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Merck
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MABS1995M

Anti-MT-ATP6 Antibody, clone 1G7-1G2

clone 1G7-1G2, from mouse

别名:

ATP synthase subunit a, F-ATPase protein 6

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关于此项目

UNSPSC Code:
12352203
NACRES:
NA.41
eCl@ss:
32160702
Conjugate:
unconjugated
Clone:
1G7-1G2, monoclonal
Application:
WB
Citations:
1
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biological source

mouse

conjugate

unconjugated

antibody form

purified immunoglobulin

antibody product type

primary antibodies

clone

1G7-1G2, monoclonal

species reactivity

human

packaging

antibody small pack of 25 μg

technique(s)

western blot: suitable

isotype

IgG2bκ

NCBI accession no.

UniProt accession no.

target post-translational modification

unmodified

Quality Level

Gene Information

human ... MT-ATP6(4508)

General description

ATP synthase subunit a (UniProt: P00846; also known as F-ATPase protein 6) is encoded by the MT-ATP6 (also known as ATP6, ATPASE6, MTATP6) gene (Gene ID: 4508) in human. F-ATPase Protein 6 is an inner mitochondrial membrane protein and is a component of Complex V, which produces ATP from ADP in the presence of proton gradient across the membrane. F-type ATPases have 2 components, CF1 - the catalytic core - and CF0- the membrane proton channel. The CF1 catalytic core contains five subunits: alpha3, beta3, gamma1, delta1, epsilon1 and CF0 has three main subunits known as a, b, and c. Together they form a rotary motor. During catalysis, ATP synthesis in the catalytic domain of F1 is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Defects in MT-ATP6 gene cause multiple mitochondrial diseases, such as Leber hereditary optic neuropathy (LHON), which is characterized by acute and subacute loss of central vision due to optic nerve dysfunction. Some defects also lead to mitochondrial complex V deficiency that leads to neuropathy, ataxia, and hypertrophic cardiomyopathy.
~20 kDa observed; 24.82 kDa calculated. Uncharacterized bands may be observed in some lysate(s).

Immunogen

A synthetic peptide corresponding to the N-terminus of human MT-ATP6.
Epitope: N-terminus

Application

Anti-MT-ATP6, clone 1G7-1G2, Cat. No. MABS1995, is a mouse monoclonal antibody that detects ATP synthase subunit a and has been tested for use in Western Blotting.
Research Category
Signaling
Western Blotting Analysis: 0.5 µg/mL from a representative lot detected MT-ATP6 in mitochondria from human neonatal dermal fibroblasts and mitochondria from human neonatal dermal fibroblasts depleted of mtDNA (Courtesy of Michael F. Marusich, Ph.D., mAbDx, Inc., Eugene, OR USA).

Biochem/physiol Actions

Clone 1G7-1G2 detects ATP synthase subunit a (MT-ATP6) in mitochondria isolated from human cells.

Physical form

Format: Purified
Protein L
Purified mouse monoclonal antibody IgG2b in HEPES-Buffered Saline (15 mM HEPES, 150 mM NaCl, pH 7.2) with 0.02% sodium azide.

Preparation Note

Stable for 1 year at 2-8°C from date of receipt.

Analysis Note

Evaluated by Western Blotting in Mitochondria from human neonatal dermal fibroblasts and mitochondria from human neonatal dermal fibroblasts depleted of mtDNA.

Western Blotting Analysis: 1 µg/mL of this antibody detected MT-ATP6 in Mitochondria from human neonatal dermal fibroblasts and mitochondria from human neonatal dermal fibroblasts depleted of mtDNA.

Other Notes

Concentration: Please refer to lot specific datasheet.

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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存储类别

12 - Non Combustible Liquids

wgk

WGK 1

flash_point_f

Not applicable

flash_point_c

Not applicable


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Li-Sheng Zhang et al.
Nature cell biology, 23(7), 684-691 (2021-07-14)
Members of the mammalian AlkB family are known to mediate nucleic acid demethylation1,2. ALKBH7, a mammalian AlkB homologue, localizes in mitochondria and affects metabolism3, but its function and mechanism of action are unknown. Here we report an approach to site-specifically

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