Anti-ATP5E monoclonal antibody (DMABT-H13103)

Mouse anti-Human ATP5E monoclonal antibody for WB, IHC, ELISA Datasheet

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Host Species
Antibody Isotype
Species Reactivity
ATP5E (AAH01690,2a.a. ~ 51 a.a) full-length recombinant protein with GST tag. MW of the GST tag alone is 26 KDa.


Alternative Names
ATP5E; ATP synthase, H+ transporting, mitochondrialG2complex, epsilon subunit; ATP synthase subunit epsilon, mitochondrial; FF-ATPase; mitochondrial ATPase; H(+)-transporting two-sector ATPase
Entrez Gene ID
UniProt ID

Product Background

Gene summary
ATP5E (ATP Synthase, H+ Transporting, Mitochondrial F1 Complex, Epsilon Subunit) is a Protein Coding gene. Diseases associated with ATP5E include mitochondrial complex iii deficiency, nuclear type 5 and isolated atp synthase deficiency. 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 ATPase activity and proton-transporting ATPase activity, rotational mechanism. An important paralog of this gene is ATP5EP2. This gene encodes a subunit of mitochondrial ATP synthase. Mitochondrial ATP synthase catalyzes ATP synthesis, utilizing an electrochemical gradient of protons across the inner membrane during oxidative phosphorylation. ATP synthase is composed of two linked multi-subunit complexes: the soluble catalytic core, F1, and the membrane-spanning component, Fo, comprising the proton channel. The catalytic portion of mitochondrial ATP synthase consists of 5 different subunits (alpha, beta, gamma, delta, and epsilon) assembled with a stoichiometry of 3 alpha, 3 beta, and a single representative of the other 3. The proton channel consists of three main subunits (a, b, c). This gene encodes the epsilon subunit of the catalytic core. Two pseudogenes of this gene are located on chromosomes 4 and 13. Read-through transcripts that include exons from this gene are expressed from the upstream gene SLMO2.
Antigen Description
Mitochondrial complex V deficiency, nuclear 3 (MC5DN3) [MIM:614053]: A mitochondrial disorder with heterogeneous clinical manifestations including dysmorphic features, psychomotor retardation, hypotonia, growth retardation, cardiomyopathy, enlarged liver, hypoplastic kidneys and elevated lactate levels in urine, plasma and cerebrospinal fluid. Note=The disease is caused by mutations affecting the gene represented in this entry. ATP synthase subunit epsilon, mitochondrial is an enzyme that in humans is encoded by the ATP5E gene. Mitochondrial membrane ATP synthase (F1Fo ATP synthase or Complex V) produces ATP from ADP in the presence of a proton gradient across the membrane which is generated by electron transport complexes of the respiratory chain. F-type ATPases consist of two structural domains, F1 - containing the extramembraneous catalytic core, and Fo - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F1 is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F1 domain and of the central stalk which is part of the complex rotary element. Rotation of the central stalk against the surrounding alpha3beta3 subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits (By similarity).
Alzheimers disease, organism-specific biosystem; Alzheimers disease, conserved biosystem; Electron Transport Chain, organism-specific biosystem; F-type ATPase, eukaryotes, organism-specific biosystem; Formation of ATP by chemiosmotic coupling, organism-specific biosystem; Huntingtons disease, organism-specific biosystem; Huntingtons disease, conserved biosystem.


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Fillingame, RH; et al. Coupling H+ transport and ATP synthesis ln F1F0-ATP synthases: Glimpses of interacting parts in a dynamic molecular machine. JOURNAL OF EXPERIMENTAL BIOLOGY 200:217-224(1997).
Nakanishi-Matsui, M; Futai, M; et al. Stochastic rotational catalysis of proton pumping F-ATPase. PHILOSOPHICAL TRANSACTIONS OF THE ROYAL SOCIETY B-BIOLOGICAL SCIENCES 363:2135-2142(2008).

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