|Immunocytochemistry (ICC)||1-2 µg/mL|
|Immunofluorescence (IF)||1-2 µg/mL|
|Western Blot (WB)||0.5 µg/mL|
|Immunohistochemistry (IHC)||See 2 publications below|
|Western Blot (WB)||See 30 publications below|
|Immunocytochemistry (ICC)||See 5 publications below|
|Immunofluorescence (IF)||See 1 publications below|
|Miscellaneous PubMed (MISC)||See 7 publications below|
|Immunohistochemistry (Paraffin) (IHC (P))||See 1 publications below|
|Species reactivity||Bovine, C. elegans, Human, Mouse, Non-human primate, Rat|
|Published species||C. elegans, Fruit fly, Human, Mouse, Rat|
|Host / Isotype||Mouse / IgG1, kappa|
|Immunogen||Human Heart Mitochondria.|
|Storage buffer||HEPES buffered saline|
|Contains||0.02% sodium azide|
|Storage conditions||4° C|
The antibody was produced in vitro using hybridomas grown in serum-free medium, and then purified by biochemical fractionation. Near homogeneity was judged by SDS-PAGE.
The epitope recognized by the anti-ATP synthase beta 3D5AB1 is in the region containing the active site of the beta-subunit and is centered approximately at amino acid residue 83. The complete amino acid sequence of the epitope is not known. See Chi SL, Wahl ML, Kenan DJ et al. (2007) Angiostatin-like activity of a monoclonal antibody to the catalytic subunit of F1F0 ATP synthase. Cancer Res 67:4716-4724.
Complex V, also called F1F0ATPase or ATP synthase, is responsible for ATP production in oxidative phosphorylation and can work in reverse as a proton pumping ATPase. This reaction is accomplished by a flux of protons across the membrane as a result of electron transfer. The enzyme was thought to be localized exclusively to mitochondria. However, it has recently been identified on the plasma membrane of several cell types including hepatocytes where it functions as the HDL receptor, on endothelial cells where it may act as the angiostatin receptor, and on the surface of cancer cells. The ATP synthase protein has two main sections: the F1 ATP-ase (soluble) and the F0 ATP-ase (membrane-embedded). The F1 section consists of the alpha, beta, gamma, delta, and epsilon subunits. While the F0 consists of a, b, and c subunits. ATP synthase is extremely conserved through evolution and can be found in plants, fungi, bacteria, and animals. The enzyme in mammals is composed of 17 subunits, five of which make up the easily detached F1. The remainder subunits are components of two stalk domains and the proton pumping F0 part of the machinery. Two of the subunits of the F0 part are encoded on mitochondrial DNA while the other subunits are nuclear encoded. Mutations in the mitochondrial-encoded subunits of ATP synthase (Complex V) cause OXPHOS disease.
For Research Use Only. Not for use in diagnostic procedures. Not for resale without express authorization.
Protein Aliases: ATP synthase subunit beta, mitochondrial; ATP synthase, H+ transporting mitochondrial F1 complex, alpha subunit; ATP synthase, H+ transporting mitochondrial F1 complex, beta subunit; ATPMB; ATPSB; epididymis secretory protein Li 271; F1-ATPase beta-subunit; MGC5231; mitochondrial ATP synthase beta subunit; mitochondrial ATP synthase, H+ transporting F1 complex beta subunit; mitochondrial ATP synthetase, beta subunit
Gene Aliases: ATP5B; ATPMB; ATPSB; BOS_5573; HEL-S-271
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