Anti-ATP5H in Antibody Picoband® (monoclonal, 6B12) Fluoro647 Conjugated

ATP5H is also known as ATPQ. Mitochondrial ATP synthase catalyzes ATP synthesis, utilizing an electrochemical gradient of protons across the inner membrane during oxidative phosphorylation. It is composed of two linked multi-subunit complexes: the soluble catalytic core, F1, and the membrane-spanning component, Fo, which comprises the proton channel. The F1 complex consists of 5 different subunits (alpha, beta, gamma, delta, and epsilon) assembled in a ratio of 3 alpha, 3 beta, and a single representative of the other 3. The Fo seems to have nine subunits (a, b, c, d, e, f, g, F6 and 8) . This gene encodes the d subunit of the Fo complex. Alternatively spliced transcript variants encoding different isoforms have been identified for this gene. In addition, three pseudogenes are located on chromosomes 9, 12 and 15.

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E.coli-derived human ATP5H recombinant protein (Position: A2-L161) . Human ATP5H shares 81% and 78% amino acid (aa) sequence identity with mouse and rat ATP5H, respectively.

Mitochondrial membrane ATP synthase (F (1) F (0) 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, F (1) - containing the extramembraneous catalytic core, and F (0) - containing the membrane proton channel, linked together by a central stalk and a peripheral stalk. During catalysis, ATP synthesis in the catalytic domain of F (1) is coupled via a rotary mechanism of the central stalk subunits to proton translocation. Part of the complex F (0) domain and the peripheric stalk, which acts as a stator to hold the catalytic alpha (3) beta (3) subcomplex and subunit a/ATP6 static relative to the rotary elements.

1. Boada M, et al. ATP5H/KCTD2 locus is associated with Alzheimer's disease risk. Mol Psychiatry, 2014 Jun. 2. Kim DW, et al. Identification of mitochondrial F (1) F (0) -ATP synthase interacting with galectin-3 in colon cancer cells. Cancer Sci, 2008 Oct.