Product Datasheet  
ATPG Antibody  
Catalog Number: 34449  
Technical:tech@swbio.com  
Information:info@swbio.com  
Description  
  • host_species:  
  • Rabbit
  • Amount:  
  • 100μgμg
  • Swiss-Prot No.:  
  • Swiss-Prot: P36542
    NCBI Gene ID: 509
  • Form of Antibody:  
  • Rabbit IgG in phosphate buffered saline (without Mg2+ and Ca2+), pH 7.4, 150mM NaCl, 0.02% sodium azide and 50% glycerol.
  • Storage:  
  • Store at -20˚C
  • Immunogen:  
  • Synthesized peptide derived from internal of human ATPG.
  • reactivity:  
  • Hu Ms Rt
  • appl_detail:  
  • Western blotting: 1:500~1:3000

  • other_names:  
  • ATP synthase gamma chain; mitochondrial precursor; ATP5C1; ATPG; EC 3.6.3.14
  • Purification:  
  • The antibody was affinity-purified from rabbit antiserum by affinity-chromatography using epitope-specific immunogen.
  • Specificity:  
  • The antibody detects endogenous levels of total ATPG protein.
  • Applications:  
  • WB
  • Background:  
  • Mitochondrial membrane ATP synthase (F1F0 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 F0 - 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 the central stalk which is part of the complex rotary element. The gamma subunit protrudes into the catalytic domain formed of alpha3beta3. Rotation of the central stalk against the surrounding alpha3beta3 subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.

    Matsuda C., J. Biol. Chem. 268:24950-24958(1993).
    Deloukas P., Nature 429:375-381(2004).
    The MGC Project Team; Genome Res. 14:2121-2127(2004).



 
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