This antibody is purified through a protein A column, followed by peptide affinity purification.
Immunogen
This ATP5F1 antibody is generated from rabbits immunized with a KLH conjugated synthetic peptide between 161-195 amino acids from the Central region of human ATP5F1.
ATP5F1
Reactivity: Human, Mouse, Rat
WB, ELISA, IHC, IF
Host: Rabbit
Polyclonal
unconjugated
Application Notes
WB: 1:1000
Restrictions
For Research Use only
Format
Liquid
Buffer
Purified polyclonal antibody supplied in PBS with 0.09 % (W/V) sodium azide.
Preservative
Sodium azide
Precaution of Use
This product contains Sodium azide: a POISONOUS AND HAZARDOUS SUBSTANCE which should be handled by trained staff only.
Storage
4 °C,-20 °C
Expiry Date
6 months
Burkard, Planyavsky, Kaupe, Breitwieser, Bürckstümmer, Bennett, Superti-Furga, Colinge: "Initial characterization of the human central proteome." in: BMC systems biology, Vol. 5, pp. 17, (2011) (PubMed).
Choudhary, Kumar, Gnad, Nielsen, Rehman, Walther, Olsen, Mann: "Lysine acetylation targets protein complexes and co-regulates major cellular functions." in: Science (New York, N.Y.), Vol. 325, Issue 5942, pp. 834-40, (2009) (PubMed).
Higuti, Tsurumi, Osaka, Kawamura, Tsujita, Yoshihara, Tani, Tanaka, Ichihara: "Molecular cloning of cDNA for the import precursor of human subunit B of H(+)-ATP synthase in mitochondria." in: Biochemical and biophysical research communications, Vol. 178, Issue 3, pp. 1014-20, (1991) (PubMed).
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.