Home Primary Antibodies ATP synthase C Antibody [E17F23]

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ATP synthase C Antibody [E17F23]

Catalog No.: F2223

    Application: Reactivity:
    • F2223-wb
      Lane 1: HL-60

    Usage Information

    Dilution
    1:1000 - 1:2000
    1:100
    Application
    WB, IF
    Reactivity
    Human
    Source
    Rabbit Monoclonal Antibody
    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
    Predicted MW Observed MW
    14 kDa 8 kDa
    *Why do the predicted and actual molecular weights differ?
    The following reasons may explain differences between the predicted and actual protein molecular weight.

    Datasheet & SDS

    Biological Description

    Specificity
    ATP synthase C Antibody [E17F23] detects endogenous levels of total ATP synthase C protein.
    Clone
    E17F23
    Synonym(s)
    ATP5G1; ATP5MC1; ATP synthase lipid-binding protein; ATP synthase membrane subunit c locus 1; ATP synthase proteolipid P1; ATP synthase proton-transporting mitochondrial F(0) complex subunit C1; ATPase protein 9; ATPase subunit c
    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.
    References
    • https://pubmed.ncbi.nlm.nih.gov/22504883/
    • https://pubmed.ncbi.nlm.nih.gov/27439859/

    Tech Support

    Answers to questions you may have can be found in the inhibitor handling instructions. Topics include how to prepare stock solutions, how to store inhibitors, and issues that need special attention for cell-based assays and animal experiments.

    Handling Instructions

    Tel: +1-832-582-8158 Ext:3
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