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M2441

Sigma-Aldrich

Anti-MAGI-2 antibody produced in rabbit

IgG fraction of antiserum, buffered aqueous solution

Synonym(s):

Anti-ARIP, Anti-S-SCAM

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About This Item

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.46

biological source

rabbit

Quality Level

conjugate

unconjugated

antibody form

IgG fraction of antiserum

antibody product type

primary antibodies

clone

polyclonal

form

buffered aqueous solution

species reactivity

rat

technique(s)

microarray: suitable
western blot: 1:250 using rat brain extracts

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

General description

MAGI-2 is composed of three domains including six PDZ, one guanylate kinase (GK) and two WW domain.
The MAGUK (Membrane Associated Guanylate kinase) family of proteins localize to regions of cell-cell contact, such as tight junctions in epithelial cells and synaptic junctions in neurons, and are believed to be involved in the assembly of multiprotein complexes via their protein-protein interaction domains.2

MAGI-2 was initially identified in rat, as a protein interacting with N-methyl-D-aspartate receptors (NMDA-R) and neuronal cell adhesion proteins, and was named S-SCAM.4Three isoforms of S-SCAM were identified, of 1277, 1113 and 1053 amino acids length, respectively.5

Immunogen

synthetic peptide corresponding to amino acids 554-571 of MAGI-2/S-SCAM conjugated to KLH.

Application

Anti-MAGI-2 antibody produced in rabbit has been used in immunoblotting and immunolabeling.

Biochem/physiol Actions

Membrane associated guanylate kinase inverted-2 (MAGI-2) as well as MAGI-3, was shown to interact with the tumor suppressor PTEN through one of its PDZ domains, apparently acting as a scaffolding protein that could assemble a multi subunit signaling complex. It is known to be involved in the assembly of multiprotein complexes via their protein-protein interaction domains.

Physical form

Solution in 0.01 M phosphate buffered saline, pH 7.4, containing 15 mM sodium azide.

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 2

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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S-SCAM/MAGI-2 is an essential synaptic scaffolding molecule for the GluA2-containing maintenance pool of AMPA receptors
Danielson E, et al.
The Journal of Neuroscience, 32(20), 6967-6980 (2012)
Bingbing Zhu et al.
Kidney international, 96(3), 642-655 (2019-06-07)
The essential role of membrane associated guanylate kinase 2 (MAGI2) in podocytes is indicated by the phenotypes of severe glomerulosclerosis of both MAGI2 knockout mice and in patients with congenital nephrotic syndrome (CNS) caused by mutations in MAGI2. Here, we
IgSF9b regulates anxiety behaviors through effects on centromedial amygdala inhibitory synapses
Babaev O, et al.
Nature Communications, 9(1), 5400-5400 (2018)
Evidence for regulation of the PTEN tumor suppressor by a membrane-localized multi-PDZ domain containing scaffold protein MAGI-2
Wu X, et al.
Proceedings of the National Academy of Sciences of the USA, 97(8), 4233-4238 (2000)
Nina Wittenmayer et al.
Frontiers in cellular neuroscience, 17, 1182493-1182493 (2023-12-04)
Synapse formation is critical for the wiring of neural circuits in the developing brain. The synaptic scaffolding protein S-SCAM/MAGI-2 has important roles in the assembly of signaling complexes at post-synaptic densities. However, the role of S-SCAM in establishing the entire

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