Anti-NDUFA10 monoclonal antibody (CAB-3995MH)

Mouse anti-Human NDUFA10 monoclonal antibody for ELISA, WB Datasheet

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Specifications


Host Species
Mouse
Antibody Isotype
IgG1
Clone
4C0-2B2
Species Reactivity
Human
Immunogen
NDUFA1 (AAH00266, 24 a.a~71 a.a) full length recombinant protein with GST tag. MW of the GST tag alone is 26 KDa.
Conjugate
Unconjugated

Applications


Application Notes
WB: 1:500-1000
*Suggested working dilutions are given as a guide only. It is recommended that the user titrates the product for use in their own experiment using appropriate negative and positive controls.

Target


Alternative Names
NDUFA10; NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, 10, 42kDa; NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, 10 (42kD); NADH dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 10, mitochondrial; CI 42k; complex I 42kDa subunit
Entrez Gene ID
UniProt ID

Product Background


Gene summary
NDUFA10 (NADH:Ubiquinone Oxidoreductase Subunit A10) is a Protein Coding gene. Diseases associated with NDUFA10 include leigh syndrome and leigh syndrome with leukodystrophy. Among its related pathways are Metabolism and Respiratory electron transport, ATP synthesis by chemiosmotic coupling, and heat production by uncoupling proteins. GO annotations related to this gene include NADH dehydrogenase (ubiquinone) activity and nucleoside kinase activity. The protein encoded by this gene is a component of 42 kDa complex I, the first enzyme complex in the electron transport chain of mitochondria. This protein has NADH dehydrogenase activity and oxidoreductase activity. It transfers electrons from NADH to the respiratory chain. A mutation in this gene was found in an individual with Leigh syndrome.
Antigen Description
The human NDUFA1 gene codes for an essential component of complex I of the respiratory chain, which transfers electrons from NADH to ubiquinone. It has been noted that the N-terminal hydrophobic domain has the potential to be folded into an alpha-helix spanning the inner mitochondrial membrane with a C-terminal hydrophilic domain interacting with globular subunits of complex I.The NDUFA10 protein is a subunit of NADH dehydrogenase (ubiquinone), which is located in the mitochondrial inner membrane and is the largest of the five complexes of the electron transport chain. Mutations in subunits of NADH dehydrogenase (ubiquinone), also known as Complex I, frequently lead to complex neurodegenerative diseases such as Leighs syndrome. Furthermore, reduced NDUFA10 expression levels due to FOXM1-directed hypermethylation are associated with human squamous cell carcinoma and may be related to other forms of cancer. The human NDUFA10 gene codes for a subunit of Complex I of the respiratory chain, which transfers electrons from NADH to ubiquinone. NADH binds to Complex I and transfers two electrons to the isoalloxazine ring of the flavin mononucleotide (FMN) prosthetic arm to form FMNH2. The electrons are transferred through a series of iron-sulfur (Fe-S) clusters in the prosthetic arm and finally to coenzyme Q10 (CoQ), which is reduced to ubiquinol (CoQH2). The flow of electrons changes the redox state of the protein, resulting in a conformational change and pK shift of the ionizable side chain, which pumps four hydrogen ions out of the mitochondrial matrix. The function about NDUFA10 antigen include ATP binding; NADH dehydrogenase (ubiquinone) activity; phosphotransferase activity, alcohol group as acceptor.
Pathway
Alzheimers disease, organism-specific biosystem; Alzheimers disease, conserved biosystem; Electron Transport Chain, organism-specific biosystem; Huntingtons disease, organism-specific biosystem; Huntingtons disease, conserved biosystem; Metabolic pathways, organism-specific biosystem; Metabolism, organism-specific biosystem.

Citations


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References


del Castillo, C; Morales, L; et al. Proteomic analysis of the nucleus accumbens of rats with different vulnerability to cocaine addiction. NEUROPHARMACOLOGY 57:41-48(2009).
Ji, BH; La, YJ; et al. A Comparative Proteomics Analysis of Rat Mitochondria from the Cerebral Cortex and Hippocampus in Response to Antipsychotic Medications. JOURNAL OF PROTEOME RESEARCH 8:3633-3641(2009).

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