Datasheet

生物学的記述

Specificity	ATP synthase C Antibody [E17F23] detects endogenous levels of total ATP synthase C protein.
Background	ATP synthase C subunit (ATP5G1/2/3), also known as the proteolipid, is a key membrane protein forming the core of the Fo proton channel in mitochondrial F-type ATP synthase, also called Complex V, responsible for ATP production during oxidative phosphorylation. It's 75 amino acids fold into a hairpin structure with two transmembrane α-helices, assembling into an oligomeric c-ring typically composed of 8 to 15 identical subunits that rotate within the inner mitochondrial membrane. The conserved Asp61 residue in each subunit’s second helix acts as a proton binding site; protonation and deprotonation of Asp61 facilitate H+ translocation across the membrane, enabling rotary catalysis. The c-ring rotation drives the central stalk (γ subunit), inducing conformational changes in the F1 α3β3 catalytic domain, where ATP is synthesized from ADP and inorganic phosphate. The C subunit’s interaction with cardiolipin stabilizes the c-ring within the lipid bilayer. The C subunit can adopt amyloidogenic β-sheet conformations in unmodified states, which have implications in mitochondrial dysfunction. Mutations or abnormal accumulation of the c-ring disrupt proton flux and membrane integrity, leading to mitochondrial pathologies such as mitochondrial myopathies, ceroid lipofuscinoses (Batten disease), and neurodegenerative disorders. The rotary mechanism converts the proton motive force into mechanical energy, essential for cellular energy homeostasis in aerobic organisms.

Specificity

ATP synthase C Antibody [E17F23] detects endogenous levels of total ATP synthase C protein.

Background

ATP synthase C subunit (ATP5G1/2/3), also known as the proteolipid, is a key membrane protein forming the core of the Fo proton channel in mitochondrial F-type ATP synthase, also called Complex V, responsible for ATP production during oxidative phosphorylation. It's 75 amino acids fold into a hairpin structure with two transmembrane α-helices, assembling into an oligomeric c-ring typically composed of 8 to 15 identical subunits that rotate within the inner mitochondrial membrane. The conserved Asp61 residue in each subunit’s second helix acts as a proton binding site; protonation and deprotonation of Asp61 facilitate H+ translocation across the membrane, enabling rotary catalysis. The c-ring rotation drives the central stalk (γ subunit), inducing conformational changes in the F1 α3β3 catalytic domain, where ATP is synthesized from ADP and inorganic phosphate. The C subunit’s interaction with cardiolipin stabilizes the c-ring within the lipid bilayer. The C subunit can adopt amyloidogenic β-sheet conformations in unmodified states, which have implications in mitochondrial dysfunction. Mutations or abnormal accumulation of the c-ring disrupt proton flux and membrane integrity, leading to mitochondrial pathologies such as mitochondrial myopathies, ceroid lipofuscinoses (Batten disease), and neurodegenerative disorders. The rotary mechanism converts the proton motive force into mechanical energy, essential for cellular energy homeostasis in aerobic organisms.

使用情報

Application

WB, IF

Dilution

WB	IF
1:1000 - 1:2000	1:100

Reactivity

Human

Source

Rabbit Monoclonal Antibody

MW

14 kDa

Storage Buffer

PBS, pH 7.2+50% Glycerol+0.05% BSA+0.01% NaN3

Storage
(from the date of receipt)

-20°C (avoid freeze-thaw cycles), 2 years

プロトコール

References

https://pubmed.ncbi.nlm.nih.gov/22504883/
https://pubmed.ncbi.nlm.nih.gov/27439859/

ATP synthase C Antibody [E17F23]

生物学的記述

使用情報

References

Application Data