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SAB1402258

Sigma-Aldrich

Monoclonal Anti-MAG antibody produced in mouse

clone 3C7, purified immunoglobulin, buffered aqueous solution

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About This Item

MDL number:
UNSPSC Code:
12352203
NACRES:
NA.41

biological source

mouse

conjugate

unconjugated

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

3C7, monoclonal

form

buffered aqueous solution

mol wt

antigen ~36.01 kDa

species reactivity

human

technique(s)

immunohistochemistry (formalin-fixed, paraffin-embedded sections): suitable
indirect ELISA: suitable
western blot: 1-5 μg/mL

isotype

IgG1κ

NCBI accession no.

UniProt accession no.

shipped in

dry ice

storage temp.

−20°C

target post-translational modification

unmodified

Gene Information

human ... MAG(4099)

General description

The protein encoded by this gene is a type I membrane protein and member of the immunoglobulin superfamily. It is thought to be involved in the process of myelination. It is a lectin that binds to sialylated glycoconjugates and mediates certain myelin-neuron cell-cell interactions. Two alternatively spliced transcripts encoding different isoforms have been described for this gene. (provided by RefSeq)

Immunogen

MAG (NP_002352, 119 a.a. ~ 208 a.a) partial recombinant protein with GST tag. MW of the GST tag alone is 26 KDa.

Sequence
GDLGGYNQYTFSEHSVLDIVNTPNIVVPPEVVAGTEVEVSCMVPDNCPELRPELSWLGHEGLGEPAVLGRLREDEGTWVQVSLLHFVPTR

Application

Monoclonal Anti-MAG antibody produced in mouse is suitable for immunohistochemistry (formalin-fixed, paraffin-embedded sections), indirect ELISA, and western blot applications.

Biochem/physiol Actions

Myelin-associated glycoprotein (MAG) is a glycoprotein with five Ig-like domains belonging to the siglec family of molecules (sialic acid-binding, immunoglobulin-like lectins). It is highly involved in the myelin formation and its maintenance. It is expressed in oligodendrocyte processes at the axoglial junction. It possesses sialic acid binding affinity. Deletion of MAG region leads to Kearns-Sayre syndrome characterized with oligodendrocyte loss and nuclear translocation of apoptosis-inducing factor. MAG also has been reported as an important inhibitor of axonal regeneration.

Physical form

Solution in phosphate buffered saline, pH 7.4

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

WGK 1

Flash Point(F)

Not applicable

Flash Point(C)

Not applicable


Certificates of Analysis (COA)

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Zixuan Cao et al.
The Journal of neuroscience : the official journal of the Society for Neuroscience, 27(34), 9146-9154 (2007-08-24)
Myelin-associated glycoprotein (MAG) is a potent inhibitor of axonal regeneration. It contains five Ig-like domains and is a sialic binding protein. Previously, we showed that the sialic acid binding site on MAG maps to arginine 118 in Ig domain 1
Nichola Z Lax et al.
Archives of neurology, 69(4), 490-499 (2012-04-12)
To explore myelin components and mitochondrial changes within the central nervous system in patients with well-characterized mitochondrial disorders due to nuclear DNA or mitochondrial DNA (mtDNA) mutations. Immunohistochemical analysis, histochemical analysis, mtDNA sequencing, and real-time and long-range polymerase chain reaction
Demetra P Kelenis et al.
Glia, 66(9), 1862-1880 (2018-04-24)
NG2-glia are highly proliferative oligodendrocyte precursor cells (OPCs) that are widely distributed throughout the central nervous system (CNS). During development, NG2-glia predominantly differentiate into oligodendrocytes (OLs) to myelinate axon fibers, but they can also remain as OPCs persisting into the
COUP-TFII plays a role in cAMP-induced Schwann cell differentiation and in vitro myelination by up-regulating Krox20.
Han, et al.
Journal of Neurochemistry, 165, 660-681 (2023)

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