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SAB4501318

Sigma-Aldrich

Anti-MGLUR2 antibody produced in rabbit

affinity isolated antibody

Synonym(s):

GPRC1C, GRM3, MGR3, Metabotropic glutamate receptor 3 precursor, glutamate receptor

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About This Item

UNSPSC Code:
12352203
NACRES:
NA.41

biological source

rabbit

Quality Level

conjugate

unconjugated

antibody form

affinity isolated antibody

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

mol wt

antigen 95 kDa

species reactivity

rat, human, mouse

concentration

~1 mg/mL

technique(s)

ELISA: 1:1000
immunohistochemistry: 1:50-1:100
western blot: 1:500-1:1000

NCBI accession no.

UniProt accession no.

shipped in

wet ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... GRM2(2912)

General description

Metabotropic glutamate receptor 2 (MGLUR2) with 872 amino acid residues is encoded by the gene mapped to human chromosome 3. MGLUR2 belongs to the class c of G-protein-coupled receptor (GPCRs) family. It is expressed mainly in the central nervous system (CNS) of rat brain and widely expressed in human adult and fetal brain. MGLUR2 is characterized with an α-helical helix 8 (H8) domain.

Immunogen

The antiserum was produced against synthesized peptide derived from human mGluR2/3.

Immunogen Range: 823-872

Biochem/physiol Actions

Metabotropic glutamate receptor (MGLUR2) is involved in the glutamatergic system in the brain. Overexpression of glutamate in brain areas such as the prefrontal cortex, hippocampus and amygdala leads to anxiety and schizophrenia, activation of MGLUR2 in these areas reduces the excitatory neurotransmission, therefore mGlu2 receptor might be considered as a potential target for the treatment of these diseases. MGLUR2 signaling inhibits adenylyl cyclase (AC) activity. MGLUR2 is crucial in the modulation of synaptic transmission.

Features and Benefits

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Physical form

Rabbit IgG in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.

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

10 - Combustible liquids

WGK

nwg

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

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Steve Davidson et al.
Pain, 157(9), 2081-2088 (2016-05-25)
We introduce a strategy for preclinical research wherein promising targets for analgesia are tested in rodent and subsequently validated in human sensory neurons. We evaluate group II metabotropic glutamate receptors, the activation of which is efficacious in rodent models of
H Ohishi et al.
Neuroscience, 53(4), 1009-1018 (1993-04-01)
Distribution of the messenger RNA for a metabotropic glutamate receptor, mGluR2, which is coupled to the inhibitory cyclic AMP cascade, was investigated in the central nervous system of the adult rat by in situ hybridization. Transcripts of mGluR2 were specifically
Driss El Moustaine et al.
Proceedings of the National Academy of Sciences of the United States of America, 109(40), 16342-16347 (2012-09-19)
The eight metabotropic glutamate receptors (mGluRs) are key modulators of synaptic transmission and are considered promising targets for the treatment of various brain disorders. Whereas glutamate acts at a large extracellular domain, allosteric modulators have been identified that bind to
Alice Taddeucci et al.
Cells, 11(19) (2022-10-15)
The glutamatergic nerve endings of a rat prefrontal cortex (PFc) possess presynaptic 5-HT2A heteroreceptors and mGlu2/3 autoreceptors, whose activation inhibits glutamate exocytosis, and is measured as 15 mM KCl-evoked [3H]D-aspartate ([3H]D-asp) release (which mimics glutamate exocytosis). The concomitant activation of
Agostino Bruno et al.
PloS one, 7(8), e42023-e42023 (2012-08-08)
The recent elucidation of the X-ray structure of several class A GPCRs clearly indicates that the amphipathic helix 8 (H8) is a conserved structural domain in most crystallized GPCRs. Very little is known about the presence and the possible role

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