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ATP5D Antibody
Rabbit Polyclonal Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| IHC-P, E |
|---|---|
| Primary Accession | P30049 |
| Other Accession | 513 |
| Reactivity | Human |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | IgG |
| Calculated MW | 17490 Da |
| Dilution | IHC-P (10 µg/ml), |
| Gene ID | 513 |
|---|---|
| Other Names | ATP5D, F-ATPase delta subunit |
| Target/Specificity | Human ATP5D |
| Reconstitution & Storage | PBS, pH 7.4, 0.03% Proclin 300, 50% glycerol. Aliquot and store at -20°C or -80°C. Avoid freeze-thaw cycles. |
| Precautions | ATP5D Antibody is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | ATP5F1D (HGNC:837) |
|---|---|
| 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 (PubMed:29478781). 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 turnover 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(1) domain and of the central stalk which is part of the complex rotary element. Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits (PubMed:1531933). |
| Cellular Location | Mitochondrion. Mitochondrion inner membrane. |
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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 turnover 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(1) domain and of the central stalk which is part of the complex rotary element. Rotation of the central stalk against the surrounding alpha(3)beta(3) subunits leads to hydrolysis of ATP in three separate catalytic sites on the beta subunits.
References
Jordan E.M.,et al.Biochim. Biophys. Acta 1130:123-126(1992).
Halleck A.,et al.Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
Grimwood J.,et al.Nature 428:529-535(2004).
Mural R.J.,et al.Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
Hochstrasser D.F.,et al.Electrophoresis 13:992-1001(1992).
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