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Merck
CN

MAB2263

Sigma-Aldrich

Anti-GluR1-NT (NT) Antibody, clone RH95

clone RH95, from mouse

Synonym(s):

AMPA 1, AMPA-selective glutamate receptor 1, Glutamate receptor ionotropic, AMPA 1, glutamate receptor, ionotropic, AMPA 1

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About This Item

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

mouse

Quality Level

conjugate

unconjugated

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

RH95, monoclonal

species reactivity

rat

technique(s)

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

isotype

IgG2aκ

NCBI accession no.

UniProt accession no.

shipped in

wet ice

target post-translational modification

unmodified

Gene Information

human ... GRIA1(2890)

General description

110 kDa
Glutamate receptors (GluRs) are a diverse group responsible for mediating most of the excitatory synaptic transmission in the CNS of vertebrates. They can be categorized as ionotropic or metabotropic and subcategorized 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. AMPA receptors mediate fast synaptic current at most excitatory synapses, with stoichiometry characterized by subtype composition. 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. The insertion or removal of GluR1/GluR4 oligomeric channels from postsynaptic membranes appears to be LTP/LTD activity dependent while GluR2/GluR3 oligomers are continuously cycling.

Immunogen

Epitope: N-terminus
Thyroglobulin-conjugated linear peptide of rat GluR1 designed around the N-terminus.

Application

Anti-GluR1-NT (N-terminus) Antibody, clone RH95 is an antibody against GluR1-NT (N-terminus) for use in WB, IP, IC, ELISA.
Research Category
Neuroscience
Research Sub Category
Neurotransmitters & Receptors

Biochem/physiol Actions

This antibody recognizes GluR1 at the N-terminus.

Physical form

Format: Purified
Protein G Purified
Purified mouse monoclonal IgG2aκ 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 lysate
Evaluated by Western Blot in rat brain lysate.

Western Blot Analysis: A 1:1000 dilutions of this antibody detected GluR1 in 10 µg of rat brain 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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PKM? knockdown disrupts post-ischemic long-term potentiation via inhibiting postsynaptic expression of aminomethyl phosphonic acid receptors.
Cheng, N; Hu, X; Tian, T; Lu, W
Journal of biomedical research null
Xiaofen Zhong et al.
The Journal of neuroscience : the official journal of the Society for Neuroscience, 32(37), 12841-12847 (2012-09-14)
MeCP2 (methyl CpG binding protein 2) is a key player in recognizing methylated DNA and interpreting the epigenetic information encoded in different DNA methylation patterns. The functional significance of MeCP2 to the mammalian nervous system is highlighted by the discovery
Caroline Jung et al.
Psychopharmacology, 233(17), 3161-3172 (2016-07-05)
When ad libitum-fed rats undergo cocaine place preference conditioning (CPP) but are switched to food restriction for testing, CPP becomes resistant to extinction and correlates with phosphorylation of α-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptor GluA1 at Ser845 in nucleus accumbens (NAc) core.
Impaired spatial memory and enhanced long-term potentiation in mice with forebrain-specific ablation of the Stim genes.
Garcia-Alvarez, G; Shetty, MS; Lu, B; Yap, KA; Oh-Hora, M; Sajikumar, S; Bichler, Z; Fivaz, M
Frontiers in Behavioral Neuroscience null
Paul Farrow et al.
eLife, 4, e09693-e09693 (2015-12-02)
AMPA receptor (AMPAR) function is modulated by auxiliary subunits. Here, we report on three AMPAR interacting proteins-namely CKAMP39, CKAMP52 and CKAMP59-that, together with the previously characterized CKAMP44, constitute a novel family of auxiliary subunits distinct from other families of AMPAR

Related Content

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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