicable


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Dokumenty związane z niedawno zakupionymi produktami zostały zamieszczone w Bibliotece dokumentów.

Odwiedź Bibliotekę dokumentów

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
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
Romain Chassefeyre et al.
The Journal of neuroscience : the official journal of the Society for Neuroscience, 35(7), 3155-3173 (2015-02-24)
The charged multivesicular body proteins (Chmp1-7) are an evolutionarily conserved family of cytosolic proteins that transiently assembles into helical polymers that change the curvature of cellular membrane domains. Mutations in human CHMP2B cause frontotemporal dementia, suggesting that this protein may
Yu-Xiang Zhang et al.
Neuropharmacology, 141, 113-125 (2018-08-31)
Epigenetic remodeling contributes to synaptic plasticity via modification of gene expression, which underlies cocaine-induced long-term memory. A prevailing hypothesis in drug addiction is that drugs of abuse rejuvenate developmental machinery to render reward circuitry highly plastic and thus engender drug

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