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ATP5G2 Antibody (aa1-50)
Rabbit Polyclonal Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| IHC-P, E |
|---|---|
| Primary Accession | Q06055 |
| Reactivity | Human |
| Host | Rabbit |
| Clonality | Polyclonal |
| Calculated MW | 15kDa |
| Dilution | ELISA (1:40000), IHC-P (5 µg/ml), |
| Gene ID | 517 |
|---|---|
| Other Names | ATP synthase F(0) complex subunit C2, mitochondrial, ATP synthase lipid-binding protein, ATP synthase proteolipid P2, ATP synthase proton-transporting mitochondrial F(0) complex subunit C2, ATPase protein 9, ATPase subunit c, ATP5G2 |
| Target/Specificity | ATP5G2 Antibody detects endogenous levels of total ATP5G2 protein. |
| Reconstitution & Storage | Store at -20°C for up to one year. |
| Precautions | ATP5G2 Antibody (aa1-50) is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | ATP5MC2 (HGNC:842) |
|---|---|
| Function | 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. |
| Cellular Location | Mitochondrion membrane; Multi-pass membrane protein |
| Volume | 50 µl |
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Provided below are standard protocols that you may find useful for product applications.
Background
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.
References
Dyer M.R.,et al.Biochem. J. 293:51-64(1993).
Higuti T.,et al.Biochim. Biophys. Acta 1173:87-90(1993).
Otsuki T.,et al.DNA Res. 12:117-126(2005).
Scherer S.E.,et al.Nature 440:346-351(2006).
Farrell L.B.,et al.Biochem. Biophys. Res. Commun. 144:1257-1264(1987).
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