ATP synthase C Antibody [E17F23]

Catalog No.: F2223

Application: Reactivity: Human

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代表番号: 045-509-1970|電子メール：sales@selleck.co.jp

使用情報

Dilution
WB1:1000 - 1:2000 IF1:100

Application
WB, IF

Source
Rabbit Monoclonal Antibody

Reactivity
Human

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
^*なぜ予測分子量と実際の分子量が異なるのか？下記の原因により、実際の分子量が予測と異なる：タンパク質の翻訳後修飾（リン酸化/糖鎖付加），スプライシングバリアント，イソフォーム，相対的な電荷，ポリマー。

Datasheet & SDS

生物学的記述

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.

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
[1] Symersky J, et al. Nat Struct Mol Biol. 2012 Apr 15;19(5):485-91, S1. [2] Mehdipour AR, et al. Proc Natl Acad Sci U S A. 2016 Aug 2;113(31):8568-70.

PVDFメンブレン孔径参考表

Protein Size (kDa)	PVDF Transfer Membrane Pore Size (μm)
< 10	0.22
10-20	0.22
20-30	0.45
30-45	0.45
45-70	0.45
80-100	0.45
100-140	0.45
> 140	0.45

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Protein Size (kDa)	Separating Gel Percentage
4-40	20%
12-45	15%
10-70	12.5%
15-100	10%
25-100	8%
60-210	5%