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Key Documents

AB1508

Sigma-Aldrich

Anti-Glutamate Receptor 4 Antibody

Chemicon®, from rabbit

Sinónimos:

AMPA-selective glutamate receptor 4, Glutamate receptor ionotropic, AMPA 4, glutamate receptor 4, glutamate receptor, ionotrophic, AMPA 4

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About This Item

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

biological source

rabbit

Quality Level

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

purified by

affinity chromatography

species reactivity

mouse, rat

manufacturer/tradename

Chemicon®

technique(s)

immunocytochemistry: suitable
immunohistochemistry (formalin-fixed, paraffin-embedded sections): suitable
immunoprecipitation (IP): suitable
western blot: suitable

UniProt accession no.

shipped in

wet ice

target post-translational modification

unmodified

Gene Information

human ... GRIA4(2893)

General description

Glutamate receptor 4 (UniProt: P48058; also known as GluR-4, GluR4, AMPA-selective glutamate receptor 4, GluR-D, Glutamate receptor ionotropic AMPA 4, GluA4) is encoded by the GRIA4 (also known as GLUR4) gene (Gene ID: 2893) in human. The postsynaptic actions of glutamate are mediated by a variety of receptors that are named according to their selective agonists. GluR-4 is a multi-pass membrane protein that functions as ligand-gated ion channel in the central nervous system and plays an important role in excitatory synaptic transmission. It displays greater affinity for AMPA. GluR-4 is synthesized with a signal peptide (aa 1-20), which is cleaved off in the mature form. GluR-4 can exist as a homotetramer or heterotetramer of pore-forming glutamate receptor subunits, tetramers can also form by the dimerization of dimers. GluR-4 is generally palmitoylated and becomes de-palmitoylated upon glutamate stimulation. Palmitoylation on Cys 611 leads to its Golgi retention and reduced cell surface expression. However, palmitoylation at Cys 837 does not affect cell surface expression, but can regulate stimulation-dependent endocytosis. GluR-4 can undergo phosphorylation at Serine 862 by PKC gamma and this phosphorylation increases plasma membrane-associated GRI4 expression.

Specificity

Cat. # AB1508 recognizes C-Terminus of GluR4.
The immunogen sequence shares 100% conservation with chicken, mouse, rat, oppossum, human, chimp, and monkey.

Immunogen

Epitope: C-Terminus
Synthetic linear peptide.

Application

Immunohistochemistry:
Dilutions of 1:10 – 1:500 were tested on rat brain lysate.
Can be used for immunocytochemistry using paraformaldehyde or paraformaldehyde/glutaraldehyde fixed tissue with light and electron microscopy. Cryostat and vibratome sections can be used with or without Triton X-100 treatment. Suggested concentrations start at 1-3 μg/mL.

Western blot analysis can be done at final concentrations of 1-3 μg/mL.

Optimal working dilutions must be determined by end user.
Research Category
Neuroscience
Research Sub Category
Neurotransmitters & Receptors
This Anti-Glutamate Receptor 4 Antibody is validated for use in IH(P), IC, IH, IP, WB for the detection of Glutamate Receptor 4.

Quality

Evaluated by Western Blotting in mouse and rat brain membrane.

Western Blotting Analysis: A 1:500 dilution of this antibody detected Glutamate Receptor 4 in mouse and rat brain membrane.

Target description

Approx. 100 kDa

Linkage

Replaces: 06-308

Physical form

Antigen Affinity Purified
Purified rabbit polyclonal antibody in buffer containing 0.1 M Tris-Glycine (pH 7.4), 150 mM NaCl with 0.05% sodium azide.

Storage and Stability

Stable for 1 year at 2-8ºC 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.

Analysis Note

Control
Rat Brain

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

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 2

flash_point_f

Not applicable

flash_point_c

Not applicable


Certificados de análisis (COA)

Busque Certificados de análisis (COA) introduciendo el número de lote del producto. Los números de lote se encuentran en la etiqueta del producto después de las palabras «Lot» o «Batch»

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ZO-1 and the spatial organization of gap junctions and glutamate receptors in the outer plexiform layer of the mammalian retina.
Puller, C; de Sevilla Muller, LP; Janssen-Bienhold, U; Haverkamp, S
The Journal of Neuroscience null
Kellie A Park et al.
The Journal of neuroscience : the official journal of the Society for Neuroscience, 36(28), 7464-7475 (2016-07-15)
Select adhesion proteins control the development of synapses and modulate their structural and functional properties. Despite these important roles, the extent to which different synapse-organizing mechanisms act across brain regions to establish connectivity and regulate network properties is incompletely understood.
Akiko Suga et al.
Developmental biology, 330(2), 318-328 (2009-04-14)
In the nervous system, transcription factor expression in progenitor and/or nascent neurons regulates cell type specification. Although the functions of these transcription factors at early stages are well established, whether or not they are required during late developmental periods remains
Jian Zhang et al.
Vision research, 49(1), 64-73 (2008-11-04)
In the tiger salamander retina, visual signals are transmitted to the inner retina via six morphologically distinct types of photoreceptors: large/small rods, large/small single cones, and double cones composed of principal and accessory members. The objective of this study was
Akihiko S Kato et al.
Neuron, 59(6), 986-996 (2008-09-27)
AMPA-type glutamate receptors (GluRs) play major roles in excitatory synaptic transmission. Neuronal AMPA receptors comprise GluR subunits and transmembrane AMPA receptor regulatory proteins (TARPs). Previous studies identified five mammalian TARPs, gamma-2 (or stargazin), gamma-3, gamma-4, gamma-7, and gamma-8, that enhance

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