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Key Documents

MABS2047M

Sigma-Aldrich

Anti-MT-ND2 Antibody, clone 9E12-1B3

clone 9E12-1B3, from mouse

Sinónimos:

NADH-ubiquinone oxidoreductase chain 2, EC: 1.6.5.3, NADH dehydrogenase subunit 2, MT-ND2

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About This Item

UNSPSC Code:
12352203
eCl@ss:
32160702
NACRES:
NA.41

biological source

mouse

Quality Level

antibody form

purified antibody

antibody product type

primary antibodies

clone

9E12-1B3, monoclonal

species reactivity

human

packaging

antibody small pack of 25 μg

technique(s)

western blot: suitable

isotype

IgG2aκ

NCBI accession no.

UniProt accession no.

target post-translational modification

unmodified

Gene Information

human ... MT-ND2(4536)

General description

NADH-ubiquinone oxidoreductase chain 2 (UniProt: P03891; also known as EC: 1.6.5.3, NADH dehydrogenase subunit 2, MT-ND2) is encoded by the MT-ND2 (also known as MTND2, NADH2, ND2) gene (Gene ID: 4536) in human. MT-ND2 is a mitochondrial inner membrane protein that forms the core subunit of the mitochondrial membrane respiratory chain NADH dehydrogenase (Complex I). It is believed to belong to the minimal assembly required for catalysis. Complex I functions in the transfer of electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone (Coenzyme Q10) that participates in the generation of a proton gradient, which is then used for ATP synthesis. Defects in MT-ND2 gene are known to cause of Leber hereditary optic neuropathy (LHON) that is a maternally inherited disease resulting in acute or subacute loss of central vision, due to optic nerve dysfunction. LHON results from primary mitochondrial DNA mutations affecting the respiratory chain complexes.

Specificity

Clone 9E12-1B3 detects NADH-ubiquinone oxidoreductase chain 2 (MT-ND2) in mitochondria from human cells. It targets an epitope within the N-terminal region.

Immunogen

Epitope: N-terminus
Synthetic peptide corresponding to the N-terminus of human MT-ND2.

Application

Anti-MT-ND2, clone 9E12-1B3, Cat. No. MABS2047, is a mouse monoclonal antibody that detects NADH-ubiquinone oxidoreductase chain 2 and has been tested for use in Western Blotting.
Research Category
Signaling
Western Blotting Analysis: 2 µg/mL from a representative lot detected MT-ND2 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).

Quality

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 ug/mL of this antibody detected MT-ND2 in 10 µg of human neonatal dermal fibroblasts and mitochondria from human neonatal dermal fibroblasts depleted of mtDNA.

Target description

~30 kDa observed; 38.96 kDa calculated. Uncharacterized bands may be observed in some lysate(s).

Physical form

Format: Purified
Protein L
Purified mouse monoclonal antibody IgG2a in buffer containing HEPES-Buffered Saline (150 mM NaCl, 15 mM HEPES, pH 7.2) with 0.02% sodium azide.

Storage and Stability

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

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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Storage Class

12 - Non Combustible Liquids

wgk_germany

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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