Synthetic peptide corresponding to Human ATP5G1. Carrier-protein conjugated synthetic peptide encompassing a sequence within the center region of human ATP5G1. The immunogen includes the transit peptide (aa 1-61). Database link: P05496
Molt-4 whole cell lysate and Raji cell lysate.
存放说明Shipped at 4°C. Upon delivery aliquot. Store at -20°C or -80°C. Avoid freeze / thaw cycle.
功能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. A homomeric c-ring of probably 10 subunits is part of the complex rotary element.
ATP synthase lipid-binding protein mitochondrial antibody
ATP synthase proteolipid P1 antibody
ATP synthase proton transporting mitochondrial F(0) complex subunit C1 antibody
ATP synthase proton-transporting mitochondrial F(0) complex subunit C1 antibody
ATPase protein 9 antibody
ATPase subunit 9 antibody
ATPase subunit c antibody
Mitochondrial ATP synthase subunit C isoform 1 antibody
Anti-ATP5G1 antibody 图像
Western blot - Anti-ATP5G1 antibody (ab96655)
Anti-ATP5G1 antibody (ab96655) at 1/1000 dilution + Molt-4 whole cell lysate at 30 µg
Predicted band size : 14 kDa 15% SDS PAGE
Anti-ATP5G1 antibody (ab96655)参考文献
This product has been referenced in:
Zhu G et al. Acute effect of lactic acid on tumor-endothelial cell metabolic coupling in the tumor microenvironment. Oncol Lett12:3478-3484 (2016).
Read more (PubMed: 27900024) »
Alavian KN et al. An uncoupling channel within the c-subunit ring of the F1FO ATP synthase is the mitochondrial permeability transition pore. Proc Natl Acad Sci U S A111:10580-5 (2014).
Read more (PubMed: 24979777) »