Ugrás a tartalomra
Merck

M6319

Sigma-Aldrich

Anti-Mitofusin-2 (N-Terminal) antibody produced in rabbit

affinity isolated antibody, buffered aqueous solution

Szinonimák:

Mitofusin 2 Antibody, Mitofusin 2 Antibody - Anti-Mitofusin-2 (N-Terminal) antibody produced in rabbit, Anti-CMT2A, Anti-CMT2A2, Anti-CPRP1, Anti-KIAA0214, Anti-MARF, Anti-Mfn2

Bejelentkezésa Szervezeti és Szerződéses árazás megtekintéséhez


About This Item

MDL-szám:
UNSPSC kód:
12352203
NACRES:
NA.41
konjugátum:
unconjugated
application:
IF
IP
WB CL
klón:
polyclonal
faj reaktivitás:
mouse, human, rat
citations:
49
technika/technikák:
immunoprecipitation (IP): 5-10 μg using HeLa human epitheloid carcinoma cell lysate
indirect immunofluorescence: 20-30 μg/mL using differentiated mouse C2 cells
western blot (chemiluminescent): 0.5-1 μg/mL using extracts of rat or mouse brain mitochondria

biológiai forrás

rabbit

Minőségi szint

konjugátum

unconjugated

antitest forma

affinity isolated antibody

antitest terméktípus

primary antibodies

klón

polyclonal

Forma

buffered aqueous solution

molekulatömeg

antigen ~86 kDa

faj reaktivitás

mouse, human, rat

technika/technikák

immunoprecipitation (IP): 5-10 μg using HeLa human epitheloid carcinoma cell lysate
indirect immunofluorescence: 20-30 μg/mL using differentiated mouse C2 cells
western blot (chemiluminescent): 0.5-1 μg/mL using extracts of rat or mouse brain mitochondria

UniProt elérési szám

kiszállítva

dry ice

tárolási hőmérséklet

−20°C

célzott transzláció utáni módosítás

unmodified

Géninformáció

human ... MFN2(9927)
mouse ... Mfn2(170731)
rat ... Mfn2(64476)

Általános leírás

Mitofusins (Mfn1 and Mfn2) are the mammalian homologs of the Drosophila protein fuzzy onion (Fzo). They are transmembrane GTPases embedded in the outer membrane of mitochondria, essential for fusion of mitochondria in mammalian cells. Mfn1 and Mfn2 form homotypic and heterotypic complexes that are functional for fusion. Mitochondrial fusion is also important for cell growth, mitochondrial membrane potential, respiration, and embryonic development. Mice deficient in either Mfn1 or Mfn2 die in mid-gestation. Mfn2 mutant embryos have a specific and severe disruption of a layer of the placenta. Mitofusin 2 is broadly expressed, with highest expression in heart and skeletal muscle and is induced during myogenesis. Repression of Mfn2 causes morphological and functional fragmentation of the mitochondrial network into independent clusters and reduces mitochondrial membrane potential and glucose oxidation. Thus, Mfn2 is essential for the maintenance of mitochondrial network and controls mitochondrial metabolism. 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.

Egyediség

Anti-Mitofusin 2 (N-terminal) antibody recognizes human, rat, and mouse mitofusin 2. Detection of the mitofusin 2 band by immunoblotting is specifically inhibited with the immunizing peptide.
The antibody is specific for N-terminal of mitofusin 2 (~86 kDa)

Immunogén

synthetic peptide corresponding to amino acid residues 38-55 of human mitofusin 2 with C-terminal added cysteine, conjugated to KLH. The corresponding sequence differs by one amino acid in both rat and mouse mitofusin 2.

Alkalmazás

Anti-Mitofusin 2 (N-terminal) antibody is suitable for immunoblotting (~86 kDa), immunoprecipitation, and immunofluorescence applications.
By immunoblotting, a working antibody concentration of 0.5-1 mg/mL is recommended using an extracts of rat and mouse brain mitochondria and a chemiluminescent detection reagent.
By indirect immunofluorescence, a working antibody concentration of 20-30 mg/mL is recommended using differentiated mouse C2 cells.
5-10 mg of the antibody immunoprecipitates mitofusin 2 from HeLa human epithelioid carcinoma cell lysate.
Anti-mitofusion 2 antibody may be used for immunoprecipitation in HeLa cells; immunoblotting in mouse and rat brain mitochondia and immunoflurescence in mouse C2 cells
Applications in which this antibody has been used successfully, and the associated peer-reviewed papers, are given below.
Western Blotting (1 paper)

Fizikai forma

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

Jogi nyilatkozat

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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Tárolási osztály kódja

12 - Non Combustible Liquids

WGK

WGK 1

Lobbanási pont (F)

Not applicable

Lobbanási pont (C)

Not applicable


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Analitikai tanúsítványok (COA)

Lot/Batch Number

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Dokumentumtár megtekintése

Mamta Rai et al.
Journal of cell science, 127(Pt 1), 191-203 (2013-11-08)
Mitochondrial biogenesis and morphological changes are associated with tissue-specific functional demand, but the factors and pathways that regulate these processes have not been completely identified. A lack of mitochondrial fusion has been implicated in various developmental and pathological defects. The
Short mitochondrial ARF triggers Parkin/PINK1-dependent mitophagy
Grenier K, et al.
The Journal of Biological Chemistry (2014)
Kensuke Tsushima et al.
Circulation research, 122(1), 58-73 (2017-11-03)
Cardiac lipotoxicity, characterized by increased uptake, oxidation, and accumulation of lipid intermediates, contributes to cardiac dysfunction in obesity and diabetes mellitus. However, mechanisms linking lipid overload and mitochondrial dysfunction are incompletely understood. To elucidate the mechanisms for mitochondrial adaptations to
Robert H Baloh et al.
The Journal of neuroscience : the official journal of the Society for Neuroscience, 27(2), 422-430 (2007-01-12)
Mutations in the mitochondrial fusion protein mitofusin 2 (MFN2) are the most commonly identified cause of Charcot-Marie-Tooth type 2 (CMT2), a dominantly inherited disease characterized by degeneration of peripheral sensory and motor axons. However, the mechanism by which mutations in
Jean-Philippe Leduc-Gaudet et al.
Physiological reports, 6(4) (2018-02-27)
Multiple aspects of mitochondrial function and dynamics remain poorly studied in the skeletal muscle of pediatric models in response to a short-term high-fat diet (HFD). This study investigated the impact of a short-term HFD on mitochondrial function and dynamics in

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