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ATP5B / ATP Synthase Beta Antibody
Rabbit Polyclonal Antibody
- SPECIFICATION
- CITATIONS
- PROTOCOLS
- BACKGROUND
Application 
| WB, IHC-P |
|---|---|
| Primary Accession | P06576 |
| Other Accession | 506 |
| Reactivity | Human, Mouse, Rat |
| Host | Rabbit |
| Clonality | Polyclonal |
| Isotype | IgG |
| Calculated MW | 56560 Da |
| Dilution | IHC-P (5 µg/ml), WB (1:500 - 1:2000), |
| Gene ID | 506 |
|---|---|
| Other Names | ATP5B, ATPMB, ATPSB, Beta-mtATPase, F0F1-ATP synthase beta subunit, ATP synthase beta subunit |
| Target/Specificity | Human ATP5B / ATP Synthase Beta. |
| Reconstitution & Storage | PBS, pH 7.3, 0.02% sodium azide, 50% glycerol. Long term: -80°C; Short term: -20°C. Avoid freeze-thaw cycles. |
| Precautions | ATP5B / ATP Synthase Beta Antibody is for research use only and not for use in diagnostic or therapeutic procedures. |
| Name | ATP5F1B (HGNC:830) |
|---|---|
| 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. Subunits alpha and beta form the catalytic core in F(1). 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. |
| Cellular Location | Mitochondrion inner membrane; Peripheral membrane protein {ECO:0000250|UniProtKB:P00829}; Matrix side {ECO:0000250|UniProtKB:P00829, ECO:0000269|PubMed:25168243} |
| Volume | 50 µl |
Thousands of laboratories across the world have published research that depended on the performance of antibodies from Abcepta to advance their research. Check out links to articles that cite our products in major peer-reviewed journals, organized by research category.
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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. Subunits alpha and beta form the catalytic core in F(1). 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
Neckelmann N.,et al.Genomics 5:829-843(1989).
Ohta S.,et al.J. Biol. Chem. 263:11257-11262(1988).
Ohta S.,et al.J. Biochem. 99:135-141(1986).
Ota T.,et al.Nat. Genet. 36:40-45(2004).
Mural R.J.,et al.Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
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