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M9073

Sigma-Aldrich

Anti-Mitofusin 2 antibody,Mouse monoclonal

clone Mito-2, purified from hybridoma cell culture

Synonyme(s) :

Anti-CMT2A, Anti-CMT2A2, Anti-CPRP1, Anti-HSG, Anti-Hyperplasia suppressor, Anti-KIAA0214, Anti-MARF, Anti-MFN2, Anti-Mitochondrial assembly regulatory factor, Anti-Transmembrane GTPase MFN2

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About This Item

Numéro MDL:
Code UNSPSC :
12352203
Nomenclature NACRES :
NA.41

Source biologique

mouse

Conjugué

unconjugated

Forme d'anticorps

purified from hybridoma cell culture

Type de produit anticorps

primary antibodies

Clone

Mito-2, monoclonal

Forme

buffered aqueous solution

Poids mol.

antigen ~86 kDa

Espèces réactives

mouse, rat

Concentration

~1.0 mg/mL

Technique(s)

western blot: 2-5 μg/mL using whole extract of rat brain mitochondria

Isotype

IgG1

Numéro d'accès UniProt

Conditions d'expédition

dry ice

Température de stockage

−20°C

Modification post-traductionnelle de la cible

unmodified

Informations sur le gène

human ... MFN2(9927)

Description générale

Mitofusin-2 (MFN2) is an outer mitochondrial membrane protein.
Monoclonal Anti-Mitofusin 2 (mouse IgG1 isotype) is derived from the hybridoma Mito-2 produced by the fusion of mouse myeloma cells and splenocytes from BALB/c mice immunized with a synthetic peptide corresponding to a fragment of human Mitofusin 2 conjugated to KLH. Mitofusin 2ismammalian homolog of the Drosophila protein fuzzy onion (Fzo). It is a transmembrane GTPases embedded in the outer membrane of mitochondria. Mitofusin 2 is broadly expressed, with highest expression in heart and skeletal muscle and is induced during myogenesis.

Application

Anti-Mitofusin 2 antibody,Mouse monoclonal has been used in western blotting.

Actions biochimiques/physiologiques

Mitofusin 2 (Mfn2) mutant embryos have a specific and severe disruption of a layer of the placenta. Repression of Mfn2 causes morphological and functional fragmentation of the mitochondrial network into independent clusters and reduces mitochondrial membrane potential and glucose oxidation. Thus, this Mfn2-dependent regulatory mechanism is disturbed in obesity by reduced Mfn2 expression. Mutations in Mitofusin 2 cause Charcot-Marie-Tooth neuropathy type 2A, a neurological disorder that results from degeneration of axons in peripheral nerves.
Mitofusin-2 (MFN2) plays an important role as a mitochondrial fusion protein and controls many cell processes. It is mainly involved in regulating metabolic processes in the mitochondria. MFN2 prevents the formation of reactive oxygen species and controls endoplasmic reticulum stress. Mutations in the gene encoding this protein have been linked to diabetes and obesity.

Forme physique

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

Clause de non-responsabilité

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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Consulter la Bibliothèque de documents

Short-duration swimming exercise after myocardial infarction attenuates cardiac dysfunction and regulates mitochondrial quality control in aged mice
Zhao D, et al.
Oxidative Medicine and Cellular Longevity, 2018 (2018)
Mutations in the mitochondrial GTPase mitofusin 2 cause Charcot-Marie-Tooth neuropathy type 2A
Zuchner S, et al.
Nature Genetics, 36(5), 449-449 (2004)
Mitofusin-2 determines mitochondrial network architecture and mitochondrial metabolism A novel regulatory mechanism altered in obesity
Bach D, et al.
The Journal of Biological Chemistry, 278(19), 17190-17197 (2003)
Membrane topology and mitochondrial targeting of mitofusins, ubiquitous mammalian homologs of the transmembrane GTPase Fzo
Rojo M, et al.
Journal of Cell Science, 115(8), 1663-1674 (2002)
The dynamics of cardiolipin synthesis post-mitochondrial fusion
Xu FY, et al.
Biochimica et Biophysica Acta - Biomembranes, 1798(8), 1577-1585 (2010)

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